Composition and method for treating viral infection

Abstract

Methods for inhibiting virus propagation and treating virus infection are provided which include administering to cells infected with viruses a compound capable of inhibiting viral budding from the cells.

Description

FIELD OF THE INVENTION

[0002] The present invention generally relates to pharmaceuticals and methods of treating diseases, particularly to methods and pharmaceutical compositions for treating viral infections.

BACKGROUND OF THE INVENTION

[0003] Viruses are the smallest of parasites, and are completely dependent on the cells they infect for their reproduction. Viruses are composed of an outer coat of protein, which is sometimes surrounded by a lipid envelope, and an inner nucleic acid core consisting of either RNA or DNA. Generally, after docking with the plasma membrane of a susceptible cell, the viral core penetrates the cell membrane to initiate the viral infection. After infecting cells, viruses commandeer the cell's molecular machinery to direct their own replication and packaging. The “replicative phase” of the viral life cycle may begin immediately upon entry into the cell, or may occur after a period of dormancy or latency. After the infected cell synthesizes sufficient amounts of viral components, the “packaging phase” of the viral life cycle begins and new viral particles are assembled. Some viruses reproduce without killing their host cells, and many of these bud from host cell membranes. Other viruses cause their host cells to lyse or burst, releasing the newly assembled viral particles into the surrounding environment, where they can begin the next round of their infectious cycle. Several hundred different types of viruses are known to infect humans, however, since many of these have only recently been recognized, their clinical significance is not fully understood. Of these viruses that infect humans, many infect their hosts without producing overt symptoms, while others (e.g., influenza) produce a well-characterized set of symptoms. Importantly, although symptoms can vary with the virulence of the infecting strain, identical viral strains can have drastically different effects depending upon the health and immune response of the host. Despite remarkable achievements in the development of vaccines for certain viral infections (i.e., polio and measles), and the eradication of specific viruses from the human population (e.g., smallpox), viral diseases remain as important medical and public health problems. Indeed, viruses are responsible for several “emerging” (or reemerging) diseases (e.g., West Nile encephalitis & Dengue fever), and also for the largest pandemic in the history of mankind (HIV and AIDS).

[0004] Viruses that primarily infect humans are spread mainly via respiratory and enteric excretions. These viruses are found worldwide, but their spread is limited by inborn resistance, prior immunizing infections or vaccines, sanitary and other public health control measures, and prophylactic antiviral drugs. Zoonotic viruses pursue their biologic cycles chiefly in animals, and humans are secondary or accidental hosts. These viruses are limited to areas and environments able to support their nonhuman natural cycles of infection (vertebrates or arthropods or both). However, with increased global travel by humans, and the likely accidental co-transport of arthropod vectors bearing viral payloads, many zoonotic viruses are appearing in new areas and environments as emerging diseases. For example, West Nile virus, which is spread by the bite of an infected mosquito, and can infect people, horses, many types of birds, and other animals, was first isolated from a febrile adult woman in the West Nile District of Uganda in 1937. The virus made its first appearance in the Western Hemisphere, in the New York City area in the autumn of 1999, and during its first year in North America, caused the deaths of 7 people and the hospitalization of 62. At the time of this writing (August, 2002) the virus has been detected in birds in 37 states and the District of Columbia, and confirmed human infections have occurred in Alabama, the District of Columbia, Florida, Illinois, Indiana, Louisiana, Massachusetts, Mississippi, Missouri, New York City, Ohio, and Texas. (See: http://www.cdc.gov/od/oc/media/wncount.htm).

[0005] Additionally, some viruses are known to have oncogenic properties. Human T-cell lymphotropic virus type 1 (a retrovirus) is associated with human leukemia and lymphoma. Epstein-Barr virus has been associated with malignancies such as nasopharyngeal carcinoma, Burkitt's lymphoma, Hodgkin's disease, and lymphomas in immunosuppressed organ transplant recipients. Kaposi's sarcoma-associated virus is associated with Kaposi's sarcoma, primary effusion lymphomas, and Castleman's disease (a lymphoproliferative disorder).

[0006] Treatment of viral diseases presents unique challenges to modern medicine. Since viruses depend on host cells to provide many functions necessary for their multiplication, it is difficult to inhibit viral replication without at the same time affecting the host cell itself. Consequently, antiviral treatments are often directed at the functions of specific enzymes of particular viruses. However, such antiviral treatments that specifically target viral enzymes (e.g., HIV protease, or HIV reverse transcriptase) often have limited usefulness, because resistant strains of viruses readily arise through genetic drift and mutation.

SUMMARY OF THE INVENTION

[0007] The present invention provides a method for inhibiting viral budding from virus-infected cells and thus inhibiting viral propagation in the cells. The method can be useful in treating infection by viruses that utilize the Tsg101 protein of their host cells for viral budding within and/or out of the cells. In general, the method comprises administering to a patient in need of such treatment a composition comprising a peptide having an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R. Preferably, X1 is threonine (T) or serine (S), and X2 is alanine (A). Preferably the peptide is associated with a transporter that is capable of increasing the uptake of the peptide by a mammalian cell by at least 100%, preferably at least 300%.

[0008] Thus, the method can be used in treating infection by viruses such as HIV, Ebola virus, HBV, HSV1, HSV2, HSV5, EBV, Influenza A virus, HPV, HTLV-2, West Nile virus, Measles virus, Rubella virus, Colorado tick fever virus, foot-and-mouth disease virus, human foamy virus, hepatitis E virus, hepatitis G virus, human parechovirus 2, and Semliki forest virus. In a preferred embodiment, the method is used in treating HIV infection and AIDS, and/or preventing AIDS. When the method is used in treating HIV infection, preferably the peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

[0009] In preferred embodiments, the peptide in the composition is covalently linked to the transporter. Advantageously, the transporter is selected from the group consisting of penetratins, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof. Preferably, the transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof. Alternatively, the transporter can be non-peptidic molecules or structures such as liposomes, dendrimers, and siderophores.

[0010] In specific embodiments, the peptide in the composition includes a contiguous amino acid sequence of from 8 to about 100 residues, preferably from 8 to about 50 residues, more preferably from 9 to about 20 residues, of a viral protein selected from the group consisting of HIV GAG, Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein the contiguous amino acid sequence encompasses the P(T/S)AP motif of the viral protein. For example, the peptide used in the composition can include an amino acid sequence selected from the group consisting of SEQ ID NOs: 1-37, SEQ ID NOs: 38-125, SEQ ID NOs: 126-268, SEQ ID NOs: 269-554, SEQ ID NOs: 555-697, SEQ ID NOs: 698-749, SEQ ID NOs: 750-892, SEQ ID NOs: 893-1035, SEQ ID NOs: 1036-1178, SEQ ID NOs: 1179-1321, SEQ ID NOs: 1322-1464, SEQ ID NOs: 1465-1607, SEQ ID NOs: 1608-1750, SEQ ID NOs: 1751-1893, SEQ ID NOs: 1894-2036, SEQ ID NOs: 2037-2179, SEQ ID NOs: 2180-2322, SEQ ID NOs: 2323-2459, SEQ ID NOs: 2460-2602, SEQ ID NOs: 2603-2745, SEQ ID NOs: 2746-2887, SEQ ID NOs: 2888-3030, SEQ ID NOs: 3031-3173, SEQ ID NOs: 3174-3316, and SEQ ID NOs: 3317-3459.

[0011] In preferred embodiments, the transporter in the composition according to the method of the present invention is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, preferably at least 300%.

[0012] When the transporter used in the method of the present invention is a peptide, a hybrid polypeptide or fusion polypeptide is provided. The hybrid polypeptide includes (a) a first portion having an amino acid sequence motif PX1X2P capable of binding the UEV domain of Tsg101, wherein X1and X2 are amino acids, and X2 is not R, and (b) a second portion which is a peptidic transporter capable of increasing the uptake of the first portion by human cells. Advantageously, the transporter is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, preferably at least 300%. Preferably, the first portion consists of from 8 to 100, more preferably 8 to 50, even more preferably 9 to 20 amino acid residues. The hybrid polypeptide can be chemically synthesized or produced by recombinant expression. Thus, the present invention also provides isolated nucleic acids encoding the hybrid polypeptides, and host cells recombinantly expressing the hybrid polypeptides.

[0013] The peptide of the present invention can be administered to a patient in the presence or absence of a transporter. The peptide with or without a transporter can be administered directly to a patient in a pharmaceutical composition. Alternatively, the peptide or hybrid polypeptide according to the present invention can be introduced into a patient indirectly by administering to the patient a nucleic acid encoding the peptide or hybrid polypeptide.

[0014] Various modifications may be made to improve the stability and solubility of the peptides or hybrid polypeptides, and/or optimize its binding affinity to the UEV domain of Tsg101. In particular, various protection groups can be incorporated into the amino acid residues of the peptides or hybrid polypeptides. In addition, the compounds according to the present invention can also be in various pharmaceutically acceptable salt forms.

[0015] In another aspect of the present invention, methods of combination therapy for treating or preventing HIV and/or AIDS, and other viral infection are provided. In such methods, both a compound of the present invention (in the presence or absence of a transporter) and one or more other antiviral compounds are administered to a patient in need of treatment. Such other antiviral compounds should be pharmaceutically compatible with the compound of the present invention. Compounds suitable for use in combination therapies with the Tsg101-binding compounds according to the present invention include, but are not limited to, any small molecule drugs, antibodies, immunomodulators, and vaccines.

[0016] In accordance with another aspect of the present invention, isolated peptides are provided consisting of a contiguous amino acid sequence of from 8 to about 30 amino acid residues of a viral protein selected from the group consisting of HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, IPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, wherein the contiguous amino acid sequence encompasses the P(T/S)AP motif of the viral protein, and wherein the peptide is capable of binding the UEV domain of Tsg101. Preferably, the peptide does not contain a contiguous amino acid sequence of an HIV GAG protein or Ebola virus Matrix (EbVp40) protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on the peptide. In addition, the present invention also provides isolated nucleic acids encoding the isolated peptides.

[0017] In preferred embodiments, the isolated peptide consists of from 9 to about 20 amino acid residues. For example, such isolated peptides may include an amino acid sequence selected from the group consisting of SEQ ID NOs: 38-125, SEQ ID NOs: 126-286, SEQ ID NOs: 269-554, SEQ ID NOs: 555-697, SEQ ID NOs: 698-749, SEQ ID NOs: 750-892, SEQ ID NOs: 893-1035, SEQ ID NOs: 1036-1178, SEQ ID NOs: 1179-1321, SEQ ID NOs: 1322-1464, SEQ ID NOs: 1465-1607, SEQ ID NOs: 1608-1750, SEQ ID NOs: 1751-1893, SEQ ID NOs: 1894-2036, SEQ ID NOs: 2037-2179, SEQ ID NOs: 2180-2322, SEQ ID NOs: 2323-2459, SEQ ID NOs: 2460-2602, SEQ ID NOs: 2603-2745, SEQ ID NOs: 2888-3030, SEQ ID NOs: 3174-3316, and SEQ ID NOs: 3317-3459.

[0018] The foregoing and other advantages and features of the invention, and the manner in which the same are accomplished, will become more readily apparent upon consideration of the following detailed description of the invention taken in conjunction with the accompanying examples, which illustrate preferred and exemplary embodiments.

BRIEF DESCRIPTION OF THE DRAWINGS

[0019] FIG. 1 is a competitive inhibition curve showing that the p(1-14) peptide having the first 14 amino acid residues is capable of inhibiting protein-protein interaction between GST-p6 and myc-Tsg 101(1-207);

[0020] FIG. 2 is a Dixon plot showing p6(1-14) inhibition of the interaction between GST-p6 and myc-Tsg101(1-207);

[0021] FIG. 3 is another Dixon plot showing p6(1-14) inhibition of the interaction between GST-p6 and myc-Tsg101(1-207);

[0022] FIG. 4 is the graphical test results showing the effect of the compound MPI-PEP1 at various concentrations on HIV viral propagation in cell culture and on cell viability in the cell culture;

[0023] FIG. 5 is the graphical test results of the compound MPI-PEP2;

[0024] FIG. 6 is the graphical test results of the compound MPI-PEP3; and

[0025] FIG. 7 is the graphical test results of AZT as a positive control compound.

DETAILED DESCRIPTION OF THE INVENTION

[0026] As used herein, the term “viral infection” generally encompasses infection of an animal host, particularly a human host, by one or more viruses. Thus, treating viral infection will encompass the treatment of a person who is a carrier of one or more specific viruses or a person who is diagnosed of active symptoms caused by and/or associated with infection by the viruses. A carrier of virus may be identified by any methods known in the art. For example, a person can be identified as virus carrier on the basis that the person is antiviral antibody positive, or is virus-positive, or has symptoms of viral infection. That is, “treating viral infection” should be understood as treating a patient who is at any one of the several stages of viral infection progression. In addition, “treating or preventing viral infection” will also encompass treating suspected infection by a particular virus after suspected past exposure to virus by e.g., blood transfusion, exchange of body fluids, bites, accidental needle stick, or exposure to patient blood during surgery, or other contacts with a person with viral infection that may result in transmission of the virus.

[0027] Specifically, as used herein, the term “HIV infection” generally encompasses infection of a host animal, particularly a human host, by the human immunodeficiency virus (HIV) family of retroviruses including, but not limited to, HIV I, HIV II, HIV III (a.k.a. HTLV-III, LAV-1, LAV-2), and the like. “HIV” can be used herein to refer to any strains, forms, subtypes, clades and variations in the HIV family. Thus, treating HIV infection will encompass the treatment of a person who is a carrier of any of the HIV family of retroviruses or a person who is diagnosed of active AIDS, as well as the treatment or prophylaxis of the AIDS-related conditions in such persons. A carrier of HIV may be identified by any methods known in the art. For example, a person can be identified as HIV carrier on the basis that the person is anti-HIV antibody positive, or is HIV-positive, or has symptoms of AIDS. That is, “treating HIV infection” should be understood as treating a patient who is at any one of the several stages of HIV infection progression, which, for example, include acute primary infection syndrome (which can be asymptomatic or associated with an influenza-like illness with fevers, malaise, diarrhea and neurologic symptoms such as headache), asymptomatic infection (which is the long latent period with a gradual decline in the number of circulating CD4+ T cells), and AIDS (which is defined by more serious AIDS-defining illnesses and/or a decline in the circulating CD4 cell count to below a level that is compatible with effective immune function). In addition, “treating or preventing HIV infection” will also encompass treating suspected infection by HIV after suspected past exposure to HIV by e.g., contact with HIV-contaminated blood, blood transfusion, exchange of body fluids, “unsafe” sex with an infected person, accidental needle stick, receiving a tattoo or acupuncture with contaminated instruments, or transmission of the virus from a mother to a baby during pregnancy, delivery or shortly thereafter. The term “treating HIV infection” may also encompass treating a person who has not been diagnosed as having HIV infection but is believed to be at risk of infection by HIV.

[0028] The term “treating AIDS” means treating a patient who exhibits more serious AIDS-defining illnesses and/or a decline in the circulating CD4 cell count to below a level that is compatible with effective immune function. The term “treating AIDS” also encompasses treating AIDS-related conditions, which means disorders and diseases incidental to or associated with AIDS or HIV infection such as AIDS-related complex (ARC), progressive generalized lymphadenopathy (PGL), anti-HIV antibody positive conditions, and HIV-positive conditions, AIDS-related neurological conditions (such as dementia or tropical paraparesis), Kaposi's sarcoma, thrombocytopenia purpurea and associated opportunistic infections such as Pneumocystis carinii pneumonia, Mycobacterial tuberculosis, esophageal candidiasis, toxoplasmosis of the brain, CMV retinitis, HIV-related encephalopathy, HIV-related wasting syndrome, etc.

[0029] Thus, the term “preventing AIDS” as used herein means preventing in a patient who has HIV infection or is suspected to have HIV infection or is at risk of HIV infection from developing AIDS (which is characterized by more serious AIDS-defining illnesses and/or a decline in the circulating CD4 cell count to below a level that is compatible with effective immune function) and/or AIDS-related conditions.

[0030] The terms “polypeptide,” “protein,” and “peptide” are used herein interchangeably to refer to amino acid chains in which the amino acid residues are linked by peptide bonds or modified peptide bonds. The amino acid chains can be of any length of greater than two amino acids. Unless otherwise specified, the terms “polypeptide,” “protein,” and “peptide” also encompass various modified forms thereof. Such modified forms may be naturally occurring modified forms or chemically modified forms. Examples of modified forms include, but are not limited to, glycosylated forms, phosphorylated forms, myristoylated forms, palmitoylated forms, ribosylated forms, acetylated forms, etc. Modified forms also encompass pharmaceutically acceptable salt forms. In addition, modifications also include intra-molecular crosslinking and covalent attachment to various moieties such as lipids, flavin, biotin, polyethylene glycol or derivatives thereof, etc. In addition, modifications may also include cyclization, and branching. Further, amino acids other than the conventional twenty amino acids encoded by genes may also be included in a polypeptide.

[0031] As used herein, the term “Tsg101” means human Tsg101 protein, unless otherwise specified.

[0032] As disclosed in commonly assigned co-pending applications, mature HIV-1NYU/BR5 p6 (gag polyprotein amino acids 449-500) was used as a bait in a yeast two-hybrid system to screen a prey library derived from human spleen cDNA. A gene encoding the tumor suppressor TSG 101 protein (Tsg101; aa 7-390) was isolated as an interactor. The p6 bait used here contains a late domain motif (-PTAP-).

[0033] In addition, different p6 point mutants (E6G, P7L, A9R, or P10L) were generated and tested for their ability to bind Tsg101 protein. While the wild-type p6 peptide and the E6G p6 mutant were capable of binding Tsg101 protein, each of the P7L, A9R, and P10L point mutations abolishes the p6 binding affinity to Tsg101. The P7L, A9R, and P10L point mutations alter the PTAP motif in p6 peptide. The same mutations in the PTAP motif of the HIV p6 gag protein prevent HIV particles from budding from the host cells. See Huang et al., J. Virol., 69:6810-6818 (1995).

[0034] As is known in the art, the P(T/S)AP motif is conserved among the p6gag domains of all known primate lentiviruses. In nonprimate lentiviruses, which lack a p6gag domain, the P(T/S)AP motif is at the immediate C terminus of the Gag polyprotein. It has been shown that the P(T/S)AP motif is required for efficient pinching off of the lentivirus bud from the host cell surface. It is critical for lentivirus' particularly HIV virus' particle production. See Huang et al., J. Virol., 69:6810-6818 (1995). Specifically, deletion of the motif (PTAP−) results in drastic reduction of lentiviral particle production. In addition, the PTAP-deficient HIV proceeded through the typical stages of morphogenesis but failed to complete the process. Rather, they remain tethered to the plasma membrane and thus rendered non-infectious. That is, the lentiviral budding process is stalled. See Huang et al., J. Virol., 69:6810-6818 (1995).

[0035] Also as disclosed in commonly assigned co-pending applications, it has been found that Tsg101 binds directly to the P(T/S)AP domain of HIV-1 p6. The Tsg101 prey fragment isolated in yeast two-hybrid assay contains the ubiquitin E2 variant (UEV) domain indicating that the UEV domain is involved in the binding to the P(T/S)AP domain. This is consistent with the fact that ubiquitin is required from retrovirus budding and that proteasome inhibition reduces the level of free ubiquitin in HIV-1-infected cells and interferes with the release and maturation of HIV-1 and HIV-2. See Patnaik et al., Proc. Natl. Acad. Sci. USA, 97(24):13069-74 (2000); Schubert et al., Proc. Natl. Acad. Sci. USA, 97(24):13057-62 (2000); Strack et al., Proc. Natl. Acad. Sci. USA, 97(24):13063-8 (2000).

[0036] Tsg101 plays an important role in vacuolar protein sorting (Vps). The Vps pathway sorts membrane-bound proteins for eventual degradation in the lysosome (vacuole in yeast). See Lemmon and Traub, Curr. Opin. Cell. Biol., 12:457-66 (2000). Two alternative entrees into the Vps pathway are via vesicular trafficking from the Golgi (e.g., in degrading misfolded membrane proteins) or via endocytosis from the plasma membrane (e.g., in downregulating surface proteins like epidermal growth factor receptor (EGFR)). Vesicles carrying proteins from either source can enter the Vps pathway by fusing with endosomes. As these endosomes mature, their cargos are sorted for lysosomal degradation via the formation of structures called multivesicular bodies (MVB). MVB are created when surface patches on late endosomes bud into the compartment, forming small (˜50-100 nm) vesicles. A maturing MVB can contain tens or even hundreds of these vesicles. The MVB then fuses with the lysosome, releasing the vesicles for degradation in this hydrolytic organelle. Tsg101 appears to perform important roles in the Vps pathway. For example, deletion of the yeast Tsg101 ortholog (Vps23/Stp22) gives rise to a class E Vps phenotype, blocks vacuolar protein sorting from the golgi, and inhibits surface receptor downregulation. See Babst et al, Traffic, 1:248-258 (2000); Li et al., Mol. Cell Biol., 19:3588-3599 (1999). Mammalian Tsg101 similarly participates in endosomal trafficking. For example, efficient down-regulation of activated EGFR requires Tsg101 function. See Babst et al, Traffic, 1:248-258 (2000); Bishop and Woodman, J. Biol. Chem., 276:11735 (2001).

[0037] It is known that short chains of Ub (1-3 molecules) can “mark” surface receptors for endocytosis and degradation in the lysosome. Hicke, Trends Cell Biol., 9:107-112 (1999); Rotin et al., J. Membr. Biol., 176:1-17 (2000). There is also growing evidence that Ub conjugation (and hydrolysis) plays important roles in targeting proteins into the Vps pathway. See Dupre and Haguenauer-Tsapis, Mol. Cell Biol., 12:421-435 (2001); Losko et al., Mol. Cell Biol., 12:1047-1059 (2001). Several classes of proteins that carry the P(T/S)AP motif are surface receptors known to be degraded via the Vps pathway or function in the Vps pathway. Such proteins include connexins 43 and 45, hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs, a homolog of yeast Vps27p), and secretory carrier membrane protein-3 (Scamp-3). See Farr et al., Biochem. J., 345(3):503-509 (2000); Staub and Rotin., Structure, 4:495-499 (1996); Chin et al., J. Biol. Chem., 276:7069-78 (2001); Komada and Kitamura, Biochem. Biophys. Res. Commun., 281:1065-9 (2001). A plausible role for Tsg101 in this process is to recognize ubiquitinated proteins that carry P(T/S)AP motifs and help coordinate their incorporation into vesicles that bud into the MVB.

[0038] Interestingly, it has been noted that the topologies of viral budding and multivesicular body (MVB) formation are similar. In particular, both processes involve the membrane invaginating away from (rather than into) the cytoplasm. Indeed, these two processes are the only known examples in which cell buds a vesicle out of the cytoplasm, suggesting that viral budding and MVB formation may employ analogous mechanisms.

[0039] In addition, the recruitment of cellular machinery to facilitate virus budding appears to be a general phenomenon, and distinct late domains have been identified in the structural proteins of several other enveloped viruses. See Vogt, Proc. Natl. Acad. Sci. USA, 97:12945-12947 (2000). Two well characterized late domains are the “PY” motif (consensus sequence: PPXY; X=any amino acid) found in membrane-associated proteins from certain enveloped viruses. See Craven et al., J. Virol., 73:3359-3365 (1999); Harty et al., Proc. Natl. Acad. Sci. USA, 97:13871-13876 (2000); Harty et al., J. Virol., 73:2921-2929 (1999); and Jayakar et al., J. Virol., 74:9818-9827 (2000). The cellular target for the PY motif is Nedd4 which also contains a Hect ubiquitin E3 ligase domain. The “YL” motif (YXXL) was found in the Gag protein of equine infectious anemia virus (EIAV). Puffer et al., J. Virol., 71:6541-6546 (1997); Puffer et al., J. Virol., 72:10218-10221 (1998). The cellular receptor for the “YL” motif appears to be the AP-50 subunit of AP-2. Puffer et al., J. Virol., 72:10218-10221 (1998). Interestingly, the late domains such as the P(T/S)AP motif, PY motif and the YL motif can still function when moved to different positions within retroviral Gag proteins, which suggests that they are docking sites for cellular factors rather than structural elements. Parent et al., J. Virol., 69:5455-5460 (1995); Yuan et al., EMBO J., 18:4700-4710 (2000). Moreover, the late domains such as the P(T/S)AP motif, PY motif and the YL motif can function interchangeably. That is one late domain motif can be used in place of another late domain motif without affecting viral budding. Parent et al., J. Virol., 69:5455-5460 (1995); Yuan et al., EMBO J., 18:4700-4710 (2000); Strack et al., Proc. Natl. Acad. Sci. USA, 97:13063-13068 (2000).

[0040] Accordingly, while not wishing to be bound by any theory, it is believed that although the three late domain motifs bind to different cellular targets, they utilize common cellular pathways to effect viral budding. In particular, it is believed that the different cellular receptors for viral late domain motifs feed into common downstream steps of the vacuolar protein sorting (VPS) and MVB pathway. As discussed above, Tsg101 functions in the VPS pathway. Another protein, Vps4 functions in Tsg101 cycling and endosomal trafficking. Particularly, Vps4 mutants prevent normal Tsg101 trafficking and induce formation of aberrant, highly vacuolated endosomes that are defective in the sorting and recycling of endocytosed substrates. See Babst et al, Traffic, 1:248-258 (2000); Bishop and Woodman, J. Biol. Chem., 276:11735 (2001).

[0041] While not wishing to be bound by any theory, it is believed that the binding of the P(T/S)AP motif in viral proteins to Tsg101 enables viruses having the P(T/S)AP motif to usurp cellular machinery normally used for MVB formation to allow viral budding from the plasma membrane. It is also believed that Tsg101 serves as the common docking site for all viruses that utilize the P(T/S)AP motif to bud off host cell cytoplasm membrane. In addition, depletion of Tsg101 or interference with the interaction between Tsg101 and the P(T/S)AP motif in virus-infected cells would prevent viral budding from the cells. Moreover, an examination of HIV-1 amino acid sequence variants in GenBank using BLAST (Basic Local Alignment Search Tool) identified a number of HIV strains with the standard P(T/S)AP motif being replaced with variations of the P(T/S)AP motif, indicating that such variations may also enable viral budding and that peptides with such variations may also bind Tsg101. Such identified variations include PIAP (SEQ ID NO: 3) (see Zhang et al., J. Virol., 71:6662-6670 (1997); Farrar et al., J. Med. Virol., 34:104-113 (1991)), and PTTP (SEQ ID NO: 4) (see Zhang et al., J. Virol., 71:6662-6670 (1997).

[0042] In accordance with the present invention, a number of proteins of non-HIV viruses have been found to also contain the P(T/S)AP motif. The proteins are summarized in Table 1 below. The amino acid sequences of such proteins are provided under SEQ ID NOs: 3460-3484.

TABLE 1
Viral Proteins Containing the P(T/S)AP Motif
	P(T/S)AP-Containing	GenBank
Virus	Protein	Accession No.
Ebola Virus	Matrix Protein	AAL25816
HIV	GAG	AF324493
Hepatitis B Virus	PreS1/PreS2/S Envelope	BAA85340
Human Herpesvirus1	RL2	NP_044601
Human Herpesvirus 2	Virion Glycoprotein K	NP_044524
Human Herpesvirus 2	Glycoprotein I	P06764
Strain 333
Human Herpesvirus	BYRF1, Encodes EBNA-2	NP_039845
4/Epstein Barr Virus
Influenza A Virus	Hemagglutinin	AAG38554
(A/Pintail
Duck/Alberta/114/79
(H8N4))
Human Papillomavirus	L1 Protein, My09/My11	AAA67231
	Region
Human Papillomavirus	Minor Capsid Protein L2	NP_043365
Type 23
Human Papillomavirus	Major Capsid Protein L1	P27232
Type 35
Human Papillomavirus	Minor Capsid Protein L2	NP_040303
Type 6b
Human Papillomavirus	Late Protein	NP_041865
Type 9
Human T-Cell	Gag Protein	CAA61543
Lymphotropic Virus
Type 2
West Nile Virus	Polyprotein Precursor	NP_041724
Measles Virus	Matrix Protein	CAA34587
Rubella Virus	Non-Structural Protein	BAB32473
Colorado Tick Fever	VP12	AAB02025
Virus
Foot-and-Mouth	VP1 Capsid Protein	AAA42637
Disease Virus
Human Foamy Virus	Gag	NP_044279
Hepatitis E Virus	ORF-3	AAC35758
Hepatitis G Virus	Polyprotein Precursor	AAB65834
Human Herpesvirus 5	UL32	AAG31644
Human Parechovirus 2	Polyprotein	NP_046804
Semliki Forest Virus	Polyprotein	CAA76683

[0043] Thus, the inventors of the present invention propose to employ peptides derived from such viral proteins to treat viral infection including HIV infection as well as infection by other viruses listed in the above Table 1.

[0044] In accordance with a first aspect of the present invention, a method is provided for inhibiting virus budding from virus-infected cells and thus inhibiting viral propagation in the cells. The method includes administering to the cells a compound comprising an amino acid sequence motif of PX1X2P and capable of binding the UEV domain of Tsg101, wherein X1is any amino acid or amino acid analog and X2 is an amino acid or amino acid analog other than arginine (R). The compounds can be administered to cells in vitro or cells in vivo in a human or animal body. In the case of in vivo applications of the method, viral infection can be treated and alleviated by using the compound to inhibit viral propagation.

[0045] Preferably, the method is used for inhibiting viral budding of a virus that utilizes the Tsg101 protein of their host cells for viral budding within and/or out of the cells. The method is therefore useful in inhibiting viral propagation. In one embodiment, the method is used for inhibiting viral budding by an animal virus selected from the group consisting of HIV, hepatitis B virus, hepatitis E virus, hepatitis G virus, human papillomavirus, human herpes virus 1 (HSV1), human herpes virus 1 (HSV2), human herpes virus 5 (HSV5), Measles virus, Rubella virus, West Nile virus, human foamy virus, human parechovirus, Colorado tick fever virus, human T-cell lymphotropic virus, influenza A virus, foot-and-mouth disease virus, Ebola virus, and Semliki Forest virus.

[0046] In a preferred embodiments, the method is applied to inhibit viral budding by HIV, hepatitis B virus, HSV1 and HSV2. By inhibiting viral propagation in cells in a patient, the viral load in the patient body can be prevented from increasing and can even be decreased. Accordingly, the method of the present invention can also be used in treating viral infection as well as symptoms caused by and/or associated with the viral infection. In addition, when applied at an early stage before a patient develops a full-blown disease caused by viral infection, the method can be used to prevent such a disease by inhibiting viral propagation and decreasing the viral load in the patient. For example, human hepatitis B virus is known to cause hepatitis which may increase the risk of liver cancer. Thus, if the compounds of the present invention is applied to a patient at an early stage of the hepatitis B viral infection before the full development of hepatitis, hepatitis may be prevented and the likelihood of liver cancer in the patient may be reduced. Similarly, human papillomaviruses are believed to cause cervical cancer. Thus, by treating human papillomavirus infection, the risk of cervical cancer can be reduced.

[0047] The compound which comprises the amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101 can be of any type of chemical compounds so long as the compound is capable of binding the UTEV domain of Tsg011. In the case of viruses such foot-and-mouth disease virus which infects animals such as canine and cattles, the compounds to be administered to the animals should be capable of binding the Tsg101 orthologs in the animals. For example, the compound can be a peptide, a modified peptide, an oligonucleotide-peptide hybrid (e.g., PNA), etc. In a preferred embodiment, the compound administered is capable of binding the UEV domain of human Tsg101.

[0048] In one embodiment, in the compound comprising an amino acid sequence motif PX1X2P and capable of binding the UEV domain of Tsg101, X1is selected from the group consisting of threonine (T), serine (S), and isoleucine (I) and analogs thereof, and X2 is not R. In another embodiment, the X2 in the motif is alanine (A) or threonine (T) or an analog thereof. In a more preferred embodiment, the compound administered has the amino acid sequence motif of PX1X2P, wherein X1is selected from the group consisting of T, S, and I and analogs thereof, and X2 is A or T or an analog thereof.

[0049] Thus, the compound can be a tetrapeptide having an amino acid sequence of PX1X2P, wherein X2 is an amino acid or an amino acid analog other than arginine. In one embodiment, the tetrapeptide has an amino acid sequence of P(T/S/I)(A/T)P (SEQ ID NOs: 1-6). In a preferred embodiment, the tetrapeptide has the sequence of PTAP (SEQ ID NO: 1). In another preferred embodiment, the tetrapeptide has the sequence of PSAP (SEQ ID NO. 2).

[0050] The compound can also include a longer peptide comprising the amino acid sequence motif of PX1X2P and capable of binding the UEV domain of Tsg101. Advantageously, the compound is a peptide that contains an amino acid sequence of less than about 400, 375, 350, 325, 300, 275, 250, 225 or 200 residues. Preferably, the peptide contains an amino acid sequence of less than about 175, 150, 125, 115, 100, 95, 90, 85, 80, 75, 70, 65, 60 or 55 residues. More preferably, the peptide contains an amino acid sequence of less than about 50, 48, 45, 42, 40, 38, 35, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21 or 20 residues. In preferred embodiments, the peptide contains an amino acid sequence of from about 4 to about 200, 6 to about 150, 8 to about 100, preferably from about 8 to about 50, more preferably from about 9 to about 50, from about 9 to 45, 9 to 40, 9 to 37, 9 to 35, 9 to 30, 9 to 25 residues. More advantageously, the peptide contains an amino acid sequence of from 9 to about 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 residues, even more advantageously, from 10 to about 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 residues. Preferably, the PX1X2P motif in the sequence is the P(T/S)AP motif.

[0051] In a preferred embodiment, the compound includes a peptide that contains a contiguous amino acid sequence of an HIV GAG protein and is capable of binding the UEV domain of Tsg101. The contiguous amino acid sequence encompasses the late domain motif of the GAG protein, which can be the P(T/S/I)(A/T)P motif or a variant thereof.

[0052] In specific embodiments, the compound includes an amino acid sequence selected from the group of EPTAP (SEQ ID NO: 7), EPSAP (SEQ ID NO: 8), PTAPP (SEQ ID NO: 9), PSAPP (SEQ ID NO: 10), EPTAPP (SEQ ID NO: 11), EPSAPP (SEQ ID NO: 12), PEPTAP(SEQ ID NO: 13), PEPSAP (SEQ ID NO: 14), RPEPTAP (SEQ ID NO: 15), RPEPSAP (SEQ ID NO: 16), PEPTAPP (SEQ ID NO: 17), PEPSAPP (SEQ ID NO: 18), EPTAPPEE (SEQ ID NO: 19), EPSAPPEE (SEQ ID NO: 20), EPTAPPAE (SEQ ID NO: 21), PEPTAPPEE (SEQ ID NO: 22), PEPTAPPAE (SEQ ID NO: 23), PEPSAPPEE (SEQ ID NO: 24), PGPTAPPEE (SEQ ID NO: 25), PGPTAPPAE (SEQ ID NO: 26), PGPSAPPEE (SEQ ID NO: 27), RPEPTAPPEE (SEQ ID NO: 28), RPEPSAPPEE (SEQ ID NO: 29), RPEPTAPPAE (SEQ ID NO: 30), RPEPSAPPAE (SEQ ID NO: 31), RPGPTAPPEE (SEQ ID NO: 32), RPGPSAPPEE (SEQ ID NO: 33), RPGPTAPPAE (SEQ ID NO: 34), RPGPSAPPAE (SEQ ID NO: 35) LQSRPEPTAPPEE (SEQ ID NO: 36), LQSRPEPSAPPEE (SEQ ID NO: 37).

[0053] In another embodiment, the compound includes a contiguous amino acid sequence of a viral protein selected from the group consisting of Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein the contiguous amino acid sequence encompasses the P(T/S)AP motif of the viral protein.

[0054] In a specific embodiment, the compound includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein that encompasses the P(T/S)AP motif of the protein.

[0055] Advantageously, the compound is a peptide that contains a contiguous amino acid sequence of less than about 400, 375, 350, 325, 300, 275, 250, 225 or 200 residues of one of the viral proteins in Table 1, which encompasses the P(T/S)AP motif of the viral protein, and is capable of binding the UEV domain of Tsg101. Preferably, the peptide contains a contiguous amino acid sequence of less than about 175, 150, 125, 115, 100, 95, 90, 85, 80, 75, 70, 65, 60 or 55 residues of one of the viral proteins in Table 1, which encompasses the P(T/S)AP motif of the viral protein, and is capable of binding the UEV domain of Tsg101. More preferably, the peptide contains a contiguous amino acid sequence of less than about 50, 48, 45, 42, 40, 38, 35, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21 or 20 residues of one of the viral proteins in Table 1, which encompasses the P(T/S)AP motif of the viral protein, and is capable of binding the UEV domain of Tsg101. In preferred embodiments, the peptide contains a contiguous amino acid sequence of from about 4 to about 50, preferably from about 6 to about 50, from about 8 to about 50, more preferably from about 9 to about 50, from about 9 to 45, 9 to 40, 9 to 37, 9 to 35, 9 to 30, 9 to 25 residues of one of the viral proteins in Table 1, which encompasses the P(T/S)AP motif of the viral protein, and is capable of binding the UEV domain of Tsg101. More advantageously, the peptide contains a contiguous amino acid sequence of from 9 to about 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 residues of a viral protein in Table 1, even more advantageously, from 10 to about 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 residues of one of the viral proteins in Table 1, which encompasses the P(T/S)AP motif of the viral protein, and is capable of binding the UEV domain of Tsg101.

[0056] In specific embodiment, the peptide has a contiguous amino acid sequence of Ebola virus Matrix protein as provided in SEQ ID NOs: 38-125 in Table 2. In another specific embodiment, the peptide has a contiguous amino acid sequence of HBV PreS1/PreS2/S Envelope protein as provided in SEQ ID NOs: 126-268 in Table 3. In another specific embodiment, the peptide has a contiguous amino acid sequence of HSV1 RL2 protein as provided in SEQ ID NOs: 269-554 in Table 4. In yet another specific embodiment, the peptide has a contiguous amino acid sequence of HSV2 viron glycoprotein K as provided in SEQ ID NOs: 555-697 in Table 5. The peptide can also has a contiguous amino acid sequence of HSV2 Strain 333 glycoprotein I as provided in SEQ ID NOs: 698-749 in Table 6. The peptide can also has a contiguous amino acid sequence of EBV nuclear protein EBNA2 as provided in SEQ ID NOs: 750-892 in Table 7, of Influenza A virus hemagglutinin as provided in SEQ ID NOs: 893-1035 in Table 8, of HPV L1 protein (My09/My11 Region) as provided in SEQ ID NOs: 1036-1178 in Table 9, of HPV Type 23 L2 proteins as provided in SEQ ID NOs: 1179-1321 in Table 10, of HPV Type 35 L1 protein as provided in SEQ ID NOs: 1322-1464 in Table 11, of HPV Type 6b L2 protein as provided in SEQ ID NOs: 1465-1607 in Table 12, of HPV Type 9 late protein as provided in SEQ ID NOs: 1608-1750 in Table 13, of HTLV-2 GAG protein as provided in SEQ ID NOs: 1751-1893 in Table 14, of West Nile virus polyprotein precursor as provided in SEQ ID NOs: 1894-2036 in Table 15, of Measles virus matrix protein as provided in SEQ ID NOs: 2037-2179 in Table 16, of Rubella virus non-structural protein as provided in SEQ ID NOs: 2180-2322 in Table 17, of Colorado tick fever virus VP12 as provided in SEQ ID NOs: 2323-2459 in Table 18, of foot-and-mouth disease virus VP1 capsid protein as provided in SEQ ID NOs: 2460-2602 in Table 19, of human foamy virus GAG protein as provided in SEQ ID NOs: 2603-2745 in Table 20, of hepatitis E virus ORF-3 protein as provided in SEQ ID NOs: 2746-2887 in Table 21, of hepatitis G virus polyprotein precursor as provided in SEQ ID NOs: 2888-3030 in Table 22, of HSV5 UL32 protein as provided in SEQ ID NOs: 3031-3173 in Table 23, of human parechovirus 2 polyprotein as provided in SEQ ID NOs: 3174-3316 in Table 24, and of Semliki forest virus polyprotein as provided in SEQ ID NOs: 3317-3459 in Table 25.

[0057] In another embodiment, the PX1X2P motif in the compound according to the present invention is within an amino acid sequence that is at least 70 percent, preferably at least 80 percent or 85 percent, more preferably at least 90 percent or 95 percent identical to a contiguous span of at least 6, 7, 8 or 9 amino acids, preferably 10, 11, 12, 13, 14, 15 or more amino acids of one of the proteins in Table 1, which spans the late P(T/S)AP motif of the protein. In other embodiments, the PX1X2P motif in the compound according to the present invention is within an amino acid sequence that is at least 70 percent, preferably at least 80 percent or 85 percent, more preferably at least 90 percent or 95 percent identical to a contiguous span of at least 6, 7, 8 or 9 amino acids, preferably 10, 11, 12, 13, 14, 15 or more amino acids of a naturally occuring HIV Gag p6 protein or Ebola virus Matrix protein, which spans the late domain motif P(T/S)AP of the protein. In this respect, the percentage identity is determined by the algorithm of Karlin and Altschul, Proc. Natl. Acad. Sci. USA, 90:5873-77 (1993), which is incorporated into the various BLAST programs. Specifically, the percentage identity is determined by the “BLAST 2 Sequences” tool, which is available at http://www.ncbi.nlm.nih.gov/gorf/bl2.html. See Tatusova and Madden, FEMS Microbiol. Lett., 174(2):247-50 (1999). For pairwise protein-protein sequence comparison, the BLASTP 2.1.2 program is employed using default parameters (Matrix: BLOSUM62; gap open: 11; gap extension: 1; x13 dropoff: 15; expect: 10.0; and wordsize: 3, with filter). It should be understood that such homologue peptides should retain the ability to bind the UEV domain of Tsg101. Preferably, in such embodiments of the present invention, X1in the PX1X2P motif is selected from the group consisting of T, S, and I and analog thereof, and X2 is not R. More preferably, X1is selected from the group consisting of T, S, and I and analog thereof, and X2 is A or T or an analog thereof. Most preferably, X1is T or S or an analog thereof, and X2 is A or an analog thereof.

[0058] The homologues can be made by site-directed mutagenesis based on a late domain motif-containing Gag polyprotein sequence of HIV or Ebola matrix protein, or a protein in Table 1. The site-directed mutagenesis can be designed to generate amino acid substitutions, insertions, or deletions. Methods for conducting such mutagenesis should be apparent to skilled artisans in the field of molecular biology. The resultant homologues can be tested for their binding affinity to the UEV domain of Tsg101.

[0059] The peptide portion in the compounds according to the present invention can also be in a modified form. Various modifications may be made to improve the stability and solubility of the compound, and/or optimize its binding affinity to the UEV domain of Tsg101. Examples of modified forms include, but are not limited to, glycosylated forms, phosphorylated forms, myristoylated forms, palmitoylated forms, ribosylated forms, acetylated forms, etc. Modifications also include intra-molecular crosslinking and covalent attachment to various moieties such as lipids, flavin, biotin, polyethylene glycol or derivatives thereof, etc. In addition, modifications may also include cyclization, and branching. Amino acids other than the conventional twenty amino acids encoded by genes may also be included in a polypeptide sequence in the compound of the present invention. For example, the compounds may include D-amino acids in place of L-amino acids.

[0060] To increase the stability of the compounds according to the present invention, various protection groups can also be incorporated into the amino acid residues of the compounds. In particular, terminal residues are preferably protected. Carboxyl groups may be protected by esters (e.g., methyl, ethyl, benzyl, p-nitrobenzyl, t-butyl or t-amyl esters, etc.), lower alkoxyl groups (e.g., methoxy, ethoxy, propoxy, butoxy, etc.), aralkyloxy groups (e.g., benzyloxy, etc.), amino groups, lower alkylamino or di(lower alkyl)amino groups. The term “lower alkoxy” is intended to mean an alkoxy group having a straight, branched or cyclic hydrocarbon moiety of up to six carbon atoms. Protection groups for amino groups may include lower alkyl, benzyloxycarbonyl, t-butoxycarbonyl, and sobornyloxycarbonyl. “Lower alkyl” is intended to mean an alkyl group having a straight, branched or cyclic hydrocarbon moiety of up to six carbon atoms. In one example, a 5-oxo-L-prolyl residue may be used in place of a prolyl residue. A 5-oxo-L-prolyl residue is especially desirable at the N-terminus of a peptide compound. In another example, when a proline residue is at the C-terminus of a peptide compound, a N-ethyl-L-prolinamide residue may be desirable in place of the proline residue. Various other protection groups known in the art useful in increasing the stability of peptide compounds can also be employed.

[0061] In addition, the compounds according to the present invention can also be in various pharmaceutically acceptable salt forms. “Pharmaceutically acceptable salts” refers to the relatively non-toxic, organic or inorganic salts of the compounds of the present invention, including inorganic or organic acid addition salts of the compound. Examples of such salts include, but are not limited to, hydrochloride salts, hydrobromide salts, sulfate salts, bisulfate salts, nitrate salts, acetate salts, phosphate salts, nitrate salts, oxalate salts, valerate salts, oleate salts, borate salts, benzoate salts, laurate saltes, stearate salts, palmitate salts, lactate salts, tosylate salts, citrate salts, maleate, salts, succinate salts, tartrate salts, naththylate salts, fumarate salts, mesylate salts, laurylsuphonate salts, glucoheptonate salts, and the like. See, e.g., Berge, et al. J. Pharm. Sci., 66:1-19 (1977).

[0062] Suitable pharmaceutically acceptable salts also include, but are not limited to, alkali metal salts, alkaline earth salts, and ammonium salts. Thus, suitable salts may be salts of aluminum, calcium, lithium, magnesium, potassium, sodium and zinc. In addition, organic salts may also be used including, e.g., salts of lysine, N,N′-dibenzylethylenediamine, chloroprocaine, choline, diethanolamine, ethylenediamine, meglumine (N-methylglucamine), procaine and tris. In addition, metal complex forms (e.g. copper complex compounds, zinc complex compounds, etc.) of the compounds of the present invention may also exhibit improved stability.

[0063] Additionally, as will be apparent to skilled artisans apprised of the present disclosure, peptide mimetics can be designed based on the above-described compounds according to the present invention. However, it is noted that the mimetics must be capable of binding the UEV domain of Tsg101. For example, peptoid analogs of the P(T/S)(A/T)P motif can be prepared using known methods. Peptoids are oligomeric N-substituted glycines. Typically, various side chain groups can be included when forming an N-substituted glycine (peptoid monomer) that mimics a particular amino acid. Peptoid monomers can be linked together to form an oligomeric N-substituted glycines—peptoid. Peptoids are easy to synthesize in large amounts. In contrast to peptides, the backbone linkage of peptoids are resistant to hydrolytic enzymes. In addition, since a variety of functional groups can be presented as side chains off of the oligomeric backbone, peptoid analogs corresponding to any peptides can be produced with improved characterics. See Simon et al., Proc. Natl. Acad. Sci. USA, 89:9367-9371 (1992); Figliozzi et al., Methods Enzymol., 267:437-447 (1996); Horwell, Trends Biotechnol., 13:132-134 (1995); and Horwell, Drug Des. Discov., 12:63-75 (1994), all of which are incorporated herein by reference.

[0064] Thus, peptoid analogs of the above-described compounds of the present invention can be made using methods known in the art. The thus prepared peptoid analogs can be tested for their binding affinity to Tsg101. They can also be tested in anti-viral assays for their ability to inhibit virus budding from infected host cells and ability to inhibit virus propagation.

[0065] Mimetics of the compounds of the present invention can also be selected by rational drug design and/or virtual screening. Methods known in the art for rational drug design can be used in the present invention. See, e.g., Hodgson et al., Bio/Technology, 9:19-21 (1991); U.S. Pat. Nos. 5,800,998 and 5,891,628, all of which are incorporated herein by reference. An example of rational drug design is the development of HIV protease inhibitors. See Erickson et al., Science, 249:527-533 (1990). Structural information on the UEV domain of Tsg101 and/or the binding complex formed by the Tsg101 UEV domain and the HIV Gag p6 P(T/S)AP motif or a protein in Table 1 are obtained. The interacting complex can be studied using various biophysics techniques including, e.g., X-ray crystallography, NMR, computer modeling, mass spectrometry, and the like. Likewise, structural information can also be obtained from protein complexes formed by the Tsg101 UEV domain and a variation of the PTAP motif.

[0066] Computer programs are employed to select compounds based on structural models of the binding complex formed by the Tsg101 UEV domain and the HIV Gag p6P(T/S)AP motif or the P(T/S)AP motif in one of the proteins in Table 1. In addition, once an effective compound is identified, structural analogs or mimetics thereof can be produced based on rational drug design with the aim of improving drug efficacy and stability, and reducing side effects.

[0067] In addition, understanding of the interaction between the Tsg101 UEV domain and compounds of the present invention can also be derived from mutagenesis analysis using yeast two-hybrid system or other methods for detection protein-protein interaction. In this respect, various mutations can be introduced into the interacting proteins and the effect of the mutations on protein-protein interaction is examined by a suitable method such as in vitro binding assay or the yeast two-hybrid system.

[0068] Various mutations including amino acid substitutions, deletions and insertions can be introduced into the protein sequence of the Tsg101 UEV domain and/or a compound of the present invention using conventional recombinant DNA technologies. Generally, it is particularly desirable to decipher the protein binding sites. Thus, it is important that the mutations introduced only affect protein-protein interaction and cause minimal structural disturbances. Mutations are preferably designed based on knowledge of the three-dimensional structure of the interacting proteins. Preferably, mutations are introduced to alter charged amino acids or hydrophobic amino acids exposed on the surface of the proteins, since ionic interactions and hydrophobic interactions are often involved in protein-protein interactions. Alternatively, the “alanine scanning mutagenesis” technique is used. See Wells, et al., Methods Enzymol., 202:301-306 (1991); Bass et al., Proc. Natl. Acad. Sci. USA, 88:4498-4502 (1991); Bennet et al., J. Biol. Chem., 266:5191-5201 (1991); Diamond et al., J. Virol., 68:863-876 (1994). Using this technique, charged or hydrophobic amino acid residues of the interacting proteins are replaced by alanine, and the effect on the interaction between the proteins is analyzed using e.g., an in vitro binding assay. In this manner, the domains or residues of the proteins important to compound-target interaction can be identified.

[0069] Based on the structural information obtained, structural relationships between the Tsg101 UEV domain and a compound of the present invention are elucidated. The moieties and the three-dimensional structures critical to the interaction are revealed. Medicinal chemists can then design analog compounds having similar moieties and structures.

[0070] The residues or domains critical to the modulating effect of the identified compound constitute the active region of the compound known as its “pharmacophore.” Once the pharmacophore has been elucidated, a structural model can be established by a modeling process that may incorporate data from NMR analysis, X-ray diffraction data, alanine scanning, spectroscopic techniques and the like. Various techniques including computational analysis, similarity mapping and the like can all be used in this modeling process. See e.g., Perry et al., in OSAR: Quantitative Structure-Activity Relationships in Drug Design, pp.189-193, Alan R. Liss, Inc., 1989; Rotivinen et al., Acta Pharinaceutical Fennica, 97:159-166 (1988); Lewis et al., Proc. R. Soc. Lond., 236:125-140 (1989); McKinaly et al., Annu. Rev. Pharmacol. Toxiciol., 29:111-122 (1989). Commercial molecular modeling systems available from Polygen Corporation, Waltham, Mass., include the CHARMm program, which performs the energy minimization and molecular dynamics functions, and QUANTA program which performs the construction, graphic modeling and analysis of molecular structure. Such programs allow interactive construction, visualization and modification of molecules. Other computer modeling programs are also available from BioDesign, Inc. (Pasadena, Calif.), Hypercube, Inc. (Cambridge, Ontario), and Allelix, Inc. (Mississauga, Ontario, Canada).

[0071] A template can be formed based on the established model. Various compounds can then be designed by linking various chemical groups or moieties to the template. Various moieties of the template can also be replaced. These rationally designed compounds are further tested. In this manner, pharmacologically acceptable and stable compounds with improved efficacy and reduced side effect can be developed. The compounds identified in accordance with the present invention can be incorporated into a pharmaceutical formulation suitable for administration to an individual.

[0072] The mimetics including peptoid analogs can exhibit optimal binding affinity to the UEV domain of human Tsg101 or animal orthologs thereof. Various known methods can be utilized to test the Tsg101-binding characteristics of a mimetics. For example, the entire Tsg101 protein or a fragment thereof containing the UEV domain may be recombinantly expressed, purified, and contacted with the mimetics to be tested. Binding can be determined using a surface plasmon resonance biosensor. See e.g., Panayotou et al., Mol. Cell. Biol., 13:3567-3576 (1993). Other methods known in the art for estimating and determining binding constants in protein-protein interactions can also be employed. See Phizicky and Fields, et al., Microbiol. Rev., 59:94-123 (1995). For example, protein affinity chromatography may be used. First, columns are prepared with different concentrations of an interacting member, which is covalently bound to the columns. Then a preparation of its interacting partner is run through the column and washed with buffer. The interacting partner bound to the interacting member linked to the column is then eluted. Binding constant is then estimated based on the concentrations of the bound protein and the eluted protein. Alternatively, the method of sedimentation through gradients monitors the rate of sedimentation of a mixture of proteins through gradients of glycerol or sucrose. At concentrations above the binding constant, the two interacting members sediment as a complex. Thus, binding constant can be calculated based on the concentrations. Other suitable methods known in the art for estimating binding constant include but are not limited to gel filtration column such as nonequilibrium “small-zone” gel filtration columns (See e.g., Gill et al., J. Mol. Biol., 220:307-324 (1991)), the Hummel-Dreyer method of equilibrium gel filtration (See e.g., Hummel and Dreyer, Biochim. Biophys. Acta, 63:530-532 (1962)) and large-zone equilibrium gel filtration (See e.g., Gilbert and Kellett, J. Biol. Chem., 246:6079-6086 (1971)), sedimentation equilibrium (See e.g., Rivas and Minton, Trends Biochem., 18:284-287 (1993)), fluorescence methods such as fluorescence spectrum (See e.g., Otto-Bruc et al, Biochemistry, 32:8632-8645 (1993)) and fluorescence polarization or anisotropy with tagged molecules (See e.g., Weiel and Hershey, Biochemistry, 20:5859-5865 (1981)), and solution equilibrium measured with immobilized binding protein (See e.g., Nelson and Long, Biochemistry, 30:2384-2390 (1991)).

[0073] The compounds capable of binding Tsg101 UEV domain according the present invention can be delivered into cells by direct cell internalization, receptor mediated endocytosis, or via a “transporter.” It is noted that the compound administered to cells in vitro or in vivo in the method of the present invention preferably is delivered into the cells in order to achieve optimal results. Thus, preferably, the compound to be delivered is associated with a transporter capable of increasing the uptake of the compound by an animal cell, preferably a mammalian cell, susceptible to infection by a virus, particularly a virus selected from those in Table 1. As used herein, the term “associated with” means a compound to be delivered is physically associated with a transporter. The compound and the transporter can be covalently linked together, or associated with each other as a result of physical affinities such as forces caused by electrical charge differences, hydrophobicity, hydrogen bonds, van der Waals force, ionic force, or a combination thereof. For example, the compound can be encapsulated within a transporter such as a liposome.

[0074] As used herein, the term “transporter” refers to an entity (e.g., a compound or a composition or a physical structure formed from multiple copies of a compound or multiple different compounds) that is capable of facilitating the uptake of a compound of the present invention by a mammalian cell, particularly a human cell. Typically, the cell uptake of a compound of the present invention in the presence of a “transporter” is at least 50% or 75% higher, preferably at least 100% or 200% higher, and more preferably at least 300%, 400% or 500% higher than the cell uptake of the compound in the absence of the “transporter.” Methods of assaying cell uptake of a compound should be apparent to skilled artisans. For example, the compound to be delivered can be labeled with a radioactive isotope or another detectable marker (e.g., a fluorescence marker), and added to cultured cells in the presence or absence of a transporter, and incubated for a time period sufficient to allow maximal uptake. Cells can then be separated from the culture medium and the detectable signal (e.g., radioactivity) caused by the compound inside the cells can be measured. The result obtained in the presence of a transporter can be compared to that obtained in the absence of a transporter.

[0075] Many molecules and structures known in the art can be used as “transporter.” In one embodiment, a penetratin is used as a transporter. For example, the homeodomain of Antennapedia, a Drosophila transcription factor, can be used as a transporter to deliver a compound of the present invention. Indeed, any suitable member of the penetratin class of peptides can be used to carry a compound of the present invention into cells. Penetratins are disclosed in, e.g., Derossi et al., Trends Cell Biol., 8:84-87 (1998), which is incorporated herein by reference. Penetratins transport molecules attached thereto across cytoplasm membranes or nucleus membranes efficiently in a receptor-independent, energy-independent, and cell type-independent manner. Methods for using a penetratin as a carrier to deliver oligonucleotides and polypeptides are also disclosed in U.S. Pat. No. 6,080,724; Pooga et al., Nat. Biotech., 16:857 (1998); and Schutze et al., J. Immunol., 157:650 (1996), all of which are incorporated herein by reference. U.S. Pat. No. 6,080,724 defines the minimal requirements for a penetratin peptide as a peptide of 16 amino acids with 6 to 10 of which being hydrophobic. The amino acid at position 6 counting from either the N- or C-terminal is tryptophan, while the amino acids at positions 3 and 5 counting from either the N- or C-terminal are not both valine. Preferably, the helix 3 of the homeodomain of Drosophila Antennapedia is used as a transporter. More preferably, a peptide having a sequence of the amino acids 43-58 of the homeodomain Antp is employed as a transporter. In addition, other naturally occurring homologs of the helix 3 of the homeodomain of Drosophila Antennapedia can also be used. For example, homeodomains of Fushi-tarazu and Engrailed have been shown to be capable of transporting peptides into cells. See Han et al., Mol. Cells, 10:728-32 (2000). As used herein, the term “penetratin” also encompasses peptoid analogs of the penetratin peptides. Typically, the penetratin peptides and peptoid analogs thereof are covalently linked to a compound to be delivered into cells thus increasing the cellular uptake of the compound.

[0076] In another embodiment, the HIV-1 tat protein or a derivative thereof is used as a “transporter” covalently linked to a compound according to the present invention. The use of HIV-1 tat protein and derivatives thereof to deliver macromolecules into cells has been known in the art. See Green and Loewenstein, Cell, 55:1179 (1988); Frankel and Pabo, Cell, 55:1189 (1988); Vives et al., J. Biol. Chem., 272:16010-16017 (1997); Schwarze et al., Science, 285:1569-1572 (1999). It is known that the sequence responsible for cellular uptake consists of the highly basic region, amino acid residues 49-57. See e.g., Vives et al., J. Biol. Chem., 272:16010-16017 (1997); Wender et al., Proc. Nat'l Acad. Sci. USA, 97:13003-13008 (2000). The basic domain is believed to target the lipid bilayer component of cell membranes. It causes a covalently linked protein or nucleic acid to cross cell membrane rapidly in a cell type-independent manner. Proteins ranging in size from 15 to 120 kD have been delivered with this technology into a variety of cell types both in vitro and in vivo. See Schwarze et al., Science, 285:1569-1572 (1999). Any HIV tat-derived peptides or peptoid analogs thereof capable of transporting macromolecules such as peptides can be used for purposes of the present invention. For example, any native tat peptides having the highly basic region, amino acid residues 49-57 can be used as a transporter by covalently linking it to the compound to be delivered. In addition, various analogs of the tat peptide of amino acid residues 49-57 can also be useful transporters for purposes of this invention. Examples of various such analogs are disclosed in Wender et al., Proc. Nat'l Acad. Sci. USA, 97:13003-13008 (2000) (which is incorporated herein by reference) including, e.g., d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57 (i.e., l-Tat57-49 and d-Tat57-49), L-arginine oligomers, arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, and various homologues, derivatives (e.g., modified forms with conjugates linked to the small peptides) and peptoid analogs thereof. As used herein, the term “oligomer” means a molecule that includes a covalently linked chain of amino acid residues of the same amino acids having a large enough number of such amino acid residues to confer transporter activities on the molecule. Typically, an oligomer contains at least 6, preferably at least 7, 8, or at least 9 such amino acid residues. In one embodiment, the transporter is a peptide that includes at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

[0077] Other useful transporters known in the art include, but are not limited to, short peptide sequences derived from fibroblast growth factor (See Lin et al., J. Biol. Chem., 270:14255-14258 (1998)), Galparan (See Pooga et al., FASEB J. 12:67-77 (1998)), and HSV-1 structural protein VP22 (See Elliott and O'Hare, Cell, 88:223-233 (1997)).

[0078] As the above-described various transporters are generally peptides, fusion proteins can be conveniently made by recombinant expression to contain a transporter peptide covalently linked by a peptide bond to a peptide having the PX1X2P motif. Alternatively, conventional methods can be used to chemically synthesize a transporter peptide or a peptide of the present invention or both.

[0079] In addition to peptide-based transporters, various other types of transporters can also be used, including but not limited to cationic liposomes (see Rui et al., J. Am. Chem. Soc., 120:11213-11218 (1998)), dendrimers (Kono et al., Bioconjugate Chem., 10:1115-1121 (1999)), siderophores (Ghosh et al., Chem. Biol., 3:1011-1019 (1996)), etc. In a specific embodiment, the compound according to the present invention is encapsulated into liposomes for delivery into cells.

[0080] Additionally, when a compound according to the present invention is a peptide, it can be administered to cells by a gene therapy method. That is, a nucleic acid encoding the peptide can be administered to in vitro cells or to cells in vivo in a human or animal body. Various gene therapy methods are well known in the art. Successes in gene therapy have been reported recently. See e.g., Kay et al., Nature Genet., 24:257-61 (2000); Cavazzana-Calvo et al., Science, 288:669 (2000); and Blaese et al., Science, 270:475 (1995); Kantoff, et al., J. Exp. Med., 166:219 (1987).

[0081] In one embodiment, the peptide consists of a contiguous amino acid sequence of from 8 to about 30 amino acid residues of a viral protein selected from the group consisting of HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, wherein the contiguous amino acid sequence encompasses the P(T/S)AP motif of the viral protein, and wherein the peptide is capable of binding the UEV domain of Tsg101. In specific embodiments, the peptide does not contain a contiguous amino acid sequence of an HIV GAG protein, or of an Ebola virus Matrix (EbVp40) protein, or of a polyprotein precursor, or of hepatitis E virus ORF-3 protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

[0082] Advantageously, the isolated peptide consists of from 9 to about 20 amino acid residues. Examples of such isolated peptides include peptides having an amino acid sequence selected from the group consisting of SEQ ID NOs: 38-125, SEQ ID NOs: 126-268, SEQ ID NOs: 269-554, SEQ ID NOs: 555-697, SEQ ID NOs: 698-749, SEQ ID NOs: 750-892, SEQ ID NOs: 893-1035, SEQ ID NOs: 1036-1178, SEQ ID NOs: 1179-1321, SEQ ID NOs: 1322-1464, SEQ ID NOs: 1465-1607, SEQ ID NOs: 1608-1750, SEQ ID NOs: 1751-1893, SEQ ID NOs: 1894-2036, SEQ ID NOs: 2037-2179, SEQ ID NOs: 2180-2322, SEQ ID NOs: 2323-2459, SEQ ID NOs: 2460-2602, SEQ ID NOs: 2603-2745, SEQ ID NOs: 2888-3030, SEQ ID NOs: 3174-3316, and SEQ ID NOs: 3317-3459.

[0083] Any suitable gene therapy methods may be used for purposes of the present invention. Generally, an exogenous nucleic acid encoding a peptide compound of the present invention is incorporated into a suitable expression vector and is operably linked to a promoter in the vector. Suitable promoters include but are not limited to viral transcription promoters derived from adenovirus, simian virus 40 (SV40) (e.g., the early and late promoters of SV40), Rous sarcoma virus (RSV), and cytomegalovirus (CMV) (e.g., CMV immediate-early promoter), human immunodeficiency virus (HIV) (e.g., long terminal repeat (LTR)), vaccinia virus (e.g., 7.5K promoter), and herpes simplex virus (HSV) (e.g., thymidine kinase promoter). Where tissue-specific expression of the exogenous gene is desirable, tissue-specific promoters may be operably linked to the exogenous gene. In this respect, a CD4+ T cell-specific promoter will be most desirable. In addition, selection markers may also be included in the vector for purposes of selecting, in vitro, those cells that contain the exogenous nucleic acid encoding the peptide compound of the present invention. Various selection markers known in the art may be used including, but not limited to, e.g., genes conferring resistance to neomycin, hygromycin, zeocin, and the like.

[0084] In one embodiment, the exogenous nucleic acid is incorporated into a plasmid DNA vector. Many commercially available expression vectors may be useful for the present invention, including, e.g., pCEP4, pcDNAI, pIND, pSecTag2, pVAX1, pcDNA3.1, and pBI-EGFP, and pDisplay.

[0085] Various viral vectors may also be used. Typically, in a viral vector, the viral genome is engineered to eliminate the disease-causing capability, e.g., the ability to replicate in the host cells. The exogenous nucleic acid to be introduced into a patient may be incorporated into the engineered viral genome, e.g., by inserting it into a viral gene that is non-essential to the viral infectivity. Viral vectors are convenient to use as they can be easily introduced into tissue cells by way of infection. Once in the host cell, the recombinant virus typically is integrated into the genome of the host cell. In rare instances, the recombinant virus may also replicate and remain as extrachromosomal elements.

[0086] A large number of retroviral vectors have been developed for gene therapy. These include vectors derived from oncoretroviruses (e.g., MLV), viruses (e.g., HIV and SIV) and other retroviruses. For example, gene therapy vectors have been developed based on murine leukemia virus (See, Cepko, et al., Cell, 37:1053-1062 (1984), Cone and Mulligan, Proc. Natl. Acad. Sci. U.S.A., 81:6349-6353 (1984)), mouse mammary tumor virus (See, Salmons et al., Biochem. Biophys. Res. Commun., 159:1191-1198 (1984)), gibbon ape leukemia virus (See, Miller et al., J. Virology, 65:2220-2224 (1991)), HIV, (See Shimada et al., J. Clin. Invest., 88:1043-1047 (1991)), and avian retroviruses (See Cosset et al., J. Virology, 64:1070-1078 (1990)). In addition, various retroviral vectors are also described in U.S. Pat. Nos. 6,168,916; 6,140,111; 6,096,534; 5,985,655; 5,911,983; 4,980,286; and 4,868,116, all of which are incorporated herein by reference.

[0087] Adeno-associated virus (AAV) vectors have been successfully tested in clinical trials. See e.g., Kay et al., Nature Genet. 24:257-61 (2000). AAV is a naturally occurring defective virus that requires other viruses such as adenoviruses or herpes viruses as helper viruses. See Muzyczka, Curr. Top. Microbiol. Immun., 158:97 (1992). A recombinant AAV virus useful as a gene therapy vector is disclosed in U.S. Pat. No. 6,153,436, which is incorporated herein by reference.

[0088] Adenoviral vectors can also be useful for purposes of gene therapy in accordance with the present invention. For example, U.S. Pat. No. 6,001,816 discloses an adenoviral vector, which is used to deliver a leptin gene intravenously to a mammal to treat obesity. Other recombinant adenoviral vectors may also be used, which include those disclosed in U.S. Pat. Nos. 6,171,855; 6,140,087; 6,063,622; 6,033,908; and 5,932,210, and Rosenfeld et al., Science, 252:431-434 (1991); and Rosenfeld et al., Cell, 68:143-155 (1992).

[0089] Other useful viral vectors include recombinant hepatitis viral vectors (See, e.g., U.S. Pat. No. 5,981,274), and recombinant entomopox vectors (See, e.g., U.S. Pat. Nos. 5,721,352 and 5,753,258).

[0090] Other non-traditional vectors may also be used for purposes of this invention. For example, International Publication No. WO 94/18834 discloses a method of delivering DNA into mammalian cells by conjugating the DNA to be delivered with a polyelectrolyte to form a complex. The complex may be microinjected into or taken up by cells.

[0091] The exogenous nucleic acid fragment or plasmid DNA vector containing the exogenous gene may also be introduced into cells by way of receptor-mediated endocytosis. See e.g., U.S. Pat. No. 6,090,619; Wu and Wu, J. Biol. Chem., 263:14621 (1988); Curiel et al., Proc. Natl. Acad. Sci. USA, 88:8850 (1991). For example, U.S. Pat. No. 6,083,741 discloses introducing an exogenous nucleic acid into mammalian cells by associating the nucleic acid to a polycation moiety (e.g., poly-L-lysine, having 3-100 lysine residues), which is itself coupled to an integrin receptor binding moiety (e.g., a cyclic peptide having the amino acid sequence RGD).

[0092] Alternatively, the exogenous nucleic acid or vectors containing it can also be delivered into cells via amphiphiles. See e.g., U.S. Pat. No. 6,071,890. Typically, the exogenous nucleic acid or a vector containing the nucleic acid forms a complex with the cationic amphiphile. Mammalian cells contacted with the complex can readily absorb the complex.

[0093] The exogenous nucleic acid can be introduced into a patient for purposes of gene therapy by various methods known in the art. For example, the exogenous nucleic acid alone or in a conjugated or complex form described above, or incorporated into viral or DNA vectors, may be administered directly by injection into an appropriate tissue or organ of a patient. Alternatively, catheters or like devices may be used for delivery into a target organ or tissue. Suitable catheters are disclosed in, e.g., U.S. Pat. Nos. 4,186,745; 5,397,307; 5,547,472; 5,674,192; and 6,129,705, all of which are incorporated herein by reference.

[0094] In addition, the exogenous nucleic acid encoding a peptide compound of the present invention or vectors containing the nucleic acid can be introduced into isolated cells using any known techniques such as calcium phosphate precipitation, microinjection, lipofection, electroporation, gene gun, receptor-mediated endocytosis, and the like. Cells expressing the exogenous gene may be selected and redelivered back to the patient by, e.g., injection or cell transplantation. The appropriate amount of cells delivered to a patient will vary with patient conditions, and desired effect, which can be determined by a skilled artisan. See e.g., U.S. Pat. Nos. 6,054,288; 6,048,524; and 6,048,729. Preferably, the cells used are autologous, i.e., obtained from the patient being treated.

[0095] When the transporter used in the method of the present invention is a peptidic transporter, a hybrid polypeptide or fusion polypeptide is provided. In preferred embodiments, the hybrid polypeptide includes (a) a first portion comprising an amino acid sequence motif PX1X2P, and capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and (b) a second portion which is a peptidic transporter capable of increasing the uptake of the first portion by human cells. Preferably, the first portion consists of from about 8 to about 100 amino acid residues, more preferably 9 to 20 amino acid residues. Preferably, the peptidic transporter is capable of increasing the uptake of the first portion by a mammalian cell by at least 100%, more preferably by at least 300%. In one embodiment, the first portion does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

[0096] The hybrid polypeptide can be produced in a patient's body by administering to the patient a nucleic acid encoding the hybrid polypeptide by a gene therapy method as described above. Alternatively, the hybrid polypeptide can be chemically synthesized or produced by recombinantly expression.

[0097] Thus, the present invention also provides isolated nucleic acids encoding the hybrid polypeptides and host cells recombinantly expressing the hybrid polypeptides. Such a host cell can be prepared by introducing into a suitable cell an exogenous nucleic acid encoding one of the hybrid polypeptides by standard molecular cloning techniques as described above. The nucleic acids can be prepared by linked a nucleic acid encoding the first portion and a nucleic acid encoding the second portion. Methods for preparing such nucleic acids and for using them in recombinant expression should be apparent to skilled artisans.

[0098] The compounds according to the present invention capable of binding Tsg101 are a novel class of antiviral compounds distinct from other commercially available compounds. While not wishing to be bound by any theory or hypothesis, it is believed that the compounds according to the present invention inhibit virus through a mechanism distinct from those of the antiviral compounds known in the art. Therefore, it may be desirable to employ combination therapies to administer to a patient both a compound according to the present invention, with or without a transporter, and another anti-viral compound of a different class. However, it is to be understood that such other antiviral compounds should be pharmaceutically compatible with the compound of the present invention. By “pharmaceutically compatible” it is intended that the other anti-viral agent(s) will not interact or react with the above composition, directly or indirectly, in such a way as to adversely affect the effect of the treatment, or to cause any significant adverse side reaction in the patient. In this combination therapy approach, the two different pharmaceutically active compounds can be administered separately or in the same pharmaceutical composition. Compounds suitable for use in combination therapies with the Tsg101-binding compounds according to the present invention include, but are not limited to, small molecule drugs, antibodies, immunomodulators, and vaccines.

[0099] In the case of treating HIV infection and AIDS, and/or preventing AIDS using the compounds of the present invention, another anti-HIV compound may be used with a compound of the present invention in a combination therapy. Compounds suitable for use in combination therapies with the Tsg101-binding compounds according to the present invention include, but are not limited to, HIV protease inhibitors, nucleoside HIV reverse transcriptase inhibitors, non-nucleoside HIV reverse transcriptase inhibitors, HIV integrase inhibitors, immunomodulators, and vaccines.

[0100] Examples of nucleoside HIV reverse transcriptase inhibitors include 3′-Azido-3′-deoxythymidine (Zidovudine, also known as AZT and RETROVIR®), 2′,3′-Didehydro-3′-deoxythymidine (Stavudine, also known as 2′,3′-dihydro-3′-deoxythymidine, d4T, and ZERIT®), (2R-cis)-4-Amino-1-[2-(hydroxymethyl)-1,3-oxathiolan-5-yl]-2(1H)-pyrimidinone (Lamivudine, also known as 3TC, and EPIVIR®), and 2′,3′-dideoxyinosine (ddI).

[0101] Examples of non-nucleoside HIV reverse transcriptase inhibitors include (−)-6-Chloro-4-cyclopropylethynyl-4-trifluoromethyl-1,4-dihydro-2H-3,1 -benzoxazin-2-one (efavirenz, also known as DMP-266 or SUSTIVA®) (see U.S. Pat. No. 5,519,021), 1-[3-[(1-methylethyl)aminol]-2-pyridinyl]-4-[[5-[(methylsulfonyl)amino]- 1H -indol-2-yl]carbonyl]piperazine (Delavirdine, see PCT International Patent Application No. WO 91/09849), and (1S,4R)-cis-4-[2-amino-6-(cycloprpoylamino)-9H-purin-9-yl]-2-cyclopentene-1-methanol (Abacavir).

[0102] Examples of protease inhibitors include [5S-(5R*,8R*, 10R*, 11R*)]-10-hydroxy-2-methyl-5-(1-methylethyl)-1-[2-(1-methylethyl)-4-thiazolyl]-3,6-dioxo-8,11-bis(phenylmethyl)-2,4,7,12-tetraazatridecan-13-oic acid 5-thiazolylmethyl ester (Ritonavir, marketed by Abbott as NORVIR®), [3S-[2(2S*,3S*),3a,4ab,8ab]]-N-(1,1-dimethylethyl)decahydro-2-[2-hydroxy-3-[(3-hydroxy-2-methylbenzoyl)amino]-4-(phenylthio)butyl]-3-isoquinolinecarb oxamide monomethanesulfonate (Nelfinavir, marketed by Agouron as VIRACEPT®), N-(2(R)-hydroxy-1(S)-indanyl)-2(R)-phenylmethyl-4-(S)-hydroxy-5-(1-(4-(2-benzo[b]furanylmethyl)-2(S)-N′(t-butylcarboxamido)-piperazinyl))-pentaneamide (See U.S. Pat. No. 5,646,148), N-(2(R)-hydroxy-1(S)-indanyl)2(R)-phenylmethyl-4-(S)-hydroxy-5-(1-(4-(3-pyridylmethyl)-2(S)-N′-(t-butylcarboxamido)-piperazinyl))-pentaneamide (Indinavir, marketed by Merck as CRIXIVAN®), 4-amino-N-((2 syn,3S)-2-hydroxy-4-phenyl-3-((S)-tetrahydrofuran-3-yloxycarbonylamino)-butyl)-N-isobutyl-benzenesulfonamide (amprenavir, see U.S. Pat. No. 5,585,397), and N-tert-butyl-decahydro-2-[2(R)-hydroxy-4-phenyl-3(S)-[[N-(2-quinolylcarbonyl)-L-asparaginyl]amino]butyl]-(4aS,8aS)-isoquinoline-3(S)-carboxamide (Saquinavir, marketed by Roche Laboratories as INVIRASE®).

[0103] Examples of suitable HIV integrase inhibitors are disclosed in U.S. Pat. Nos. 6,110,716; 6,124,327; and 6,245,806, which are incorporated herein by reference.

[0104] In addition, antifusogenic peptides disclosed in, e.g., U.S. Pat. No. 6,017,536 can also be included in the combination therapies according to the present invention. Such peptides typically consist of a 16 to 39 amino acid region of a simian immunodeficiency virus (SIV) protein and are identified through computer algorithms capable of recognizing the ALLMOTI5, 107×178×4, or PLZIP amino acid motifs. See U.S. Pat. No. 6,017,536, which is incorporated herein by reference.

[0105] Typically, a compound of the present invention is administered to a patient in a pharmaceutical composition, which typically includes one or more pharmaceutically acceptable carriers that are inherently nontoxic and non-therapeutic. That is, the compounds are used in the manufacture of medicaments for use in the methods of treating viral infection provided in the present invention.

[0106] The pharmaceutical composition according to the present invention may be administered to a subject needing treatment or prevention through any appropriate routes such as parenteral, oral, or topical administration. The active compounds of this invention are administered at a therapeutically effective amount to achieve the desired therapeutic effect without causing any serious adverse effects in the patient treated. Generally, the toxicity profile and therapeutic efficacy of therapeutic agents can be determined by standard pharmaceutical procedures in suitable cell models or animal models or human clinical trials. As is known in the art, the LD50 represents the dose lethal to about 50% of a tested population. The ED50 is a parameter indicating the dose therapeutically effective in about 50% of a tested population. Both LD50 and ED50 can be determined in cell models and animal models. In addition, the IC50 may also be obtained in cell models and animal models, which stands for the circulating plasma concentration that is effective in achieving about 50% of the maximal inhibition of the symptoms of a disease or disorder. Such data may be used in designing a dosage range for clinical trials in humans. Typically, as will be apparent to skilled artisans, the dosage range for human use should be designed such that the range centers around the ED50 and/or IC50, but significantly below the LD50 obtained from cell or animal models.

[0107] Typically, the compounds of the present invention can be effective at an amount of from about 0.01 microgram to about 5000 mg per day, preferably from about 1 microgram to about 2500 mg per day. However, the amount can vary with the body weight of the patient treated and the state of disease conditions. The active ingredient may be administered at once, or may be divided into a number of smaller doses to be administered at predetermined intervals of time. The suitable dosage unit for each administration of the compounds of the present invention can be, e.g., from about 0.01 microgram to about 2000 mg, preferably from about 1 microgram to about 1000 mg.

[0108] In the case of combination therapy, a therapeutically effective amount of another anti-viral compound can be administered in a separate pharmaceutical composition, or alternatively included in the pharmaceutical composition that contains a compound according to the present invention. The pharmacology and toxicology of many of such other anti-viral compounds are known in the art. See e.g., Physicians Desk Reference, Medical Economics, Montvale, N.J.; and The Merck Index, Merck & Co., Rahway, N.J. The therapeutically effective amounts and suitable unit dosage ranges of such compounds used in art can be equally applicable in the present invention.

[0109] It should be understood that the dosage ranges set forth above are exemplary only and are not intended to limit the scope of this invention. The therapeutically effective amount for each active compound can vary with factors including but not limited to the activity of the compound used, stability of the active compound in the patient's body, the severity of the conditions to be alleviated, the total weight of the patient treated, the route of administration, the ease of absorption, distribution, and excretion of the active compound by the body, the age and sensitivity of the patient to be treated, and the like, as will be apparent to a skilled artisan. The amount of administration can also be adjusted as the various factors change over time.

[0110] The active compounds according to this invention can be administered to patients to be treated through any suitable routes of administration. Advantageously, the active compounds are delivered to the patient parenterally, i.e., by intravenous, intramuscular, intraperiotoneal, intracisternal, subcutaneous, or intraarticular injection or infusion.

[0111] For parenteral administration, the active compounds can be formulated into solutions or suspensions, or in lyophilized forms for conversion into solutions or suspensions before use. Lyophilized compositions may include pharmaceutically acceptable carriers such as gelatin, DL-lactic and glycolic acids copolymer, D-mannitol, etc. To convert the lyophilized forms into solutions or suspensions, diluent containing, e.g., carboxymethylcellulose sodium, D-mannitol, polysorbate 80, and water may be employed. Lyophilized forms may be stored in, e.g., a dual chamber syringe with one chamber containing the lyophilized composition and the other chamber containing the diluent. In addition, the active ingredient(s) can also be incorporated into sterile lyophilized microspheres for sustained release. Methods for making such microspheres are generally known in the art. See U.S. Pat. Nos. 4,652,441; 4,728,721; 4,849,228; 4,917,893; 4,954,298; 5,330,767; 5,476,663; 5,480,656; 5,575,987; 5,631,020; 5,631,021; 5,643,607; and 5,716,640.

[0112] In a solution or suspension form suitable for parenteral administration, the pharmaceutical composition can include, in addition to a therapeutically or prophylactically effective amount of a compound of the present invention, a buffering agent, an isotonicity adjusting agent, a preservative, and/or an anti-absorbent. Examples of suitable buffering agent include, but are not limited to, citrate, phosphate, tartrate, succinate, adipate, maleate, lactate and acetate buffers, sodium bicarbonate, and sodium carbonate, or a mixture thereof. Preferably, the buffering agent adjusts the pH of the solution to within the range of 5-8. Examples of suitable isotonicity adjusting agents include sodium chloride, glycerol, mannitol, and sorbitol, or a mixture thereof. A preservative (e.g., anti-microbial agent) may be desirable as it can inhibit microbial contamination or growth in the liquid forms of the pharmaceutical composition. Useful preservatives may include benzyl alcohol, a paraben and phenol or a mixture thereof. Materials such as human serum albumin, gelatin or a mixture thereof may be used as anti-absorbents. In addition, conventional solvents, surfactants, stabilizers, pH balancing buffers, and antioxidants can all be used in the parenteral formulations, including but not limited to dextrose, fixed oils, glycerine, polyethylene glycol, propylene glycol, ascorbic acid, sodium bisulfite, and the like. The parenteral formulation can be stored in any conventional containers such as vials, ampoules, and syringes.

[0113] The active compounds can also be delivered orally in enclosed gelatin capsules or compressed tablets. Capsules and tablets can be prepared in any conventional techniques. For example, the active compounds can be incorporated into a formulation which includes pharmaceutically acceptable carriers such as excipients (e.g., starch, lactose), binders (e.g., gelatin, cellulose, gum tragacanth), disintegrating agents (e.g., alginate, Primogel, and corn starch), lubricants (e.g., magnesium stearate, silicon dioxide), and sweetening or flavoring agents (e.g., glucose, sucrose, saccharin, methyl salicylate, and peppermint). Various coatings can also be prepared for the capsules and tablets to modify the flavors, tastes, colors, and shapes of the capsules and tablets. In addition, liquid carriers such as fatty oil can also be included in capsules.

[0114] Other forms of oral formulations such as chewing gum, suspension, syrup, wafer, elixir, and the like can also be prepared containing the active compounds used in this invention. Various modifying agents for flavors, tastes, colors, and shapes of the special forms can also be included. In addition, for convenient administration by enteral feeding tube in patients unable to swallow, the active compounds can be dissolved in an acceptable lipophilic vegetable oil vehicle such as olive oil, corn oil and safflower oil.

[0115] The active compounds can also be administered topically through rectal, vaginal, nasal, bucal, or mucosal applications. Topical formulations are generally known in the art including creams, gels, ointments, lotions, powders, pastes, suspensions, sprays, drops and aerosols. Typically, topical formulations include one or more thickening agents, humectants, and/or emollients including but not limited to xanthan gum, petrolatum, beeswax, or polyethylene glycol, sorbitol, mineral oil, lanolin, squalene, and the like.

[0116] A special form of topical administration is delivery by a transdermal patch. Methods for preparing transdermal patches are disclosed, e.g., in Brown, et al., Annual Review of Medicine, 39:221-229 (1988), which is incorporated herein by reference.

[0117] The active compounds can also be delivered by subcutaneous implantation for sustained release. This may be accomplished by using aseptic techniques to surgically implant the active compounds in any suitable formulation into the subcutaneous space of the anterior abdominal wall. See, e.g., Wilson et al., J. Clin. Psych. 45:242-247 (1984). Sustained release can be achieved by incorporating the active ingredients into a special carrier such as a hydrogel. Typically, a hydrogel is a network of high molecular weight biocompatible polymers, which can swell in water to form a gel like material. Hydrogels are generally known in the art. For example, hydrogels made of polyethylene glycols, or collagen, or poly(glycolic-co-L-lactic acid) are suitable for this invention. See, e.g., Phillips et al., J. Pharnaceut. Sci., 73:1718-1720 (1984).

[0118] The active compounds can also be conjugated, i.e., covalently linked, to a water soluble non-immunogenic high molecular weight polymer to form a polymer conjugate. Preferably, such polymers do not undesirably interfere with the cellular uptake of the active compounds. Advantageously, such polymers, e.g., polyethylene glycol, can impart solubility, stability, and reduced immunogenicity to the active compounds. As a result, the active compound in the conjugate when administered to a patient, can have a longer half-life in the body, and exhibit better efficacy. In one embodiment, the polymer is a peptide such as albumin or antibody fragment Fc. PEGylated proteins are currently being used in protein replacement therapies and for other therapeutic uses. For example, PEGylated adenosine deaminase (ADAGEN®) is being used to treat severe combined immunodeficiency disease (SCIDS). PEGylated L-asparaginase (ONCAPSPAR®) is being used to treat acute yymphoblastic leukemia (ALL). A general review of PEG-protein conjugates with clinical efficacy can be found in, e.g., Burnham, Am. J. Hosp. Pharm., 15:210-218 (1994). Preferably, the covalent linkage between the polymer and the active compound is hydrolytically degradable and is susceptible to hydrolysis under physiological conditions. Such conjugates are known as “prodrugs” and the polymer in the conjugate can be readily cleaved off inside the body, releasing the free active compounds.

[0119] Alternatively, other forms controlled release or protection including microcapsules and nanocapsules generally known in the art, and hydrogels described above can all be utilized in oral, parenteral, topical, and subcutaneous administration of the active compounds.

[0120] Another preferable delivery form is using liposomes as carrier. Liposomes are micelles formed from various lipids such as cholesterol, phospholipids, fatty acids, and derivatives thereof. Active compounds can be enclosed within such micelles. Methods for preparing liposomal suspensions containing active ingredients therein are generally known in the art and are disclosed in, e.g., U.S. Pat. No. 4,522,811, and Prescott, Ed., Methods in Cell Biology, Volume XIV, Academic Press, New York, N.Y. (1976), p. 33 et seq., both of which are incorporated herein by reference. Several anticancer drugs delivered in the form of liposomes are known in the art and are commercially available from Liposome Inc. of Princeton, N.J., U.S.A. It has been shown that liposomes can reduce the toxicity of the active compounds, and increase their stability.

EXAMPLE 1

[0121] Yeast two-hybrid assays were utilized to determine the effect of amino acid substitution mutations in the PTAP motif of HIV p6gag on the interaction between Tsg101 and p6gag. To prepare a yeast two-hybrid activation domain-Tsg101 construct, a DNA fragment encompassing the full-length coding sequence for Tsg101 according to GenBank Accession No. U82130 was obtained by PCR from a human fetal brain cDNA library and cloned into the EcoRI/Pst1 sites of the activation domain parent plasmid GADpN2 (LEU2, CEN4, ARS1, ADH1p-SV40NLS-GAL4 (768-881)-MCS (multiple cloning site)-PGKit, AmpR, ColE1_ori).

[0122] To prepare the yeast two-hybrid DNA binding domain-HIV1 p6gag construct, a DNA fragment corresponding to the HIV1 p6 peptide derived from the HIV1 .NL43 strain GAG protein was obtained by PCR from the NL43 containing plasmid R9Δapa and was cloned into the EcoRI/Sal1 sites of the binding domain parent plasmid pGBT.Q. The sequence of the amplified insert is shown in SEQ ID NO: 3485. In addition, the amino acid sequence of the HIV-1NYU/BR5 GAG is provided in GenBank under Accession No. AF324493 and is listed in SEQ ID NO: 3484.

[0123] The following amino acid substitution mutations were introduced by PCR into the HIV1 p6gag sequence in the yeast two-hybrid binding domain-HIV1 p6gag construct described above. The mutations were verified by DNA sequence analysis. Such mutations are summarized in Table 26 below.

TABLE 26

Tested Mutations in p6gag Protein

Mutant Construct

p6gag Peptide Sequence Surrounding the PTAP Motif

p6(wt)

S

R

P

E

P

T

A

P

P

E

E

S

F

R

F

p6(E6G)

G

p6(P7L)

L

p6(A9R)

R

p6(P10L)

L

[0124] To test the effect of the mutations, yeast cells of the strain Y189 purchased from Clontech (ura3-52 his3*200 ade2-101 trp1-901 leu2-3,112 met gal4 gal80 URA3::GAL1p-lacZ) were co-transformed with the activation domain-Tsg101 construct and one of the binding domain-mutant p6gag constructs or the binding domain-wild type p6gag construct. Filter lift assays for β-Gal activity were conducted by lifting the transformed yeast colonies with filters, lysing the yeast cells by freezing and thawing, and contacting the lysed cells with X-Gal. Positive β-Gal activity indicates that the p6gag wild type or mutant protein interacts with Tsg101. All binding domain constructs were also tested for self-activation of β-Gal activity. The results are shown in Table 27.

TABLE 27
Interactions Between Tsg101 and p6gag
	p6(wt)	p6(E6G)	p6(P7L)	p6(A9R)	p6(P10L)
Tsg101	+	+	−	−	−
p6(wt)	−
p6(E6G)		−
p6(P7L)			−
P6(A9R)				−
P6(P10L)					−

[0125] Thus, as is clear from Table 27, the mutations in the PTAP motif of HIV p6gag abolished the interaction between Tsg101 and HIV p6gag, while the p6/E6G mutation outside the PTAP motif did not result in the elimination of the Tsg101-p6gag interaction.

[0126] The interactions between TSG101 and wild-type p6gag (WT) or the p6gag PTAP mutants were further quantitated by performing liquid culture β-galactosidase assays. Cultures were grown overnight in synthetic media (-Leu, -Trp, +glucose) in 96 well plates, normalized for optical density, and lysed by addition of 6× lysis/substrate solution in 6× Z-buffer (60 mM KCl, 6 mM MgSO4, 360 mM Na2HPO4, 240 mM NaH2PO4, 6 mg/ml CPRG, 0.12U/ml lyticase, 0.075% NP-40). Cultures were incubated for 2 hr at 37° C., clarified by centrifugation, and the optical absorbance of each supernatant was measured (575 nm). Full length Tsg101 bound wild-type p6 in the two-hybrid liquid culture assay, resulting in high levels of β-galactosidase activity (>300-fold over background). Three different p6 point mutants were used to test whether the Tsg101 binding interaction required the PTAP late domain motif within HIV-1 p6, and all three (P6L, A9R and P10L) reduced β-galactosidase activity to background levels. Each of these point mutations also arrests HIV-1 budding at a late stage (Huang et al. 1995). These results are consistent with the hypothesis that the interaction between HIV p6gag and the human cellular protein TSG101 is essential for viral budding to occur.

EXAMPLE 2

[0127] A fusion protein with a GST tag fused to the HIV-1 GAGp6 domain was recombinantly expressed and purified by chromatography. In addition, a GAGp6 peptide containing the first 14 amino acid residues (“p6(1-14)”) was synthesized chemically by standard peptide synthesis methods. The peptide was purified by conventional protein purification techniques, e.g., by chromatography.

[0128] Nunc/Nalgene Maxisorp plates were incubated overnight at 4° C. or for 1-2 hrs at room temperature in 100 μl of a protein coupling solution containing purified GST-p6 and 50 mM Carbonate, pH=9.6. This allowed the attachment of the GST-p6 fusion protein to the plates. Liquids in the plates were then emptied and wells filled with 400 μl/well of a blocking buffer (SuperBlock; Pierce-Endogen, Rockford, Ill.). After incubating for 1 hour at room temperature, 100 μl of a mixture containing Drosophila S2 cell lysate myc-tagged Tsg101 (residues 1-207) and a specific amount of the p6(1-14) peptide were applied to the wells of the plate. This mixture was allowed to react for 2 hours at room temperature to form p6:Tsg101 protein-protein complexes.

[0129] Plates were then washed 4×100 μl with 1× PBST solution (Invitrogen; Carlsbad, Calif.). After washing, 100 μl of 1 μg/ml solution of anti-myc monoclonal antibody (Clone 9E10; Roche Molecular Biochemicals; Indianapolis, Ind.) in 1×PBST was added to the wells of the plate to detect the myc-epitope tag on the Tsg101 protein. Plates were then washed again with 4×100 μl with 1×PBST solution and 100 μl of 1 μg/ml solution of horseradish peroxidase (HRP) conjugated Goat anti-mouse IgG (Jackson Immunoresearch Labs; West Grove, Pa.) in 1×PBST was added to the wells of the plate to detect bound mouse anti-myc antibodies. Plates were then washed again with 4×100 μl with 1×PBST solution and 100 μl of fluorescent substrate (QuantaBlu; Pierce-Endogen, Rockford, Ill.) was added to all wells. After 30 minutes, 100 μl of stop solution was added to each well to inhibit the function of HRP. Plates were then read on a Packard Fusion instrument at an excitation wavelength of 325 nm and an emission wavelength of 420 nm. The presence of fluorescent signals indicates binding of Tsg101 to the fixed GST-p6. In contrast, the absence of fluorescent signals indicates that the p6(1-14) peptide is capable of disrupting the interaction between Tsg101 and HV p6.

[0130] Different concentrations of the p6(1-14) peptide were tested, and the relative intensities of the fluorescence signals obtained at different concentrations were plotted against the peptide concentrations. The competitive inhibition curve is shown in FIG. 1. Two Dixon plots are shown in FIG. 2 and FIG. 3, respectively.

EXAMPLE 3

[0131] 1. Materials

[0132] For antiviral tests, the following peptidic compounds (in Table 3) were chemically synthesized and purified by conventional protein purification techniques:

TABLE 28
Compound	Formula	SEQ ID NO:
MPI-PEP1	NH2-(R)9-PEPTAPEE-COOH	3485
MPI-PEP2	NH2-(R)9-PEPTALEE-COOH	3486
MPI-PEP3	NH2-RPEPTAP-CO-NH2	3487

[0133] The compounds were solubilized in sterile RPMI 1640 tissue culture medium to yield 40 mM stock solutions. AZT was used as a positive control antiviral compound.

[0134] Fresh human blood was obtained commercially from Interstate Blood Bank, Inc. (Memphis, Tenn.). The lymphotropic clinical isolate HIV-1ROJO was obtained from a pediatric patient attending the AIDS Clinic at the University of Alabama at Birmingham. The laboratory-adapted HIV-1HIB strain was propagated and tittered in fresh human PBMCs; pre-titered aliquots of HIV-1ROJO and Hiv-1HIB were removed from the freezer (−80° C.) and thawed rapidly to room temperature in a biological safety cabinet immediately before use. Phytohemagglutinin (PHA-P) was obtained from Sigma (St. Louis, Mo.) and recombinant IL-2 was obtained from Amgen (San Francisco, Calif.).

[0135] 2. Anti-HIV Efficacy Evaluation in Fresh Human PBMCs

[0136] Fresh human PBMCs were isolated from screened donors, seronegative for HIV and HBV. Leukophoresed blood was diluted 1:1 with Dulbecco's phosphate buffered saline (PBS), layered over 14 mL of Ficoll-Hypaque density gradient in a 50 mL centrifuge tube and then centrifuged for 30 minutes at 600×g. Banded PBMCs were aspirated from the resulting interface and subsequently washed 2× with PBS by low speed centrifugation. After the final wash, cells were enumerated by trypan blue exclusion and re-suspended at 1×107 cells/mL in RPMI 1640 supplemented with 15% Fetal Bovine Serum (FBS), 2 mM L-glutamine, 4 μg/mL PHA-P. The cells were allowed to incubate for 48-72 hours at 37° C. After incubation, PBMCs were centrifuged and reset in RPMI 1640 with 15% FBS, 2 mM L-glutamine, 100 U/ml penicillin, 100 μg/mL streptomycin, 10 μg/mL gentamycin, and 20 U/mL recombinant human IL-2. PBMCs were maintained in this medium at a concentration of 1-2×106 cells/mL with biweekly medium changes until used in the assay protocol.

[0137] For the standard PBMC assay, PHA-P stimulated cells from at least two normal donors were pooled, diluted in fresh medium to a final concentration of 1×106 cells/mL, and plated in the interior wells of 96 well round bottom microplate at 50 μL/well (5×104 cells/well). Test drug dilutions were prepared at a 2× concentration in microtiter tubes and 100 μL of each concentration was placed in appropriate wells in a standard format. 50 μL of a predetermined dilution of virus stock was placed in each test well (final MOI ≈0.1). Wells with cells and virus alone were used for virus control. Separate plates were prepared identically without virus for drug cytotoxicity studies using an XTT assay system. The PBMC cultures were maintained for seven days following infection, at which time cell-free supernate samples were collected and assayed for reverse transcriptase activity as described below.

[0138] 3. Reverse Transcriptase Activity Assay

[0139] A microtiter based reverse transcriptase (RT) reaction was utilized. See Buckheit et al., AIDS Research and Human Retroviruses 7:295-302 (1991). Tritiated thymidine triphosphate (NEN) (TTP) was resuspended in distilled H2O at 5 Ci/ml. Poly rA and oligo dT were prepared as a stock solution which was kept at −20° C. The RT reaction buffer was prepared fresh on a daily basis and consists of 125 μl 1M EGTA, 125 μl dH2O, 110 μl 10% SDS, 50 μl 1M Tris (pH 7.4), 50 μl 1M DTT, and 40 μl 1M MgCL2. These three solutions were mixed together in a ratio of 2 parts TTP, 1 part poly rA:oligo dT, and 1 part reaction buffer. Ten microliters of this reactions mixture was placed at a round bottom microtiter plate and 15 μl of virus containing supernatant was added and mixed. The plate was incubated at 37° C. in a water bath with a solid support to prevent submersion of the plate and incubated for 60 minutes. Following reaction, the reaction volume was spotted onto pieces of DE81 paper, washed 5 times 5 minutes each in a 5% sodium phosphate buffer, 2 times 1 minute each in distilled water, 2 times for 1 minute each in 70% ethanol, and then dried. Opti-Fluor-O (Packard) was added to each sample and incorporated radioactivity was quantified utilizing a Wallac 1450 MicroBeta Plus liquid scintillation counter.

[0140] 4. Cytotoxicity Measurement By MTS Staining

[0141] At assay termination the assay plates were stained with the soluble tetrazolium-based dye MTS (CellTiter Reagent, Promega) to determine cell viability and quantify compound toxicity. MTS is metabolized by the mitochondria enzymes of metabolically active cells to yield a soluble formazan product, allowing the rapid quantitative analysis cell viability and compound cytotoxicity. The MTS is a stable solution that does not require preparation before use. At termination of the assay, 20 μl of MTS reagent was added per well. The wells were incubated overnight for the HIV cytoprotection assay at 37° C. The incubation intervals were chosen based on empirically determined times for optimal dye reduction in each cell type. Adhesive plate sealers were used in place of the lids, the sealed plate was inverted several times to mix the soluble formazan product and the plate was read spectrophotometrically at 490 nm with a Molecular Devices Vmax plate reader.

[0142] 5. Data Analysis

[0143] Indices including % CPE Reduction, % Cell Viability, IC50, TC50, and others were calculated and summarized in Table 4 below. The graphical results for the three peptidic compounds tested are displayed in FIGS. 4, 5 and 6, respectively. AZT was evaluated in parallel as a relevant positive control compound in the anti-HIV assay, and the graphical result is shown in FIG. 7.

TABLE 29
Compound			Therapeutic
Name	IC50 (μM)	TC50 (μM)	Index	Comments
MPI-PEP1	21.7	>200.0	9.2	Active
MPI-PEP2	>200.0	>200.0	N/A	Inactive
MPI-PEP3	>200.0	>200.0	N/A	Inactive
AZT	0.008	>1.0	>125.00	Control;
				Highly Active

EXAMPLE 4

[0144] This demonstrates the efficacy assay for the anti-HBV effect of test compound, e.g., the compounds used in Example 3. The assay is similar to the assay described by Korba and Milman, Antiviral Res., 15:217-228 (1991) and Korba and Gerin, Antiviral Res., 19:55-70 (1992), with the exception that viral DNA detection and quantification is dramatically simplified. Briefly, HepG2-2.2.15 cells are plated in 96-well microtiter plates at an initial density of 2×104 cells/100 μl in DMEM medium supplemented with 10% fetal bovine serum. To promote cell adherence, the 96-well plates have been pre-coated with collagen prior to cell plating. After incubation at 37° C. in a humidified, 5% CO2 environment for 16-24 hours, the confluent monolayer of HepG2-2.2.15 cells is washed and the medium is replaced with complete medium containing various concentrations of test compound. Every three days, the culture medium is replaced with fresh medium containing the appropriately diluted drug. Nine days following the initial administration of test compounds, the cell culture supernate is collected and clarified by centrifugation (Sorvall RT-6000D centrifuge, 1000 rpm for 5 min). Three microliters of clarified supernate is then subjected to real-time quantitative PCR using conditions described below.

[0145] Virion-associated HBV DNA present in the tissue culture supernate is PCR amplified using primers derived from HBV strain ayw. Subsequently, the PCR-amplified HBV DNA is detected in real-time (i.e., at each PCR thermocycle step) by monitoring increases in fluorescence signals that result from exonucleolytic degradation of a quenched fluorescent probe molecule following hybridization of the probe to the amplified HBV DNA. The probe molecule, designed with the aid of Primer Express™ (PE-Applied Biosystems) software, is complementary to DNA sequences present in the HBV DNA region amplified.

[0146] Routinely, 3 μl of clarified supernate is analyzed directly (without DNA extraction) in a 50 μl PCR reaction. Reagents and conditions used are per the manufacturers suggestions (PE-Applied Biosystems). For each PCR amplification, a standard curve is simultaneously generated several log dilutions of a purified 1.2 kbp HBV ayw subgenomic fragment; routinely, the standard curve ranged from 1×106 to 1×101 nominal copy equivalents per PCR reaction.

[0147] All publications and patent applications mentioned in the specification are indicative of the level of those skilled in the art to which this invention pertains. All publications and patent applications are herein incorporated by reference to the same extent as if each individual publication or patent application was specifically and individually indicated to be incorporated by reference.

[0148] Although the foregoing invention has been described in some detail by way of illustration and example for purposes of clarity of understanding, it will be obvious that certain changes and modifications may be practiced within the scope of the appended claims.

TABLE 2
P(T/S)AP Motif Containing Peptides from Ebola Virus Matrix Protein
(GenBank Accession No. AAL25816)
SEQ ID NO:38	RVILPTAP	SEQ ID NO:71	RRVILPTAPPEYM
SEQ ID NO:39	VILPTAPP	SEQ ID NO:72	RVILPTAPPEYME
SEQ ID NO:40	ILPTAPPE	SEQ ID NO:73	VILPTAPPEYMEA
SEQ ID NO:41	LPTAPPEY	SEQ ID NO:74	ILPTAPPEYMEAI
SEQ ID NO:42	PTAPPEYM	SEQ ID NO:75	LPTAPPEYMEAIY
SEQ ID NO:43	RRVILPTAP	SEQ ID NO:76	PTAPPEYMEAIYP
SEQ ID NO:44	RVILPTAPP	SEQ ID NO:77	MRRVILPTAPPEYM
SEQ ID NO:45	VILPTAPPE	SEQ ID NO:78	RRVILPTAPPEYME
SEQ ID NO:46	ILPTAPPEY	SEQ ID NO:79	RVILPTAPPEYMEA
SEQ ID NO:47	LPTAPPEYM	SEQ ID NO:80	VILPTAPPEYMEAI
SEQ ID NO:48	PTAPPEYME	SEQ ID NO:81	ILPTAPPEYMEAIY
SEQ ID NO:49	MRRVILPTAP	SEQ ID NO:82	LPTAPPEYMEAIYP
SEQ ID NO:50	RRVILPTAPP	SEQ ID NO:83	PTAPPEYMEAIYPV
SEQ ID NO:51	RVILPTAPPE	SEQ ID NO:84	MRRVILPTAPPEYME
SEQ ID NO:52	VILPTAPPEY	SEQ ID NO:85	RRVILPTAPPEYMEA
SEQ ID NO:53	ILPTAPPEYM	SEQ ID NO:86	RVILPTAPPEYMEAI
SEQ ID NO:54	LPTAPPEYME	SEQ ID NO:87	VILPTAPPEYMEAIY
SEQ ID NO:55	PTAPPEYMEA	SEQ ID NO:88	ILPTAPPEYMEAIYP
SEQ ID NO:56	MRRVILPTAPP	SEQ ID NO:89	LPTAPPEYMEAIYPV
SEQ ID NO:57	RRVILPTAPPE	SEQ ID NO:90	PTAPPEYMEAIYPVR
SEQ ID NO:58	RVILPTAPPEY	SEQ ID NO:91	MRRVILPTAPPEYMEA
SEQ ID NO:59	VILPTAPPEYM	SEQ ID NO:92	RRVILPTAPPEYMEAI
SEQ ID NO:60	ILPTAPPEYME	SEQ ID NO:93	RVILPTAPPEYMEAIY
SEQ ID NO:61	LPTAPPEYMEA	SEQ ID NO:94	VILPTAPPEYMEAIYP
SEQ ID NO:62	PTAPPEYMEAI	SEQ ID NO:95	ILPTAPPEYMEAIYPV
SEQ ID NO:63	MRRVILPTAPPE	SEQ ID NO:96	LPTAPPEYMEAIYPVR
SEQ ID NO:64	RRVILPTAPPEY	SEQ ID NO:97	PTAPPEYMEAIYPVRS
SEQ ID NO:65	RVILPTAPPEYM	SEQ ID NO:98	MRRVILPTAPPEYMEAI
SEQ ID NO:66	VILPTAPPEYME	SEQ ID NO:99	RRVILPTAPPEYMEAIY
SEQ ID NO:67	ILPTAPPEYMEA	SEQ ID NO:100	RVILPTAPPEYMEAIYP
SEQ ID NO:68	LPTAPPEYMEAI	SEQ ID NO:101	VILPTAPPEYMEAIYPV
SEQ ID NO:69	PTAPPEYMEAIY	SEQ ID NO:102	ILPTAPPEYMEAIYPVR
SEQ ID NO:70	MRRVILPTAPPEY	SEQ ID NO:103	LPTAPPEYMEAIYPVRS
SEQ ID NO:104	PTAPPEYMEAIYPVRSN	SEQ ID NO:115	VILPTAPPEYMEAIYPVRS
SEQ ID NO:105	MRRVILPTAPPEYMEAIY	SEQ ID NO:116	ILPTAPPEYMEAIYPVRSN
SEQ ID NO:106	RRVILPTAPPEYMEAIYP	SEQ ID NO:117	LPTAPPEYMEAIYPVRSNS
SEQ ID NO:107	RVILPTAPPEYMEAIYPV	SEQ ID NO:118	PTAPPEYMEAIYPVRSNST
SEQ ID NO:108	VILPTAPPEYMEAIYPVR	SEQ ID NO:119	MRRVILPTAPPEYMEAIYPV
SEQ ID NO:109	ILPTAPPEYMEAIYPVRS	SEQ ID NO:120	RRVILPTAPPEYMEAIYPVR
SEQ ID NO:110	LPTAPPEYMEAIYPVRSN	SEQ ID NO:121	RVILPTAPPEYMEAIYPVRS
SEQ ID NO:111	PTAPPEYMEAIYPVRSNS	SEQ ID NO:122	VILPTAPPEYMEAIYPVRSN
SEQ ID NO:112	MRRVILPTAPPEYMEAIYP	SEQ ID NO:123	ILPTAPPEYMEAIYPVRSNS
SEQ ID NO:113	RRVILPTAPPEYMEAIYPV	SEQ ID NO:124	LPTAPPEYMIEAIYPVRSNST
SEQ ID NO:114	RVILPTAPPEYMEAIYPVR	SEQ ID NO:125	PTAPPEYMEAIYPVRSNSTI

[0149]

TABLE 3
P(T/S)AP Motif Containing Peptides from Hepatitis B Virus
PreS1/PreS2/S Envelope Protein
(GenBank Accession No. BAA85340)
SEQ ID NO:126	LTTVPTAP	SEQ ID NO:161	QAQGILTTVPTAP
SEQ ID NO:127	TTVPTAPP	SEQ ID NO:162	AQGILTTVPTAPP
SEQ ID NO:128	TVPTAPPP	SEQ ID NO:163	QGILTTVPTAPPP
SEQ ID NO:129	VPTAPPPA	SEQ ID NO:164	GILTTVPTAPPPA
SEQ ID NO:130	PTAP PPAS	SEQ ID NO:165	ILTTVPTAPPPAS
SEQ ID NO:131	ILTTVPTAP	SEQ ID NO:166	LTTVPTAPPPAST
SEQ ID NO:132	LTTVPTAPP	SEQ ID NO:167	TTVPTAPPPASTN
SEQ ID NO:133	TTVPTAPPP	SEQ ID NO:168	TVPTAPPPASTNR
SEQ ID NO:134	TVPTAPPPA	SEQ ID NO:169	VPTAPPPASTNRQ
SEQ ID NO:135	VPTAPPPAS	SEQ ID NO:170	PTAP PPASTNRQL
SEQ ID NO:136	PTAP PPAST	SEQ ID NO:171	PQAQGILTTVPTAP
SEQ ID NO:137	GILTTVPTAP	SEQ ID NO:172	QAQGILTTVPTAPP
SEQ ID NO:138	ILTTVPTAPP	SEQ ID NO:173	AQGILTTVPTAPPP
SEQ ID NO:139	LTTVPTAPPP	SEQ ID NO:174	QGILTTVPTAPPPA
SEQ ID NO:140	TTVPTAPPPA	SEQ ID NO:175	GILTTVPTAPPPAS
SEQ ID NO:141	TVPTAPPPAS	SEQ ID NO:176	ILTTVPTAPPPAST
SEQ ID NO:142	VPTAPPPAST	SEQ ID NO:177	LTTVPTAPPPASTN
SEQ ID NO:143	PTAP PPASTN	SEQ ID NO:178	TTVPTAPPPASTNR
SEQ ID NO:144	QGILTTVPTAP	SEQ ID NO:179	TVPTAPPPASTNRQ
SEQ ID NO:145	GILTTVPTAPP	SEQ ID NO:180	VPTAPPPASTNRQL
SEQ ID NO:146	ILTTVPTAPPP	SEQ ID NO:181	PTAP PPASTNRQLG
SEQ ID NO:147	LTTVPTAPPPA	SEQ ID NO:182	SPQAQGILTTVPTAP
SEQ ID NO:148	TTVPTAPPPAS	SEQ ID NO:183	PQAQGILTTVPTAPP
SEQ ID NO:149	TVPTAPPPAST	SEQ ID NO:184	QAQGILTTVPTAPPP
SEQ ID NO:150	VPTAPPPASTN	SEQ ID NO:185	AQGILTTVPTAPPPA
SEQ ID NO:151	PTAP PPASTNR	SEQ ID NO:186	QGILTTVPTAPPPAS
SEQ ID NO:152	AQGILTTVPTAP	SEQ ID NO:187	GILTTVPTAPPPAST
SEQ ID NO:153	QGILTTVPTAPP	SEQ ID NO:188	ILTTVPTAPPPASTN
SEQ ID NO:154	GILTTVPTAPPP	SEQ ID NO:189	LTTVPTAPPPASTNR
SEQ ID NO:155	ILTTVPTAPPPA	SEQ ID NO:190	TTVPTAPPPASTNRQ
SEQ ID NO:156	LTTVPTAPPPAS	SEQ ID NO:191	TVPTAPPPASTNRQL
SEQ ID NO:157	TTVPTAPPPAST	SEQ ID NO:192	VPTAPPPASTNRQLG
SEQ ID NO:158	TVPTAPPPASTN	SEQ ID NO:193	PTAP PPASTNRQLGR
SEQ ID NO:159	VPTAPPPASTNR	SEQ ID NO:194	WSPQAQGILTTVPTAP
SEQ ID NO:160	PTAP PPASTNRQ	SEQ ID NO:195	SPQAQGILTTVPTAPP
SEQ ID NO:196	PQAQGILTTVPTAPPP	SEQ ID NO:233	TVPTAPPPASTNRQLGRK
SEQ ID NO:197	QAQGILTTVPTAPPPA	SEQ ID NO:234	VPTAPPPASTNRQLGRKP
SEQ ID NO:198	AQGILTTVPTAPPPAS	SEQ ID NO:235	PTAP PPASTNRQLGRKPT
SEQ ID NO:199	QGILTTVPTAPPPAST	SEQ ID NO:236	LLGWSPQAQGILTTVPTAP
SEQ ID NO:200	GILTTVPTAPPPASTN	SEQ ID NO:237	LGWSPQAQGILTTVPTAPP
SEQ ID NO:201	ILTTVPTAPPPASTNR	SEQ ID NO:238	GWSPQAQGILTTVPTAPPP
SEQ ID NO:202	LTTVPTAPPPASTNRQ	SEQ ID NO:239	WSPQAQGILTTVPTAPPPA
SEQ ID NO:203	TTVPTAPPPASTNRQL	SEQ ID NO:240	SPQAQGILTTVPTAPPPAS
SEQ ID NO:204	TVPTAPPPASTNRQLG	SEQ ID NO:241	PQAQGILTTVPTAPPPAST
SEQ ID NO:205	VPTAPPPASTNRQLGR	SEQ ID NO:242	QAQGILTTVPTAPPPASTN
SEQ ID NO:206	PTAP PPASTNRQLGRK	SEQ ID NO:243	AQGILTTVPTAPPPASTNR
SEQ ID NO:207	GWSPQAQGILTTVPTAP	SEQ ID NO:244	QGILTTVPTAPPPASTNRQ
SEQ ID NO:208	WSPQAQGILTTVPTAPP	SEQ ID NO:245	GILTTVPTAPPPASTNRQL
SEQ ID NO:209	SPQAQGILTTVPTAPPP	SEQ ID NO:246	ILTTVPTAPPPASTNRQLG
SEQ ID NO:210	PQAQGILTTVPTAPPPA	SEQ ID NO:247	LTTVPTAPPPASTNRQLGR
SEQ ID NO:211	QAQGILTTVPTAPPPAS	SEQ ID NO:248	TTVPTAPPPASTNRQLGRK
SEQ ID NO:212	AQGILTTVPTAPPPAST	SEQ ID NO:249	TVPTAPPPASTNRQLGRKP
SEQ ID NO:213	QGILTTVPTAPPPASTN	SEQ ID NO:250	VPTAPPPASTNRQLGRKYT
SEQ ID NO:214	GILTTVPTAPPPASTNR	SEQ ID NO:251	PTAP PPASTNRQLGRKYTP
SEQ ID NO:215	ILTTVPTAPPPASTNRQ	SEQ ID NO:252	GLLGWSPQAQGILTTVPTAP
SEQ ID NO:216	LTTVPTAPPPASTNRQL	SEQ ID NO:253	LLGWSPQAQGILTTVPTAPP
SEQ ID NO:217	TTVPTAPPPASTNRQLG	SEQ ID NO:254	LGWSPQAQGILTTVPTAPPP
SEQ ID NO:218	TVPTAPPPASTNRQLGR	SEQ ID NO:255	GWSPQAQGILTTVPTAPPPA
SEQ ID NO:219	VPTAPPPASTNRQLGRK	SEQ ID NO:256	WSPQAQGILTTVPTAPPPAS
SEQ ID NO:220	PTAP PPASTNRQLGRKP	SEQ ID NO:257	SPQAQGILTTVPTAPPPAST
SEQ ID NO:221	LGWSPQAQGILTTVPTAP	SEQ ID NO:258	PQAQGILTTVPTAPPPASTN
SEQ ID NO:222	GWSPQAQGILTTVPTAPP	SEQ ID NO:259	QAQGILTTVPTAPPPASTNR
SEQ ID NO:223	WSPQAQGILTTVPTAPPP	SEQ ID NO:260	AQGILTTVPTAPPPASTNRQ
SEQ ID NO:224	SPQAQGILTTVPTAPPPA	SEQ ID NO:261	QGILTTVPTAPPPASTNRQL
SEQ ID NO:225	PQAQGILTTVPTAPPPAS	SEQ ID NO:262	GILTTVPTAPPPASTNRQLG
SEQ ID NO:226	QAQGILTTVPTAPPPAST	SEQ ID NO:263	ILTTVPTAPPPASTNRQLGR
SEQ ID NO:227	AQGILTTVPTAPPPASTN	SEQ ID NO:264	LTTVPTAPPPASTNRQLGRK
SEQ ID NO:228	QGILTTVPTAPPPASTNR	SEQ ID NO:265	TTVPTAPPPASTNRQLGRKP
SEQ ID NO:229	GILTTVPTAPPPASTNRQ	SEQ ID NO:266	TVPTAPPPASTNRQLGRKPT
SEQ ID NO:230	ILTTVPTAPPPASTNRQL	SEQ ID NO:267	VPTAPPPASTNRQLGRKPTP
SEQ ID NO:231	LTTVPTAPPPASTNRQLG	SEQ ID NO:268	PTAP PPASTNRQLGRKPTPL
SEQ ID NO:232	TTVPTAPPPASTNRQLGR

[0150]

TABLE 4
P(T/S)AP Motif Containing Peptides from Human Herpesvirus 1
RL2 Protein
(GenBank Accession No. NP_044601)
SEQ ID NO:269	RTAPPSAP	SEQ ID NO:304	QPAAARTAPPSAP
SEQ ID NO:270	TAPPSAPI	SEQ ID NO:305	PAAARTAPPSAPI
SEQ ID NO:271	APPSAPIG	SEQ ID NO:306	AAARTAPPSAPIG
SEQ ID NO:272	PPSAPIGP	SEQ ID NO:307	AARTAPPSAPIGP
SEQ ID NO:273	PSAP IGPH	SEQ ID NO:308	ARTAPPSAPIGPH
SEQ ID NO:274	ARTAPPSAP	SEQ ID NO:309	RTAPPSAPIGPHG
SEQ ID NO:275	RTAPPSAPI	SEQ ID NO:310	TAPPSAPIGPHGS
SEQ ID NO:276	TAPPSAPIG	SEQ ID NO:311	APPSAPIGPHGSS
SEQ ID NO:277	APPSAPIGP	SEQ ID NO:312	PPSAPIGPHGSSN
SEQ ID NO:278	PPSAPIGPH	SEQ ID NO:313	PSAP IGPHGSSNT
SEQ ID NO:279	PSAP IGPHG	SEQ ID NO:314	PQPAAARTAPPSAP
SEQ ID NO:280	AARTAPPSAP	SEQ ID NO:315	QPAAARTAPPSAPI
SEQ ID NO:281	ARTAPPSAPI	SEQ ID NO:316	PAAARTAPPSAPIG
SEQ ID NO:282	RTAPPSAPIG	SEQ ID NO:317	AAARTAPPSAPIGP
SEQ ID NO:283	TAPPSAPIGP	SEQ ID NO:318	AARTAPPSAPIGPH
SEQ ID NO:284	APPSAPIGPH	SEQ ID NO:319	ARTAPPSAPIGPHG
SEQ ID NO:285	PPSAPIGPHG	SEQ ID NO:320	RTAPPSAPIGPHGS
SEQ ID NO:286	PSAP IGPHGS	SEQ ID NO:321	TAPPSAPIGPHGSS
SEQ ID NO:287	AAARTAPPSAP	SEQ ID NO:322	APPSAPIGPHGSSN
SEQ ID NO:288	AARTAPPSAPI	SEQ ID NO:323	PPSAPIGPHGSSNT
SEQ ID NO:289	ARTAPPSAPIG	SEQ ID NO:324	PSAP IGPHGSSNTN
SEQ ID NO:290	RTAPPSAPIGP	SEQ ID NO:325	APQPAAARTAPPSAP
SEQ ID NO:291	TAPPSAPIGPH	SEQ ID NO:326	PQPAAARTAPPSAPI
SEQ ID NO:292	APPSAPIGPHG	SEQ ID NO:327	QPAAARTAPPSAPIG
SEQ ID NO:293	PPSAPIGPHGS	SEQ ID NO:328	PAAARTAPPSAPIGP
SEQ ID NO:294	PSAP IGPHGSS	SEQ ID NO:329	AAARTAPPSAPIGPH
SEQ ID NO:295	PAAARTAPPSAP	SEQ ID NO:330	AARTAPPSAPIGPHG
SEQ ID NO:296	AAARTAPPSAPI	SEQ ID NO:331	ARTAPPSAPIGPHGS
SEQ ID NO:297	AARTAPPSAPIG	SEQ ID NO:332	RTAPPSAPIGPHGSS
SEQ ID NO:298	ARTAPPSAPIGP	SEQ ID NO:333	TAPPSAPIGPHGSSN
SEQ ID NO:299	RTAPPSAPIGPH	SEQ ID NO:334	APPSAPIGPHGSSNT
SEQ ID NO:300	TAPPSAPIGPHG	SEQ ID NO:335	PPSAPIGPHGSSNTN
SEQ ID NO:301	APPSAPIGPHGS	SEQ ID NO:336	PSAP IGPHGSSNTNT
SEQ ID NO:302	PPSAPIGPHGSS	SEQ ID NO:337	AAPQPAAARTAPPSAP
SEQ ID NO:303	PSAP IGPHGSSN	SEQ ID NO:338	APQPAAARTAPPSAPI
SEQ ID NO:339	PQPAAARTAPPSAPIG	SEQ ID NO:378	PSAP IGPHGSSNTNTTTN
SEQ ID NO:340	QPAAARTAPPSAPIGP	SEQ ID NO:379	ASHAAPQPAAARTAPPSAP
SEQ ID NO:341	PAAARTAPPSAPIGPH	SEQ ID NO:380	SHAAPQPAAARTAPPSAPI
SEQ ID NO:342	AAARTAPPSAPIGPHG	SEQ ID NO:381	HAAPQPAAARTAPPSAPIG
SEQ ID NO:343	AARTAPPSAPIGPHGS	SEQ ID NO:382	AAPQPAAARTAPPSAPIGP
SEQ ID NO:344	ARTAPPSAPIGPHGSS	SEQ ID NO:383	APQPAAARTAPPSAPIGPH
SEQ ID NO:345	RTAPPSAPIGPHGSSN	SEQ ID NO:384	PQPAAARTAPPSAPIGPHG
SEQ ID NO:346	TAPPSAPIGPHGSSNT	SEQ ID NO:385	QPAAARTAPPSAPIGPHGS
SEQ ID NO:347	APPSAPIGPHGSSNTN	SEQ ID NO:386	PAAARTAPPSAPIGPHGSS
SEQ ID NO:348	PPSAPIGPHGSSNTNT	SEQ ID NO:387	AAARTAPPSAPIGPHGSSN
SEQ ID NO:349	PSAP IGPHGSSNTNTT	SEQ ID NO:388	AARTAPPSAPIGPHGSSNT
SEQ ID NO:350	HAAPQPAAARTAPPSAP	SEQ ID NO:389	ARTAPPSAPIGPHGSSNTN
SEQ ID NO:351	AAPQPAAARTAPPSAPI	SEQ ID NO:390	RTAPPSAPIGPHGSSNTNT
SEQ ID NO:352	APQPAAARTAPPSAPIG	SEQ ID NO:391	TAPPSAPIGPHGSSNTNTT
SEQ ID NO:353	PQPAAARTAPPSAPIGP	SEQ ID NO:392	APPSAPIGPHGSSNTNTTT
SEQ ID NO:354	QPAAARTAPPSAPIGPH	SEQ ID NO:393	PPSAPIGPHGSSNTNTTTN
SEQ ID NO:355	PAAARTAPPSAPIGPHG	SEQ ID NO:394	PSAP IGPHGSSNTNTTTNS
SEQ ID NO:356	AAARTAPPSAPIGPHGS	SEQ ID NO:395	GASHAAPQPAAARTAPPSAP
SEQ ID NO:357	AARTAPPSAPIGPHGSS	SEQ ID NO:396	ASHAAPQPAAARTAPPSAPI
SEQ ID NO:358	ARTAPPSAPIGPHGSSN	SEQ ID NO:397	SHAAPQPAAARTAPPSAPIG
SEQ ID NO:359	RTAPPSAPIGPHGSSNT	SEQ ID NO:398	HAAPQPAAARTAPPSAPIGP
SEQ ID NO:360	TAPPSAPIGPHGSSNTN	SEQ ID NO:399	AAPQPAAARTAPPSAPIGPH
SEQ ID NO:361	APPSAPIGPHGSSNTNT	SEQ ID NO:400	APQPAAARTAPPSAPIGPHG
SEQ ID NO:362	PPSAPIGPHGSSNTNTT	SEQ ID NO:401	PQPAAARTAPPSAPIGPHGS
SEQ ID NO:363	PSAP IGPHGSSNTNTTT	SEQ ID NO:402	QPAAARTAPPSAPIGPHGSS
SEQ ID NO:364	SHAAPQPAAARTAPPSAP	SEQ ID NO:403	PAAARTAPPSAPIGPHGSSN
SEQ ID NO:365	HAAPQPAAARTAPPSAPI	SEQ ID NO:404	AAARTAPPSAPIGPHGSSNT
SEQ ID NO:366	AAPQPAAARTAPPSAPIG	SEQ ID NO:405	AARTAPPSAPIGPHGSSNTN
SEQ ID NO:367	APQPAAARTAPPSAPIGP	SEQ ID NO:406	ARTAPPSAPIGPHGSSNTNT
SEQ ID NO:368	PQPAAARTAPPSAPIGPH	SEQ ID NO:407	RTAPPSAPIGPHGSSNTNTT
SEQ ID NO:369	QPAAARTAPPSAPIGPHG	SEQ ID NO:408	TAPPSAPIGPHGSSNTNTTT
SEQ ID NO:370	PAAARTAPPSAPIGPHGS	SEQ ID NO:409	APPSAPIGPHGSSNTNTTTN
SEQ ID NO:371	AAARTAPPSAPIGPHGSS	SEQ ID NO:410	PPSAPIGPHGSSNTNTTTNS
SEQ ID NO:372	AARTAPPSAPIGPHGSSN	SEQ ID NO:411	PSAP IGPHGSSNTNTTTNSS
SEQ ID NO:373	ARTAPPSAPIGPHGSSNT	SEQ ID NO:412	PPEYPTAP
SEQ ID NO:374	RTAPPSAPIGPHGSSNTN	SEQ ID NO:413	PEYPTAPA
SEQ ID NO:375	TAPPSAPIGPHGSSNTNT	SEQ ID NO:414	EYPTAPAS
SEQ ID NO:376	APPSAPIGPHGSSNTNTT	SEQ ID NO:415	YPTAPASE
SEQ ID NO:377	PPSAPIGPHGSSNTNTTT	SEQ ID NO:416	PTAP ASEW
SEQ ID NO:417	MPPEYPTAP	SEQ ID NO:456	PTAP ASEWNSLWM
SEQ ID NO:418	PPEYPTAPA	SEQ ID NO:457	AGNHVMPPEYPTAP
SEQ ID NO:419	PEYPTAPAS	SEQ ID NO:458	GNHVMPPEYPTAPA
SEQ ID NO:420	EYPTAPASE	SEQ ID NO:459	NHVMPPEYPTAPAS
SEQ ID NO:421	YPTAPASEW	SEQ ID NO:460	HVMPPEYPTAPASE
SEQ ID NO:422	PTAP ASEWN	SEQ ID NO:461	VMPPEYPTAPASEW
SEQ ID NO:423	VMPPEYPTAP	SEQ ID NO:462	MPPEYPTAPASEWN
SEQ ID NO:424	MPPEYPTAPA	SEQ ID NO:463	PPEYPTAPASEWNS
SEQ ID NO:425	PPEYPTAPAS	SEQ ID NO:464	PEYPTAPASEWNSL
SEQ ID NO:426	PEYPTAPASE	SEQ ID NO:465	EYPTAPASEWNSLW
SEQ ID NO:427	EYPTAPASEW	SEQ ID NO:466	YPTAPASEWNSLWM
SEQ ID NO:428	YPTAPASEWN	SEQ ID NO:467	PTAP ASEWNSLWMT
SEQ ID NO:429	PTAP ASEWNS	SEQ ID NO:468	TAGNHVMPPEYPTAP
SEQ ID NO:430	HVMPPEYPTAP	SEQ ID NO:469	AGNHVMPPEYPTAPA
SEQ ID NO:431	VMPPEYPTAPA	SEQ ID NO:470	GNHVMPPEYPTAPAS
SEQ ID NO:432	MPPEYPTAPAS	SEQ ID NO:471	NHVMPPEYPTAPASE
SEQ ID NO:433	PPEYPTAPASE	SEQ ID NO:472	HVMPPEYPTAPASEW
SEQ ID NO:434	PEYPTAPASEW	SEQ ID NO:473	VMPPEYPTAPASEWN
SEQ ID NO:435	EYPTAPASEWN	SEQ ID NO:474	MPPEYPTAPASEWNS
SEQ ID NO:436	YPTAPASEWNS	SEQ ID NO:475	PPEYPTAPASEWNSL
SEQ ID NO:437	PTAP ASEWNSL	SEQ ID NO:476	PEYPTAPASEWNSLW
SEQ ID NO:438	NHVMPPEYPTAP	SEQ ID NO:477	EYPTAPASEWNSLWM
SEQ ID NO:439	HVMPPEYPTAPA	SEQ ID NO:478	YPTAPASEWNSLWMT
SEQ ID NO:440	VMPPEYPTAPAS	SEQ ID NO:479	PTAP ASEWNSLWMTP
SEQ ID NO:441	MPPEYPTAPASE	SEQ ID NO:480	ETAGNHVMPPEYPTAP
SEQ ID NO:442	PPEYPTAPASEW	SEQ ID NO:481	TAGNHVMPPEYPTAPA
SEQ ID NO:443	PEYPTAPASEWN	SEQ ID NO:482	AGNHVMPPEYPTAPAS
SEQ ID NO:444	EYPTAPASEWNS	SEQ ID NO:483	GNHVMPPEYPTAPASE
SEQ ID NO:445	YPTAPASEWNSL	SEQ ID NO:484	NHVMPPEYPTAPASEW
SEQ ID NO:446	PTAP ASEWNSLW	SEQ ID NO:485	HVMPPEYPTAPASEWN
SEQ ID NO:447	GNHVMPPEYPTAP	SEQ ID NO:486	VMPPEYPTAPASEWNS
SEQ ID NO:448	NHVMPPEYPTAPA	SEQ ID NO:487	MPPEYPTAPASEWNSL
SEQ ID NO:449	HVMPPEYPTAPAS	SEQ ID NO:488	PPEYPTAPASEWNSLW
SEQ ID NO:450	VMPPEYPTAPASE	SEQ ID NO:489	PEYPTAPASEWNSLWM
SEQ ID NO:451	MPPEYPTAPASEW	SEQ ID NO:490	EYPTAPASEWNSLWMT
SEQ ID NO:452	PPEYPTAPASEWN	SEQ ID NO:491	YPTAPASEWNSLWMTP
SEQ ID NO:453	PEYPTAPASEWNS	SEQ ID NO:492	PTAP ASEWNSLWMTPV
SEQ ID NO:454	EYPTAPASEWNSL	SEQ ID NO:493	PETAGNHVMPPEYPTAP
SEQ ID NO:455	YPTAPASEWNSLW	SEQ ID NO:494	ETAGNHVMPPEYPTAPA
SEQ ID NO:495	TAGNHVMPPEYPTAPAS	SEQ ID NO:534	PEYPTAPASEWNSLWMTPV
SEQ ID NO:496	AGNHVMPPEYPTAPASE	SEQ ID NO:535	EYPTAPASEWNSLWMTPVG
SEQ ID NO:497	GNHVMPPEYPTAPASEW	SEQ ID NO:536	YPTAPASEWNSLWMTPVGN
SEQ ID NO:498	NHVMPPEYPTAPASEWN	SEQ ID NO:537	PTAP ASEWNSLWMTPVGNM
SEQ ID NO:499	HVMPPEYPTAPASEWNS	SEQ ID NO:538	TLLPETAGNHVMIPPEYPTAP
SEQ ID NO:500	VMPPEYPTAPASEWNSL	SEQ ID NO:539	LLPETAGNHVMPPEYPTAPA
SEQ ID NO:501	MPPEYPTAPASEWNSLW	SEQ ID NO:540	LPETAGNHVMPPEYPTAPAS
SEQ ID NO:502	PPEYPTAPASEWNSLWM	SEQ ID NO:541	PETAGNHVMPPEYPTAPASE
SEQ ID NO:503	PEYPTAPASEWNSLWMT	SEQ ID NO:542	ETAGNHVMPPEYPTAPASEW
SEQ ID NO:504	EYPTAPASEWNSLWMTP	SEQ ID NO:543	TAGNHVMPPEYPTAPASEWN
SEQ ID NO:505	YPTAPASEWNSLWMTPV	SEQ ID NO:544	AGNHVMPPEYPTAPASEWNS
SEQ ID NO:506	PTAP ASEWNSLWMTPVG	SEQ ID NO:545	GNHVMPPEYPTAPASEWNSL
SEQ ID NO:507	LPETAGNHVMPPEYPTAP	SEQ ID NO:546	NHVMPPEYPTAPASEWNSLW
SEQ ID NO:508	PETAGNHVMPPEYPTAPA	SEQ ID NO:547	HVMPPEYPTAPASEWNSLWM
SEQ ID NO:509	ETAGNHVMPPEYPTAPAS	SEQ ID NO:548	VMPPEYPTAPASEWNSLWMT
SEQ ID NO:510	TAGNHVMPPEYPTAPASE	SEQ ID NO:549	MPPEYPTAPASEWNSLWMTP
SEQ ID NO:511	AGNHVMPPEYPTAPASEW	SEQ ID NO:550	PPEYPTAPASEWNSLWMTPV
SEQ ID NO:512	GNHVMPPEYPTAPASEWN	SEQ ID NO:551	PEYPTAPASEWNSLWMTPVG
SEQ ID NO:513	NHVMPPEYPTAPASEWNS	SEQ ID NO:552	EYPTAPASEWNSLWMTPVGN
SEQ ID NO:514	HVMPPEYPTAPASEWNSL	SEQ ID NO:553	YPTAPASEWNSLWMTPVGNM
SEQ ID NO:515	VMPPEYPTAPASEWNSLW	SEQ ID NO:554	PTAP ASEWNSLWMTPVGNML
SEQ ID NO:516	MPPEYPTAPASEWNSLWM	SEQ ID NO:555	FLGPPTAP
SEQ ID NO:517	PPEYPTAPASEWNSLWMT	SEQ ID NO:556	LGPPTAPP
SEQ ID NO:518	PEYPTAPASEWNSLWMTP	SEQ ID NO:557	GPPTAPPG
SEQ ID NO:519	EYPTAPASEWNSLWMTPV	SEQ ID NO:558	PPTAPPGG
SEQ ID NO:520	YPTAPASEWNSLWMTPVG	SEQ ID NO:559	PTAP PGGA
SEQ ID NO:521	PTAP ASEWNSLWMTPVGN	SEQ ID NO:560	LFLGPPTAP
SEQ ID NO:522	LLPETAGNHVMPPEYPTAP	SEQ ID NO:561	FLGPPTAPP
SEQ ID NO:523	LPETAGNHVMPPEYPTAPA	SEQ ID NO:562	LGPPTAPPG
SEQ ID NO:524	PETAGNHVMPPEYPTAPAS	SEQ ID NO:563	GPPTAPPGG
SEQ ID NO:525	ETAGNHVMPPEYPTAPASE	SEQ ID NO:564	PPTAPPGGA
SEQ ID NO:526	TAGNHVMPPEYPTAPASEW	SEQ ID NO:565	PTAP PGGAW
SEQ ID NO:527	AGNHVMPPEYPTAPASEWN	SEQ ID NO:566	LLFLGPPTAP
SEQ ID NO:528	GNHVMPPEYPTAPASEWNS	SEQ ID NO:567	LFLGPPTAPP
SEQ ID NO:529	NHVMPPEYPTAPASEWNSL	SEQ ID NO:568	FLGPPTAPPG
SEQ ID NO:530	HVMPPEYPTAPASEWNSLW	SEQ ID NO:569	LGPPTAPPGG
SEQ ID NO:531	VMPPEYPTAPASEWNSLWM	SEQ ID NO:570	GPPTAPPGGA
SEQ ID NO:532	MPPEYPTAPASEWNSLWMT	SEQ ID NO:571	PPTAPPGGAW
SEQ ID NO:533	PPEYPTAPASEWNSLWMTP	SEQ ID NO:572	PTAP PGGAWT
SEQ ID NO:573	TLLFLGPPTAP	SEQ ID NO:612	INQTLLFLGPPTAPP
SEQ ID NO:574	LLFLGPPTAPP	SEQ ID NO:613	NQTLLFLGPPTAPPG
SEQ ID NO:575	LFLGPPTAPPG	SEQ ID NO:614	QTLLFLGPPTAPPGG
SEQ ID NO:576	FLGPPTAPPGG	SEQ ID NO:615	TLLFLGPPTAPPGGA
SEQ ID NO:577	LGPPTAPPGGA	SEQ ID NO:616	LLFLGPPTAPPGGAW
SEQ ID NO:578	GPPTAPPGGAW	SEQ ID NO:617	LFLGPPTAPPGGAWT
SEQ ID NO:579	PPTAPPGGAWT	SEQ ID NO:618	FLGPPTAPPGGAWTP
SEQ ID NO:580	PTAP PGGAWTP	SEQ ID NO:619	LGPPTAPPGGAWTPH
SEQ ID NO:581	QTLLFLGPPTAP	SEQ ID NO:620	GPPTAPPGGAWTPHA
SEQ ID NO:582	TLLFLGPPTAPP	SEQ ID NO:621	PPTAPPGGAWTPHAR
SEQ ID NO:583	LLFLGPPTAPPG	SEQ ID NO:622	PTAP PGGAWTPHARV
SEQ ID NO:584	LFLGPPTAPPGG	SEQ ID NO:623	MKINQTLLFLGPPTAP
SEQ ID NO:585	FLGPPTAPPGGA	SEQ ID NO:624	KINQTLLFLGPPTAPP
SEQ ID NO:586	LGPPTAPPGGAW	SEQ ID NO:625	INQTLLFLGPPTAPPG
SEQ ID NO:587	GPPTAPPGGAWT	SEQ ID NO:626	NQTLLFLGPPTAPPGG
SEQ ID NO:588	PPTAPPGGAWTP	SEQ ID NO:627	QTLLFLGPPTAPPGGA
SEQ ID NO:589	PTAP PGGAWTPH	SEQ ID NO:628	TLLFLGPPTAPPGGAW
SEQ ID NO:590	NQTLLFLGPPTAP	SEQ ID NO:629	LLFLGPPTAPPGGAWT
SEQ ID NO:591	QTLLFLGPPTAPP	SEQ ID NO:630	LFLGPPTAPPGGAWTP
SEQ ID NO:592	TLLFLGPPTAPPG	SEQ ID NO:631	FLGPPTAPPGGAWTPH
SEQ ID NO:593	LLFLGPPTAPPGG	SEQ ID NO:632	LGPPTAPPGGAWTPHA
SEQ ID NO:594	LFLGPPTAPPGGA	SEQ ID NO:633	GPPTAPPGGAWTPHAR
SEQ ID NO:595	FLGPPTAPPGGAW	SEQ ID NO:634	PPTAPPGGAWTPHARV
SEQ ID NO:596	LGPPTAPPGGAWT	SEQ ID NO:635	PTAP PGGAWTPHARVC
SEQ ID NO:597	GPPTAPPGGAWTP	SEQ ID NO:636	WMKINQTLLFLGPPTAP
SEQ ID NO:598	PPTAPPGGAWTPH	SEQ ID NO:637	MKINQTLLFLGPPTAPP
SEQ ID NO:599	PTAP PGGAWTPHA	SEQ ID NO:638	KINQTLLFLGPPTAPPG
SEQ ID NO:600	INQTLLFLGPPTAP	SEQ ID NO:639	INQTLLFLGPPTAPPGG
SEQ ID NO:601	NQTLLFLGPPTAPP	SEQ ID NO:640	NQTLLFLGPPTAPPGGA
SEQ ID NO:602	QTLLFLGPPTAPPG	SEQ ID NO:641	QTLLFLGPPTAPPGGAW
SEQ ID NO:603	TLLFLGPPTAPPGG	SEQ ID NO:642	TLLFLGPPTAPPGGAWT
SEQ ID NO:604	LLFLGPPTAPPGGA	SEQ ID NO:643	LLFLGPPTAPPGGAWTP
SEQ ID NO:605	LFLGPPTAPPGGAW	SEQ ID NO:644	LFLGPPTAPPGGAWTPH
SEQ ID NO:606	FLGPPTAPPGGAWT	SEQ ID NO:645	FLGPPTAPPGGAWTPHA
SEQ ID NO:607	LGPPTAPPGGAWTP	SEQ ID NO:646	LGPPTAPPGGAWTPHAR
SEQ ID NO:608	GPPTAPPGGAWTPH	SEQ ID NO:647	GPPTAPPGGAWTPHARV
SEQ ID NO:609	PPTAPPGGAWTPHA	SEQ ID NO:648	PPTAPPGGAWTPHARVC
SEQ ID NO:610	PTAP PGGAWTPHAR	SEQ ID NO:649	PTAP PGGAWTPHARVCY
SEQ ID NO:611	KINQTLLFLGPPTAP	SEQ ID NO:650	VWMKINQTLLFLGPPTAP
SEQ ID NO:651	WMKJNQTLLFLGPPTAPP	SEQ ID NO:675	LFLGPPTAPPGGAWTPHAR
SEQ ID NO:652	MKINQTLLFLGPPTAPPG	SEQ ID NO:676	FLGPPTAPPGGAWTPHARV
SEQ ID NO:653	KINQTLLFLGPPTAPPGG	SEQ ID NO:677	LGPPTAPPGGAWTPHARVC
SEQ ID NO:654	INQTLLFLGPPTAPPGGA	SEQ ID NO:678	GPPTAPPGGAWTPHARVCY
SEQ ID NO:655	NQTLLFLGPPTAPPGGAW	SEQ ID NO:679	PPTAPPGGAWTPHARVCYA
SEQ ID NO:656	QTLLFLGPPTAPPGGAWT	SEQ ID NO:680	PTAP PGGAWTPHARVCYAN
SEQ ID NO:657	TLLFLGPPTAPPGGAWTP	SEQ ID NO:681	ALVWMKINQTLLFLGPPTAP
SEQ ID NO:658	LLFLGPPTAPPGGAWTPH	SEQ ID NO:682	LVWMKINQTLLFLGPPTAPP
SEQ ID NO:659	LFLGPPTAPPGGAWTPHA	SEQ ID NO:683	VWMKINQTLLFLGPPTAPPG
SEQ ID NO:660	FLGPPTAPPGGAWTPHAR	SEQ ID NO:684	WMKINQTLLFLGPPTAPPGG
SEQ ID NO:661	LGPPTAPPGGAWTPHARV	SEQ ID NO:685	MKINQTLLFLGPPTAPPGGA
SEQ ID NO:662	GPPTAPPGGAWTPHARVC	SEQ ID NO:686	KINQTLLFLGPPTAPPGGAW
SEQ ID NO:663	PPTAPPGGAWTPHARVCY	SEQ ID NO:687	INQTLLFLGPPTAPPGGAWT
SEQ ID NO:664	PTAP PGGAWTPHARVCYA	SEQ ID NO:688	NQTLLFLGPPTAPPGGAWTP
SEQ ID NO:665	LVWMKINQTLLFLGPPTAP	SEQ ID NO:689	QTLLFLGPPTAPPGGAWTPH
SEQ ID NO:666	VWMKINQTLLFLGPPTAPP	SEQ ID NO:690	TLLFLGPPTAPPGGAWTPHA
SEQ ID NO:667	WMKINQTLLFLGPPTAPPG	SEQ ID NO:691	LLFLGPPTAPPGGAWTPHAR
SEQ ID NO:668	MKINQTLLFLGPPTAPPGG	SEQ ID NO:692	LFLGPPTAPPGGAWTPHARV
SEQ ID NO:669	KINQTLLFLGPPTAPPGGA	SEQ ID NO:693	FLGPPTAPPGGAWTPHARVC
SEQ ID NO:670	INQTLLFLGPPTAPPGGAW	SEQ ID NO:694	LGPPTAPPGGAWTPHARVCY
SEQ ID NO:671	NQTLLFLGPPTAPPGGAWT	SEQ ID NO:695	GPPTAPPGGAWTPHARVCYA
SEQ ID NO:672	QTLLFLGPPTAPPGGAWTP	SEQ ID NO:696	PPTAPPGGAWTPHARVCYAN
SEQ ID NO:673	TLLFLGPPTAPPGGAWTPH	SEQ ID NO:697	PTAP PGGAWTPHARVCYANI
SEQ ID NO:674	LLELGPPTAPPGGAWTPHA

[0151]

TABLE 5
P(T/S)AP Motif Containing Peptides from Human Herpesvirus 2
Virion Glycoprotein K
(GenBank Accession No. NP_044524)
SEQ ID NO:555	FLGPPTAP	SEQ ID NO:590	NQTLLFLGPPTAP
SEQ ID NO:556	LGPPTAPP	SEQ ID NO:591	QTLLFLGPPTAPP
SEQ ID NO:557	GPPTAPPG	SEQ ID NO:592	TLLFLGPPTAPPG
SEQ ID NO:558	PPTAPPGG	SEQ ID NO:593	LLFLGPPTAPPGG
SEQ ID NO:559	PTAP PGGA	SEQ ID NO:594	LFLGPPTAPPGGA
SEQ ID NO:560	LFLGPPTAP	SEQ ID NO:595	FLGPPTAPPGGAW
SEQ ID NO:561	FLGPPTAPP	SEQ ID NO:596	LGPPTAPPGGAWT
SEQ ID NO:562	LGPPTAPPG	SEQ ID NO:597	GPPTAPPGGAWTP
SEQ ID NO:563	GPPTAPPGG	SEQ ID NO:598	PPTAPPGGAWTPH
SEQ ID NO:564	PPTAPPGGA	SEQ ID NO:599	PTAP PGGAWTPHA
SEQ ID NO:565	PTAP PGGAW	SEQ ID NO:600	INQTLLFLGPPTAP
SEQ ID NO:566	LLFLGPPTAP	SEQ ID NO:601	NQTLLFLGPPTAPP
SEQ ID NO:567	LFLGPPTAPP	SEQ ID NO:602	QTLLFLGPPTAPPG
SEQ ID NO:568	FLGPPTAPPG	SEQ ID NO:603	TLLFLGPPTAPPGG
SEQ ID NO:569	LGPPTAPPGG	SEQ ID NO:604	LLFLGPPTAPPGGA
SEQ ID NO:570	GPPTAPPGGA	SEQ ID NO:605	LFLGPPTAPPGGAW
SEQ ID NO:571	PPTAPPGGAW	SEQ ID NO:606	FLGPPTAPPGGAWT
SEQ ID NO:572	PTAP PGGAWT	SEQ ID NO:607	LGPPTAPPGGAWTP
SEQ ID NO:573	TLLFLGPPTAP	SEQ ID NO:608	GPPTAPPGGAWTPH
SEQ ID NO:574	LLFLGPPTAPP	SEQ ID NO:609	PPTAPPGGAWTPHA
SEQ ID NO:575	LFLGPPTAPPG	SEQ ID NO:610	PTAP PGGAWTPHAR
SEQ ID NO:576	FLGPPTAPPGG	SEQ ID NO:611	KINQTLLFLGPPTAP
SEQ ID NO:577	LGPPTAPPGGA	SEQ ID NO:612	INQTLLFLGPPTAPP
SEQ ID NO:578	GPPTAPPGGAW	SEQ ID NO:613	NQTLLFLGPPTAPPG
SEQ ID NO:579	PPTAPPGGAWT	SEQ ID NO:614	QTLLFLGPPTAPPGG
SEQ ID NO:580	PTAP PGGAWTP	SEQ ID NO:615	TLLFLGPPTAPPGGA
SEQ ID NO:581	QTLLFLGPPTAP	SEQ ID NO:616	LLFLGPPTAPPGGAW
SEQ ID NO:582	TLLFLGPPTAPP	SEQ ID NO:617	LFLGPPTAPPGGAWT
SEQ ID NO:583	LLFLGPPTAPPG	SEQ ID NO:618	FLGPPTAPPGGAWTP
SEQ ID NO:584	LFLGPPTAPPGG	SEQ ID NO:619	LGPPTAPPGGAWTPH
SEQ ID NO:585	FLGPPTAPPGGA	SEQ ID NO:620	GPPTAPPGGAWTPHA
SEQ ID NO:586	LGPPTAPPGGAW	SEQ ID NO:621	PPTAPPGGAWTPHAR
SEQ ID NO:587	GPPTAPPGGAWT	SEQ ID NO:622	PTAP PGGAWTPHARV
SEQ ID NO:588	PPTAPPGGAWTP	SEQ ID NO:623	MKINQTLLFLGPPTAP
SEQ ID NO:589	PTAP PGGAWTPH	SEQ ID NO:624	KINQTLLFLGPPTAPP
SEQ ID NO:625	INQTLLFLGPPTAPPG	SEQ ID NO:662	GPPTAPPGGAWTPHARVC
SEQ ID NO:626	NQTLLFLGPPTAPPGG	SEQ ID NO:663	PPTAPPGGAWTPHARVCY
SEQ ID NO:627	QTLLFLGPPTAPPGGA	SEQ ID NO:664	PTAP PGGAWTPHARVCYA
SEQ ID NO:628	TLLFLGPPTAPPGGAW	SEQ ID NO:665	LVWMKINQTLLFLGPPTAP
SEQ ID NO:629	LLFLGPPTAPPGGAWT	SEQ ID NO:666	VWMKINQTLLFLGPPTAPP
SEQ ID NO:630	LFLGPPTAPPGGAWTP	SEQ ID NO:667	WMKINQTLLFLGPPTAPPG
SEQ ID NO:631	FLGPPTAPPGGAWTPH	SEQ ID NO:668	MKINQTLLFLGPPTAPPGG
SEQ ID NO:632	LGPPTAPPGGAWTPHA	SEQ ID NO:669	KINQTLLFLGPPTAPPGGA
SEQ ID NO:633	GPPTAPPGGAWTPHAR	SEQ ID NO:670	INQTLLFLGPPTAPPGGAW
SEQ ID NO:634	PPTAPPGGAWTPHARV	SEQ ID NO:671	NQTLLFLGPPTAPPGGAWT
SEQ ID NO:635	PTAP PGGAWTPHARVC	SEQ ID NO:672	QTLLFLGPPTAPPGGAWTP
SEQ ID NO:636	WMKINQTLLFLGPPTAP	SEQ ID NO:673	TLLFLGPPTAPPGGAWTPH
SEQ ID NO:637	MKINQTLLFLGPPTAPP	SEQ ID NO:674	LLFLGPPTAPPGGAWTPHA
SEQ ID NO:638	KINQTLLFLGPPTAPPG	SEQ ID NO:675	LFLGPPTAPPGGAWTPHAR
SEQ ID NO:639	INQTLLFLGPPTAPPGG	SEQ ID NO:676	FLGPPTAPPGGAWTPHARV
SEQ ID NO:640	NQTLLFLGPPTAPPGGA	SEQ ID NO:677	LGPPTAPPGGAWTPHARVC
SEQ ID NO:641	QTLLFLGPPTAPPGGAW	SEQ ID NO:678	GPPTAPPGGAWTPHARVCY
SEQ ID NO:642	TLLFLGPPTAPPGGAWT	SEQ ID NO:679	PPTAPPGGAWTPHARVCYA
SEQ ID NO:643	LLFLGPPTAPPGGAWTP	SEQ ID NO:680	PTAP PGGAWTPHARVCYAN
SEQ ID NO:644	LFLGPPTAPPGGAWTPH	SEQ ID NO:681	ALVWMKINQTLLFLGPPTAP
SEQ ID NO:645	FLGPPTAPPGGAWTPHA	SEQ ID NO:682	LVWMKINQTLLFLGPPTAPP
SEQ ID NO:646	LGPPTAPPGGAWTPHAR	SEQ ID NO:683	VWMKINQTLLFLGPPTAPPG
SEQ ID NO:647	GPPTAPPGGAWTPHARV	SEQ ID NO:684	WMKINQTLLFLGPPTAPPGG
SEQ ID NO:648	PPTAPPGGAWTPHARVC	SEQ ID NO:685	MKINQTLLFLGPPTAPPGGA
SEQ ID NO:649	PTAP PGGAWTPHARVCY	SEQ ID NO:686	KINQTLLFLGPPTAPPGGAW
SEQ ID NO:650	VWMKINQTLLFLGPPTAP	SEQ ID NO:687	INQTLLFLGPPTAPPGGAWT
SEQ ID NO:651	WMKINQTLLFLGPPTAPP	SEQ ID NO:688	NQTLLFLGPPTAPPGGAWTP
SEQ ID NO:652	MKINQTLLFLGPPTAPPG	SEQ ID NO:689	QTLLPLGPPTAPPGGAWTPH
SEQ ID NO:653	KINQTLLFLGPPTAPPGG	SEQ ID NO:690	TLLFLGPPTAPPGGAWTPHA
SEQ ID NO:654	INQTLLFLGPPTAPPGGA	SEQ ID NO:691	LLFLGPPTAPPGGAWTPHAR
SEQ ID NO:655	NQTLLFLGPPTAPPGGAW	SEQ ID NO:692	LFLGPPTAPPGGAWTPHARV
SEQ ID NO:656	QTLLFLGPPTAPPGGAWT	SEQ ID NO:693	FLGPPTAPPGGAWTPHARVC
SEQ ID NO:657	TLLFLGPPTAPPGGAWTP	SEQ ID NO:694	LGPPTAPPGGAWTPHARVCY
SEQ ID NO:658	LLFLGPPTAPPGGAWTPH	SEQ ID NO:695	GPPTAPPGGAWTPHARVCYA
SEQ ID NO:659	LFLGPPTAPPGGAWTPHA	SEQ ID NO:696	PPTAPPGGAWTPHARVCYAN
SEQ ID NO:660	FLGPPTAPPQGAWTPHAR	SEQ ID NO:697	PTAP PGGAWTPHARVCYANI
SEQ ID NO:661	LGPPTAPPGGAWTPHARV

[0152]

TABLE 6
P(T/S)AP Motif Containing Peptides from Human Herpesvirus 2
Strain 333 Glycoprotein I
(GenBank Accession No. P06764)
SEQ ID NO:698	PRSGPTAP	SEQ ID NO:724	VSPRPRSGPTAPQE
SEQ ID NO:699	RSGPTAPQ	SEQ ID NO:725	SPRPRSGPTAPQEV
SEQ ID NO:700	SGPTAPQE	SEQ ID NO:726	LLSVSPRPRSGPTAP
SEQ ID NO:701	GPTAPQEV	SEQ ID NO:727	LSVSPRPRSGPTAPQ
SEQ ID NO:702	RPRSGPTAP	SEQ ID NO:728	SVSPRPRSGPTAPQE
SEQ ID NO:703	PRSGPTAPQ	SEQ ID NO:729	VSPRPRSGPTAPQEV
SEQ ID NO:704	RSGPTAPQE	SEQ ID NO:730	VLLSVSPRPRSGPTAP
SEQ ID NO:705	SGPTAPQEV	SEQ ID NO:731	LLSVSPRPRSGPTAPQ
SEQ ID NO:706	PRPRSGPTAP	SEQ ID NO:732	LSVSPRPRSGPTAPQE
SEQ ID NO:707	RPRSGPTAPQ	SEQ ID NO:733	SVSPRPRSGPTAPQEV
SEQ ID NO:708	PRSGPTAPQE	SEQ ID NO:734	VVLLSVSPRPRSGPTAP
SEQ ID NO:709	RSGPTAPQEV	SEQ ID NO:735	VLLSVSPRPRSGPTAPQ
SEQ ID NO:710	SPRPRSGPTAP	SEQ ID NO:736	LLSVSPRPRSGPTAPQE
SEQ ID NO:711	PRPRSGPTAPQ	SEQ ID NO:737	LSVSPRPRSGPTAPQEV
SEQ ID NO:712	RPRSGPTAPQE	SEQ ID NO:738	PVVLLSVSPRPRSGPTAP
SEQ ID NO:713	PRSGPTAPQEV	SEQ ID NO:739	VVLLSVSPRPRSGPTAPQ
SEQ ID NO:714	VSPRPRSGPTAP	SEQ ID NO:740	VLLSVSPRPRSGPTAPQE
SEQ ID NO:715	SPRPRSGPTAPQ	SEQ ID NO:741	LLSVSPRPRSGPTAPQEV
SEQ ID NO:716	PRPRSGPTAPQE	SEQ ID NO:742	GPVVLLSVSPRPRSGPTAP
SEQ ID NO:717	RPRSGPTAPQEV	SEQ ID NO:743	PVVLLSVSPRPRSGPTAPQ
SEQ ID NO:718	SVSPRPRSGPTAP	SEQ ID NO:744	VVLLSVSPRPRSGPTAPQE
SEQ ID NO:719	VSPRPRSGPTAPQ	SEQ ID NO:745	VLLSVSPRPRSGPTAPQEV
SEQ ID NO:720	SPRPRSGPTAPQE	SEQ ID NO:746	PGPVVLLSVSPRPRSGPTAP
SEQ ID NO:721	PRPRSGPTAPQEV	SEQ ID NO:747	GPVVLLSVSPRPRSGPTAPQ
SEQ ID NO:722	LSVSPRPRSGPTAP	SEQ ID NO:748	PVVLLSVSPRPRSGPTAPQE
SEQ ID NO:723	SVSPRPRSGPTAPQ	SEQ ID NO:749	VVLLSVSPRPRSGPTAPQEV

[0153]

TABLE 7
P(T/S)AP Motif Containing Peptides from Human Herpesvirus 4/
Epstein Barr Virus BYRF1, Encodes EBNA-2 Protein
(GenBank Accession No. NP_039845)
SEQ ID NO:750	PPLRPTAP	SEQ ID NO:785	VQPHVPPLRPTAP
SEQ ID NO:751	PLRPTAPT	SEQ ID NO:786	QPHVPPLRPTAPT
SEQ ID NO:752	LRPTAPTI	SEQ ID NO:787	PHVPPLRPTAPTI
SEQ ID NO:753	RPTAPTIL	SEQ ID NO:788	HVPPLRPTAPTIL
SEQ ID NO:754	PTAP TILS	SEQ ID NO:789	VPPLRPTAPTILS
SEQ ID NO:755	VPPLRPTAP	SEQ ID NO:790	PPLRPTAPTILSP
SEQ ID NO:756	PPLRPTAPT	SEQ ID NO:791	PLRPTAPTILSPL
SEQ ID NO:757	PLRPTAPTI	SEQ ID NO:792	LRPTAPTILSPLS
SEQ ID NO:758	LRPTAPTIL	SEQ ID NO:793	RPTAPTTLSPLSQ
SEQ ID NO:759	RPTAPTILS	SEQ ID NO:794	PTAP TILSPLSQP
SEQ ID NO:760	PTAP TILSP	SEQ ID NO:795	LVQPHVPPLRPTAP
SEQ ID NO:761	HVPPLRPTAP	SEQ ID NO:796	VQPHVPPLRPTAPT
SEQ ID NO:762	VPPLRPTAPT	SEQ ID NO:797	QPHVPPLRPTAPTI
SEQ ID NO:763	PPLRPTAPTI	SEQ ID NO:798	PHVPPLRPTAPTIL
SEQ ID NO:764	PLRPTAPTIL	SEQ ID NO:799	HVPPLRPTAPTILS
SEQ ID NO:765	LRPTAPTILS	SEQ ID NO:800	VPPLRPTAPTILSP
SEQ ID NO:766	RPTAPTILSP	SEQ ID NO:801	PPLRPTAPTILSPL
SEQ ID NO:767	PTAP TILSPL	SEQ ID NO:802	PLRPTAPTILSPLS
SEQ ID NO:768	PHVPPLRPTAP	SEQ ID NO:803	LRPTAPTILSPLSQ
SEQ ID NO:769	HVPPLRPTAPT	SEQ ID NO:804	RPTAPTILSPLSQP
SEQ ID NO:770	VPPLRPTAPTI	SEQ ID NO:805	PTAP TILSPLSQPR
SEQ ID NO:771	PPLRPTAPTIL	SEQ ID NO:806	RLVQPHVPPLRPTAP
SEQ ID NO:772	PLRPTAPTILS	SEQ ID NO:807	LVQPHVPPLRPTAPT
SEQ ID NO:773	LRPTAPTILSP	SEQ ID NO:808	VQPHVPPLRPTAPTI
SEQ ID NO:774	RPTAPTILSPL	SEQ ID NO:809	QPHVPPLRPTAPTIL
SEQ ID NO:775	PTAP TILSPLS	SEQ ID NO:810	PHVPPLRPTAPTILS
SEQ ID NO:776	QPHVPPLRPTAP	SEQ ID NO:811	HVPPLRPTAPTILSP
SEQ ID NO:777	PHVPPLRPTAPT	SEQ ID NO:812	VPPLRPTAPTILSPL
SEQ ID NO:778	HVPPLRPTAPTI	SEQ ID NO:813	PPLRPTAPTILSPLS
SEQ ID NO:779	VPPLRPTAPTIL	SEQ ID NO:814	PLRPTAPTILSPLSQ
SEQ ID NO:780	PPLRPTAPTILS	SEQ ID NO:815	LRPTAPTILSPLSQP
SEQ ID NO:781	PLRPTAPTILSP	SEQ ID NO:816	RPTAPTTLSPLSQPR
SEQ ID NO:782	LRPTAPTILSPL	SEQ ID NO:817	PTAP TILSPLSQPRL
SEQ ID NO:783	RPTAPTILSPLS	SEQ ID NO:818	ARLVQPHVPPLRPTAP
SEQ ID NO:784	PTAP TILSPLSQ	SEQ ID NO:819	RLVQPHVPPLRPTAPT
SEQ ID NO:820	LVQPHVPPLRPTAPTI	SEQ ID NO:857	LRPTAPTILSPLSQPRLT
SEQ ID NO:821	VQPHVPPLRPTAPTIL	SEQ ID NO:858	RPTAPTLLSPLSQPRLTP
SEQ ID NO:822	QPHVPPLRPTAPTILS	SEQ ID NO:859	PTAP TILSPLSQPRLTPP
SEQ ID NO:823	PHVPPLRPTAPTILSP	SEQ ID NO:860	APQARLVQPHVPPLRPTAP
SEQ ID NO:824	HVPPLRPTAPTILSPL	SEQ ID NO:861	PQARLVQPHVPPLRPTAPT
SEQ ID NO:825	VPPLRPTAPTILSPLS	SEQ ID NO:862	QARLVQPHVPPLRPTAPTI
SEQ ID NO:826	PPLRPTAPTILSPLSQ	SEQ ID NO:863	ARLVQPHVPPLRPTAPTIL
SEQ ID NO:827	PLRPTAPTILSPLSQP	SEQ ID NO:864	RLVQPHVPPLRPTAPTILS
SEQ ID NO:828	LRPTAPTILSPLSQPR	SEQ ID NO:865	LVQPHVPPLRPTAPTILSP
SEQ ID NO:829	RPTAPTILSPLSQPRL	SEQ ID NO:866	VQPHVPPLRPTAPTILSPL
SEQ ID NO:830	PTAP TILSPLSQPRLT	SEQ ID NO:867	QPHVPPLRPTAPTILSPLS
SEQ ID NO:831	QARLVQPHVPPLRPTAP	SEQ ID NO:868	PHVPPLRPTAPTILSPLSQ
SEQ ID NO:832	ARLVQPHVPPLRPTAPT	SEQ ID NO:869	HVPPLRPTAPTILSPLSQP
SEQ ID NO:833	RLVQPHVPPLRPTAPTI	SEQ ID NO:870	VPPLRPTAPTILSPLSQPR
SEQ ID NO:834	LVQPHVPPLRPTAPTIL	SEQ ID NO:871	PPLRPTAPTILSPLSQPRL
SEQ ID NO:835	VQPHVPPLRPTAPTILS	SEQ ID NO:872	PLRPTAPTILSPLSQPRLT
SEQ ID NO:836	QPHVPPLRPTAPTILSP	SEQ ID NO:873	LRPTAPTILSPLSQPRLTP
SEQ ID NO:837	PHVPPLRPTAPTILSPL	SEQ ID NO:874	RPTAPTILSPLSQPRLTPP
SEQ ID NO:838	HVPPLRPTAPTISPLS	SEQ ID NO:875	PTAP TILSPLSQPRLTPPQ
SEQ ID NO:839	VPPLRPTAPTILSPLSQ	SEQ ID NO:876	TAPQARLVQPHVPPLRPTAP
SEQ ID NO:840	PPLRPTAPTILSPLSQP	SEQ ID NO:877	APQARLVQPHVPPLRPTAPT
SEQ ID NO:841	PLRPTAPTILSPLSQPR	SEQ ID NO:878	PQARLVQPHVPPLRPTAPTI
SEQ ID NO:842	LRPTAPTILSPLSQPRL	SEQ ID NO:879	QARLVQPHVPPLRPTAPTIL
SEQ ID NO:843	RPTAPTILSPLSQPRLT	SEQ ID NO:880	ARLVQPHVPPLRPTAPTILS
SEQ ID NO:844	PTAP TLLSPLSQPRLTP	SEQ ID NO:881	RLVQPHVPPLRPTAPTILSP
SEQ ID NO:845	PQARLVQPHVPPLRPTAP	SEQ ID NO:882	LVQPHVPPLRPTAPTTLSPL
SEQ ID NO:846	QARLVQPHVPPLRPTAPT	SEQ ID NO:883	VQPHVPPLRPTAPTILSPLS
SEQ ID NO:847	ARLVQPHVPPLRPTAPTI	SEQ ID NO:884	QPHVPPLRPTAPTILSPLSQ
SEQ ID NO:848	RLVQPHVPPLRPTAPTIL	SEQ ID NO:885	PHVPPLRPTAPTILSPLSQP
SEQ ID NO:849	LVQPHVPPLRPTAPTILS	SEQ ID NO:886	HVPPLRPTAPTILSPLSQPR
SEQ ID NO:850	VQPHVPPLRPTAPTILSP	SEQ ID NO:887	VPPLRPTAPTILSPLSQPRL
SEQ ID NO:851	QPHVPPLRPTAPTILSPL	SEQ ID NO:888	PPLRPTAPTILSPLSQPRLT
SEQ ID NO:852	PHVPPLRPTAPTILSPLS	SEQ ID NO:889	PLRPTAPTILSPLSQPRLTP
SEQ ID NO:853	HVPPLRPTAPTILSPLSQ	SEQ ID NO:890	LRPTAPTILSPLSQPRLTPP
SEQ ID NO:854	VPPLRPTAPTILSPLSQP	SEQ ID NO:891	RPTAPTILSPLSQPRLTPPQ
SEQ ID NO:855	PPLRPTAPTILSPLSQPR	SEQ ID NO:892	PTAP TILSPLSQPRLTPPQP
SEQ ID NO:856	PLRPTAPTILSPLSQPRL

[0154]

TABLE 8
PT/S)AP Motif Containing Peptides from Influenza A Virus
(A/Pintail Duck/Alberta/114/7(H8N4))
(GenBank Accession No. AAG38554)
SEQ ID NO:893	LVERPSAP	SEQ ID NO:928	QGWSYIVERPSAP
SEQ ID NO:894	VERPSAPE	SEQ ID NO:929	GWSYIVERPSAPE
SEQ ID NO:895	ERPSAPEG	SEQ ID NO:930	WSYIVERPSAPEG
SEQ ID NO:896	RPSAPEGM	SEQ ID NO:931	SYIVERPSAPEGM
SEQ ID NO:897	PSAP EGMC	SEQ ID NO:932	YIVERPSAPEGMC
SEQ ID NO:898	YIVERPSAP	SEQ ID NO:933	IVERPSAPEGMCY
SEQ ID NO:899	IVERPSAPE	SEQ ID NO:934	VERPSAPEGMCYP
SEQ ID NO:900	VERPSAPEG	SEQ ID NO:935	ERPSAPEGMCYPG
SEQ ID NO:901	ERPSAPEGM	SEQ ID NO:936	RPSAPEGMCYPGS
SEQ ID NO:902	RPSAPEGMC	SEQ ID NO:937	PSAP EGMCYPGSI
SEQ ID NO:903	PSAP EGMCY	SEQ ID NO:938	DQGWSYIVERPSAP
SEQ ID NO:904	SYIVERPSAP	SEQ ID NO:939	QGWSYIVERPSAPE
SEQ ID NO:905	YIVERPSAPE	SEQ ID NO:940	GWSYIVERPSAPEG
SEQ ID NO:906	IVERPSAPEG	SEQ ID NO:941	WSYIVERPSAPEGM
SEQ ID NO:907	VERPSAPEGM	SEQ ID NO:942	SYIVERPSAPEGMC
SEQ ID NO:908	ERPSAPEGMC	SEQ ID NO:943	YIVERPSAPEGMCY
SEQ ID NO:909	RPSAPEGMCY	SEQ ID NO:944	IVERPSAPEGMCYP
SEQ ID NO:910	PSAP EGMCYP	SEQ ID NO:945	VERPSAPEGMCYPG
SEQ ID NO:911	WSYIVERPSAP	SEQ ID NO:946	ERPSAPEGMCYPGS
SEQ ID NO:912	SYIVERPSAPE	SEQ ID NO:947	RPSAPEGMCYPGSI
SEQ ID NO:913	YIVERPSAPEG	SEQ ID NO:948	PSAP EGMCYPGSIE
SEQ ID NO:914	IVERPSAPEGM	SEQ ID NO:949	KDQGWSYIVERPSAP
SEQ ID NO:915	VERPSAPEGMC	SEQ ID NO:950	DQGWSYIVERPSAPE
SEQ ID NO:916	ERPSAPEGMCY	SEQ ID NO:951	QGWSYIVERPSAPEG
SEQ ID NO:917	RPSAPEGMCYP	SEQ ID NO:952	GWSYLVERPSAPEGM
SEQ ID NO:918	PSAP EGMCYPG	SEQ ID NO:953	WSYIVERPSAPEGMC
SEQ ID NO:919	GWSYIVERPSAP	SEQ ID NO:954	SYIVERPSAPEGMCY
SEQ ID NO:920	WSYIVERPSAPE	SEQ ID NO:955	YIVERPSAPEGMCYP
SEQ ID NO:921	SYIVERPSAPEG	SEQ ID NO:956	IVERPSAPEGMCYPG
SEQ ID NO:922	YIVERPSAPEGM	SEQ ID NO:957	VERPSAPEOMCYPGS
SEQ ID NO:923	IVERPSAPEGMC	SEQ ID NO:958	ERPSAPEGMCYPGSI
SEQ ID NO:924	VERPSAPEGMCY	SEQ ID NO:959	RPSAPEGMCYPGSIE
SEQ ID NO:925	ERPSAPEGMCYP	SEQ ID NO:960	PSAP EGMCYPGSIEN
SEQ ID NO:926	RPSAPEGMCYPG	SEQ ID NO:961	LKDQGWSYIVERPSAP
SEQ ID NO:927	PSAP EGMCYPGS	SEQ ID NO:962	KDQGWSYIVERPSAPE
SEQ ID NO:963	DQGWSYIVERPSAPEG	SEQ ID NO:1000	ERPSAPEGMCYPGSIENL
SEQ ID NO:964	QGWSYIVERPSAPEGM	SEQ ID NO:1001	RPSAPEGMCYPGSIENLE
SEQ ID NO:965	GWSYIVERPSAPEGMC	SEQ ID NO:1002	PSAP EGMCYPGSIENLEE
SEQ ID NO:966	WSYIVERPSAPEGMCY	SEQ ID NO:1003	DIHLKDQGWSYIVERPSAP
SEQ ID NO:967	SYIVERPSAPEGMCYP	SEQ ID NO:1004	IHLKDQGWSYIVERPSAPE
SEQ ID NO:968	YIVERPSAPEGMCYPG	SEQ ID NO:1005	HLKDQGWSYIVERPSAPEG
SEQ ID NO:969	IVERPSAPEGMCYPGS	SEQ ID NO:1006	LKDQGWSYIVERPSAPEGM
SEQ ID NO:970	VERPSAPEGMCYPGSI	SEQ ID NO:1007	KDQGWSYIVERPSAPEGMC
SEQ ID NO:971	ERPSAPEGMCYPGSIE	SEQ ID NO:1008	DQGWSYIVERPSAPEGMCY
SEQ ID NO:972	RPSAPEGMCYPGSIEN	SEQ ID NO:1009	QGWSYIVERPSAPEGMCYP
SEQ ID NO:973	PSAP EGMCYPGSIENL	SEQ ID NO:1010	GWSYIVERPSAPEGMCYPG
SEQ ID NO:974	HLKDQGWSYIVERPSAP	SEQ ID NO:1011	WSYIVERPSAPEGMCYPGS
SEQ ID NO:975	LKDQGWSYIVERPSAPE	SEQ ID NO:1012	SYIVERPSAPEGMCYPGSI
SEQ ID NO:976	KDQGWSYIVERPSAPEG	SEQ ID NO:1013	YIVERPSAPEGMCYPGSIE
SEQ ID NO:977	DQGWSYIVERPSAPEGM	SEQ ID NO:1014	IVERPSAPEGMCYPGSIEN
SEQ ID NO:978	QGWSYIVERPSAPEGMC	SEQ ID NO:1015	VERPSAPEGMCYPGSIENL
SEQ ID NO:979	GWSYIVERPSAPEGMCY	SEQ ID NO:1016	ERPSAPEGMCYPGSIENLE
SEQ ID NO:980	WSYIVERPSAPEGMCYP	SEQ ID NO:1017	RPSAPEGMCYPGSIENLEE
SEQ ID NO:981	SYIVERPSAPEGMCYPG	SEQ ID NO:1018	PSAP EGMCYPGSIENLEEL
SEQ ID NO:982	YIVERPSAPEGMCYPGS	SEQ ID NO:1019	CDIHLKDQGWSYIVERPSAP
SEQ ID NO:983	IVERPSAPEGMCYPGSI	SEQ ID NO:1020	DIHLKDQGWSYIVERPSAPE
SEQ ID NO:984	VERPSAPEGMCYPGSIE	SEQ ID NO:1021	IHLKDQGWSYIVERPSAPEG
SEQ ID NO:985	ERPSAPEGMCYPGSIEN	SEQ ID NO:1022	HLKDQGWSYIVERPSAPEGM
SEQ ID NO:986	RPSAPEGMCYPGSIENL	SEQ ID NO:1023	LKDQGWSYIVERPSAPEGMC
SEQ ID NO:987	PSAP EGMCYPGSIENLE	SEQ ID NO:1024	KDQGWSYIVERPSAPEGMCY
SEQ ID NO:988	IHLKDQGWSYIVERPSAP	SEQ ID NO:1025	DQGWSYIVERPSAPEGMCYP
SEQ ID NO:989	HLKDQGWSYIVERPSAPE	SEQ ID NO:1026	QGWSYIVERPSAPEGMCYPG
SEQ ID NO:990	LKDQGWSYIVERPSAPEG	SEQ ID NO:1027	GWSYIVERPSAPEGMCYPGS
SEQ ID NO:991	KDQGWSYIVERPSAPEGM	SEQ ID NO:1028	WSYIVERPSAPEGMCYPGSI
SEQ ID NO:992	DQGWSYIVERPSAPEGMC	SEQ ID NO:1029	SYIVERPSAPEGMCYPGSIE
SEQ ID NO:993	QGWSYIVERPSAPEGMCY	SEQ ID NO:1030	YIVERPSAPEGMCYPGSIEN
SEQ ID NO:994	GWSYIVERPSAPEGMCYP	SEQ ID NO:1031	IVERPSAPEGMCYPGSIENL
SEQ ID NO:995	WSYIVERPSAPEGMCYPG	SEQ ID NO:1032	VERPSAPEGMCYPGSIENLE
SEQ ID NO:996	SYIVERPSAPEGMCYPGS	SEQ ID NO:1033	ERPSAPEGMCYPGSIENLEE
SEQ ID NO:997	YIVERPSAPEGMCYPGSI	SEQ ID NO:1034	RPSAPEGMCYPGSIENLEEL
SEQ ID NO:998	IVERPSAPEGMCYPGSIE	SEQ ID NO:1035	PSAP EGMCYPGSIENLEELR
SEQ ID NO:999	VERPSAPEGMCYPGSIEN

[0155]

TABLE 9
P(T/S)AP Motif Containing Peptides from Human Papillomavirus
L1 Protein, My09/My11 Region
(GenBank Accession No. AAA67231)
SEQ ID NO:1036	CQKGPSAP	SEQ ID NO:1070	PSAP APKKDPYD
SEQ ID NO:1037	QKGPSAPA	SEQ ID NO:1071	SRAITCQKGPSAP
SEQ ID NO:1038	KGPSAPAP	SEQ ID NO:1072	RAITCQKGPSAPA
SEQ ID NO:1039	GPSAPAPK	SEQ ID NO:1073	AITCQKGPSAPAP
SEQ ID NO:1040	PSAP APKK	SEQ ID NO:1074	ITCQKGPSAPAPK
SEQ ID NO:1041	TCQKGPSAP	SEQ ID NO:1075	TCQKGPSAPAPKK
SEQ ID NO:1042	CQKGPSAPA	SEQ ID NO:1076	CQKGPSAPAPKKD
SEQ ID NO:1043	QKGPSAPAP	SEQ ID NO:1077	QKGPSAPAPKKDP
SEQ ID NO:1044	KGPSAPAPK	SEQ ID NO:1078	KGPSAPAPKKDPY
SEQ ID NO:1045	GPSAPAPKK	SEQ ID NO:1079	GPSAPAPKKDPYD
SEQ ID NO:1046	PSAP APKKD	SEQ ID NO:1080	PSAP APKKDPYDG
SEQ ID NO:1047	ITCQKGPSAP	SEQ ID NO:1081	QSRAITCQKGPSAP
SEQ ID NO:1048	TCQKGPSAPA	SEQ ID NO:1082	SRAITCQKGPSAPA
SEQ ID NO:1049	CQKGPSAPAP	SEQ ID NO:1083	RAITCQKGPSAPAP
SEQ ID NO:1050	QKGPSAPAPK	SEQ ID NO:1084	AITCQKGPSAPAPK
SEQ ID NO:1051	KGPSAPAPKK	SEQ ID NO:1085	ITCQKGPSAPAPKK
SEQ ID NO:1052	GPSAPAPKKD	SEQ ID NO:1086	TCQKGPSAPAPKKD
SEQ ID NO:1053	PSAP APKKDP	SEQ ID NO:1087	CQKGPSAPAPKKDP
SEQ ID NO:1054	AITCQKGPSAP	SEQ ID NO:1088	QKGPSAPAPKKDPY
SEQ ID NO:1055	ITCQKGPSAPA	SEQ ID NO:1089	KGPSAPAPKKDPYD
SEQ ID NO:1056	TCQKGPSAPAP	SEQ ID NO:1090	GPSAPAPKKDPYDG
SEQ ID NO:1057	CQKGPSAPAPK	SEQ ID NO:1091	PSAP APKKDPYDGL
SEQ ID NO:1058	QKGPSAPAPKK	SEQ ID NO:1092	LQSRAITCQKGPSAP
SEQ ID NO:1059	KGPSAPAPKKD	SEQ ID NO:1093	QSRAITCQKGPSAPA
SEQ ID NO:1060	GPSAPAPKKDP	SEQ ID NO:1094	SRAITCQKGPSAPAP
SEQ ID NO:1061	PSAP APKKDPY	SEQ ID NO:1095	RAITCQKGPSAPAPK
SEQ ID NO:1062	RAITCQKGPSAP	SEQ ID NO:1096	AITCQKGPSAPAPKK
SEQ ID NO:1063	AITCQKGPSAPA	SEQ ID NO:1097	ITCQKGPSAPAPKKD
SEQ ID NO:1064	ITCQKGPSAPAP	SEQ ID NO:1098	TCQKGPSAPAPKKDP
SEQ ID NO:1065	TCQKGPSAPAPK	SEQ ID NO:1099	CQKGPSAPAPKKDPY
SEQ ID NO:1066	CQKGPSAPAPKK	SEQ ID NO:1100	QKGPSAPAPKKDPYD
SEQ ID NO:1067	QKGPSAPAPKKD	SEQ ID NO:1101	KGPSAPAPKKDPYDG
SEQ ID NO:1068	KGPSAPAPKKDP	SEQ ID NO:1102	GPSAPAPKKDPYDGL
SEQ ID NO:1069	GPSAPAPKKDPY	SEQ ID NO:1103	PSAP APKKDPYDGLV
SEQ ID NO:1104	YLQSRAITCQKGPSAP	SEQ ID NO:1142	QKGPSAPAPKKDPYDGLV
SEQ ID NO:1105	LQSRAITCQKGPSAPA	SEQ ID NO:1143	KGPSAPAPKKDPYDGLVF
SEQ ID NO:1106	QSRAITCQKGPSAPAP	SEQ ID NO:1144	GPSAPAPKKDPYDGLVFW
SEQ ID NO:1107	SRAITCQKGPSAPAPK	SEQ ID NO:1145	PSAP APKKDPYDGLVFWE
SEQ ID NO:1108	RAITCQKGPSAPAPKK	SEQ ID NO:1146	TYRYLQSRAITCQKGPSAP
SEQ ID NO:1109	AITCQKGPSAPAPKKD	SEQ ID NO:1147	YRYLQSRAITCQKGPSAPA
SEQ ID NO:1110	ITCQKGPSAPAPKKDP	SEQ ID NO:1148	RYLQSRAITCQKGPSAPAP
SEQ ID NO:1111	TCQKGPSAPAPKKDPY	SEQ ID NO:1149	YLQSRAITCQKGPSAPAPK
SEQ ID NO:1112	CQKGPSAPAPKKDPYD	SEQ ID NO:1150	LQSRAITCQKGPSAPAPKK
SEQ ID NO:1113	QKGPSAPAPKKDPYDG	SEQ ID NO:1151	QSRAITCQKGPSAPAPKKD
SEQ ID NO:1114	KGPSAPAPKKDPYDGL	SEQ ID NO:1152	SRAITCQKGPSAPAPKKDP
SEQ ID NO:1115	GPSAPAPKKDPYDGLV	SEQ ID NO:1153	RAITCQKGPSAPAPKKDPY
SEQ ID NO:1116	PSAP APKKDPYDGLVF	SEQ ID NO:1154	AITCQKGPSAPAPKKDPYD
SEQ ID NO:1117	RYLQSRAITCQKGPSAP	SEQ ID NO:1155	ITCQKGPSAPAPKKDPYDG
SEQ ID NO:1118	YLQSRAITCQKGPSAPA	SEQ ID NO:1156	TCQKGPSAPAPKKDPYDGL
SEQ ID NO:1119	LQSRAITCQKGPSAPAP	SEQ ID NO:1157	CQKGPSAPAPKKDPYDGLV
SEQ ID NO:1120	QSRAITCQKGPSAPAPK	SEQ ID NO:1158	QKGPSAPAPKKDPYDGLVF
SEQ ID NO:1121	SRAITCQKGPSAPAPKK	SEQ ID NO:1159	KGPSAPAPKKDPYDGLVFW
SEQ ID NO:1122	RAITCQKGPSAPAPKKD	SEQ ID NO:1160	GPSAPAPKKDPYDGLVFWE
SEQ ID NO:1123	AITCQKGPSAPAPKKDP	SEQ ID NO:1161	PSAP APKKDPYDGLVFWEV
SEQ ID NO:1124	ITCQKGPSAPAPKKDPY	SEQ ID NO:1162	DTYRYLQSRAITCQKGPSAP
SEQ ID NO:1125	TCQKGPSAPAPKKDPYD	SEQ ID NO:1163	TYRYLQSRAITCQKGPSAPA
SEQ ID NO:1126	CQKGPSAPAPKKDPYDG	SEQ ID NO:1164	YRYLQSRAITCQKGPSAPAP
SEQ ID NO:1127	QKGPSAPAPKKDPYDGL	SEQ ID NO:1165	RYLQSRAITCQKGPSAPAPK
SEQ ID NO:1128	KGPSAPAPKKDPYDGLV	SEQ ID NO:1166	YLQSRAITCQKGPSAPAPKK
SEQ ID NO:1129	GPSAPAPKKDPYDGLVF	SEQ ID NO:1167	LQSRAITCQKGPSAPAPKKD
SEQ LD NO:1130	PSAP APKKDPYDGLVFW	SEQ ID NO:1168	QSRAITCQKGPSAPAPKKDP
SEQ ID NO:1131	YRYLQSRAITCQKGPSAP	SEQ ID NO:1169	SRAITCQKGPSAPAPKKDPY
SEQ ID NO:1132	RYLQSRAITCQKGPSAPA	SEQ ID NO:1170	RAITCQKGPSAPAPKKDPYD
SEQ ID NO:1133	YLQSRAITCQKGPSAPAP	SEQ ID NO:1171	AITCQKGPSAPAPKKDPYDG
SEQ ID NO:1134	LQSRAITCQKGPSAPAPK	SEQ ID NO:1172	ITCQKGPSAPAPKKDPYDGL
SEQ ID NO:1135	QSRAITCQKGPSAPAPKK	SEQ ID NO:1173	TCQKGPSAPAPKKDPYDGLV
SEQ ID NO:1136	SRAITCQKGPSAPAPKKD	SEQ ID NO:1174	CQKGPSAPAPKKDPYDGLVF
SEQ ID NO:1137	RAITCQKGPSAPAPKKDP	SEQ ID NO:1175	QKGPSAPAPKKDPYDGLVFW
SEQ ID NO:1138	AITCQKGPSAPAPKKDPY	SEQ ID NO:1176	KGPSAPAPKKDPYDGLVFWE
SEQ ID NO:1139	ITCQKGPSAPAPKKDPYD	SEQ ID NO:1177	GPSAPAPKKDPYDGLVFWEV
SEQ ID NO:1140	TCQKGPSAPAPKKDPYDG	SEQ ID NO:1178	PSAP APKKDPYDGLVFWEVD
SEQ ID NO:1141	CQKGPSAPAPKKDPYDGL

[0156]

TABLE 10
P(T/S)AP Motif Containing Peptides from Human Papillomavirus Type 23
Minor Capsid Protein L2
(GenBank Accession No. NP_043365)
SEQ ID NO:1179	IFPLPSAP	SEQ ID NO:1214		ERPTIIFPLPSAP
SEQ ID NO:1180	FPLPSAPA	SEQ ID NO:1215	RPTIIFPLPSAPA
SEQ ID NO:1181	PLPSAPAV	SEQ ID NO:1216	PTIIFPLPSAPAV
SEQ ID NO:1182	LPSAPAVV	SEQ ID NO:1217	TIIEPLPSAPAVV
SEQ ID NO:1183	PSAPAVVI	SEQ ID NO:1218	IIFPLPSAPAVVI
SEQ ID NO:1184	IIFPLPSAP	SEQ ID NO:1219	IFPLPSAPAVVIH
SEQ ID NO:1185	ILPLPSAPA	SEQ ID NO:1220	FPLPSAPAVVIHT
SEQ ID NO:1186	FPLPSAPAV	SEQ ID NO:1221	PLPSAPAVVIHTL
SEQ ID NO:1187	PLPSAPAVV	SEQ ID NO:1222	LPSAPAVVIHTLD
SEQ ID NO:1188	LPSAPAVVI	SEQ ID NO:1223	PSAPAVVIHTLDK
SEQ ID NO:1189	PSAPAVVIH	SEQ ID NO:1224	TERPTIIFPLPSAP
SEQ ID NO:1190	TIIFPLPSAP	SEQ ID NO:1225	ERPTIIFPLPSAPA
SEQ ID NO:1191	IIFPLPSAPA	SEQ ID NO:1226	RPTIIFPLPSAPAV
SEQ ID NO:1192	IFPLPSAPAV	SEQ ID NO:1227	PTIIFPLPSAPAVV
SEQ ID NO:1193	FPLPSAPAVV	SEQ ID NO:1228	TIIFPLPSAPAVVI
SEQ ID NO:1194	PLPSAPAVVI	SEQ ID NO:1229	IIFPLPSAPAVVIH
SEQ ID NO:1195	LPSAPAVVIH	SEQ ID NO:1230	IFPLPSAPAVVIHT
SEQ ID NO:1196	PSAPAVVIHT	SEQ ID NO:1231	FPLPSAPAVVIHTL
SEQ ID NO:1197	PTIIEPLPSAP	SEQ ID NO:1232	PLPSAPAVVIHTLD
SEQ ID NO:1198	TIIFPLPSAPA	SEQ ID NO:1233	LPSAPAVVIHTLDK
SEQ ID NO:1199	IIFPLPSAPAV	SEQ ID NO:1234	PSAPAVVIHTLDKS
SEQ ID NO:1200	IFPLPSAPAVV	SEQ ID NO:1235	PTERPTIIFPLPSAP
SEQ ID NO:1201	FPLPSAPAVVI	SEQ ID NO:1236	TERPTIIFPLPSAPA
SEQ ID NO:1202	PLPSAPAVVIH	SEQ ID NO:1237	ERPTIIFPLPSAPAV
SEQ ID NO:1203	LPSAPAVVIHT	SEQ ID NO:1238	RPTIIFPLPSAPAVV
SEQ ID NO:1204	PSAPAVVIHTL	SEQ ID NO:1239	PTIIFPLPSAPAVVI
SEQ ID NO:1205	RPTIIFPLPSAP	SEQ ID NO:1240	TIIFPLPSAPAVVIH
SEQ ID NO:1206	PTIIFPLPSAPA	SEQ ID NO:1241	IIFPLPSAPAVVIHT
SEQ ID NO:1207	TIIFPLPSAPAV	SEQ ID NO:1242	IFPLPSAPAVVIHTL
SEQ ID NO:1208	IWFPLPSAPAVV	SEQ ID NO:1243	FPLPSAPAVVIHTLD
SEQ ID NO:1209	IFPLPSAPAVVI	SEQ ID NO:1244	PLPSAPAVVIHTLDK
SEQ ID NO:1210	FPLPSAPAVVIH	SEQ ID NO:1245	LPSAPAVVIHTLDKS
SEQ ID NO:1211	PLPSAPAVVIHT	SEQ ID NO:1246	PSAPAVVIHTLDKSF
SEQ ID NO:1212	LPSAPAVVIHTL	SEQ ID NO:1247	GPTERPTIIFPLPSAP
SEQ ID NO:1213	PSAPAVVIHTLD	SEQ ID NO:1248	PTERPTIIFPLPSAPA
SEQ ID NO:1249	TERPTIIFPLPSAPAV	SEQ ID NO:1286	PLPSAPAVVIHTLDKSFD
SEQ ID NO:1250	ERPTIIFPLPSAPAVV	SEQ ID NO:1287	LPSAPAVVIHTLDKSFDY
SEQ ID NO:1251	RPTIIFPLPSAPAVVI	SEQ ID NO:1288	PSAPAVVIHTLDKSFDYY
SEQ ID NO:1252	PTLIIPLPSAPAVVIH	SEQ ID NO:1289	IYPGPTERPTIIFPLPSAP
SEQ ID NO:1253	TIIFPLPSAPAVVIHT	SEQ ID NO:1290	YPGPTERPTIIFPLPSAPA
SEQ ID NO:1254	IIFPLPSAPAVVIHTL	SEQ ID NO:1291	PGPTERPTIIFPLPSAPAV
SEQ ID NO:1255	IFPLPSAPAVVIHTLD	SEQ ID NO:1292	GPTERPTIIFPLPSAPAVV
SEQ ID NO:1256	FPLPSAPAVVIHTLDK	SEQ ID NO:1293	PTERPTIIFPLPSAPAVVI
SEQ ID NO:1257	PLPSAPAVVIHTLDKS	SEQ ID NO:1294	TERPTIIFPLPSAPAVVIH
SEQ ID NO:1258	LPSAPAVVIHTLDKSF	SEQ ID NO:1295	ERPTIIFPLPSAPAVVIHT
SEQ ID NO:1259	PSAPAVVIHTLDKSFD	SEQ ID NO:1296	RPTIIFPLPSAPAVVIHTL
SEQ ID NO:1260	PGPTERPTIIFPLPSAP	SEQ ID NO:1297	PTIIFPLPSAPAVVIHTLD
SEQ ID NO:1261	GPTERPTIIFPLPSAPA	SEQ ID NO:1298	TIIFPLPSAPAVVIHTLDK
SEQ ID NO:1262	PTERPTIIFPLPSAPAV	SEQ ID NO:1299	IIFPLPSAPAVVIHTLDKS
SEQ ID NO:1263	TERPTIIFPLPSAPAVV	SEQ ID NO:1300	IFPLPSAPAVVIHTLDKSF
SEQ ID NO:1264	ERPTIIFPLPSAPAVVI	SEQ ID NO:1301	FPLPSAPAVVIHTLDKSFD
SEQ ID NO:1265	RPTIIFPLPSAPAVVIH	SEQ ID NO:1302	PLPSAPAVVIHTLDKSFDY
SEQ ID NO:1266	PTIIFPLPSAPAVVIHT	SEQ ID NO:1303	LPSAPAVVIHTLDKSFDYY
SEQ ID NO:1267	TIIFPLPSAPAVVIHTL	SEQ ID NO:1304	PSAPAVVIHTLDKSFDYYL
SEQ ID NO:1268	IIFPLPSAPAVVIHTLD	SEQ ID NO:1305	VIYPGPTERPTIIFPLPSAP
SEQ ID NO:1269	IFPLPSAPAVVIHTLDK	SEQ ID NO:1306	IYPGPTERPTIIFPLPSAPA
SEQ ID NO:1270	FPLPSAPAVVIHTLDKS	SEQ ID NO:1307	YPGPTERPTIIFPLPSAPAV
SEQ ID NO:1271	PLPSAPAVVIHTLDKSF	SEQ ID NO:1308	PGPTERPTIIFPLPSAPAVV
SEQ ID NO:1272	LPSAPAVVIHTLDKSFD	SEQ ID NO:1309	GPTERPTIIFPLPSAPAVVI
SEQ ID NO:1273	PSAPAVVIHTLDKSFDY	SEQ ID NO:1310	PTERPTIIFPLPSAPAVVIH
SEQ ID NO:1274	YPGPTERPTIIFPLPSAP	SEQ ID NO:1311	TERPTIIFPLPSAPAVVIHT
SEQ ID NO:1275	PGPTERPTIIFPLPSAPA	SEQ ID NO:1312	ERPTIIFPLPSAPAVVIHTL
SEQ ID NO:1276	GPTERPTIIFPLPSAPAV	SEQ ID NO:1313	RPTIIFPLPSAPAVVIHTLD
SEQ ID NO:1277	PTERPTIIFPLPSAPAVV	SEQ ID NO:1314	PTIIFPLPSAPAVVIHTLDK
SEQ ID NO:1278	TERPTIIFPLPSAPAVVI	SEQ ID NO:1315	TIIFPLPSAPAVVIHTLDKS
SEQ ID NO:1279	ERPTIIFPLPSAPAVVIH	SEQ ID NO:1316	IIFPLPSAPAVVIHTLDKSF
SEQ ID NO:1280	RPTIIFPLPSAPAVVIHT	SEQ ID NO:1317	IFPLPSAPAVVIHTLDKSFD
SEQ ID NO:1281	PTIIFPLPSAPAVVIHTL	SEQ ID NO:1318	FPLPSAPAVVIHTLDKSFDY
SEQ ID NO:1282	TIIFPLPSAPAVVIHTLD	SEQ ID NO:1319	PLPSAPAVVIHTLDKSFDYY
SEQ ID NO:1283	IIFPLPSAPAVVIHTLDK	SEQ ID NO:1320	LPSAPAVVIHTLDKSFDYYL
SEQ ID NO:1284	IFPLPSAPAVVIHTLDKS	SEQ ID NO:1321	PSAPAVVIHTLDKSFDYYLH
SEQ ID NO:1285	FPLPSAPAVVIHTLDKSF

[0157]

TABLE 11
P(T/S)AP Motif Containing Peptides from Human Papillomavrius Type 35
Major Capsid Protein L1
(GenBank Accession No. P27232)
SEQ ID NO:1322	TCQKPSAP	SEQ ID NO:1357	TSQAVTCQKPSAP
SEQ ID NO:1323	CQKPSAPK	SEQ ID NO:1358	SQAVTCQKPSAPK
SEQ ID NO:1324	QKPSAPKP	SEQ ID NO:1359	QAVTCQKPSAPKP
SEQ ID NO:1325	KPSAPKPK	SEQ ID NO:1360	AVTCQKPSAPKPK
SEQ ID NO:1326	PSAPKPKD	SEQ ID NO:1361	VTCQKPSAPKPKD
SEQ ID NO:1327	VTCQKPSAP	SEQ ID NO:1362	TCQKPSAPKPKDD
SEQ ID NO:1328	TCQKPSAPK	SEQ ID NO:1363	CQKPSAPKPKDDP
SEQ ID NO:1329	CQKPSAPKP	SEQ ID NO:1364	QKPSAPKPKDDPL
SEQ ID NO:1330	QKPSAPKPK	SEQ ID NO:1365	KPSAPKPKDDPLK
SEQ ID NO:1331	KPSAPKPKD	SEQ ID NO:1366	PSAPKPKDDPLKN
SEQ ID NO:1332	PSAPKPKDD	SEQ ID NO:1367	VTSQAVTCQKPSAP
SEQ ID NO:1333	AVTCQKPSAP	SEQ ID NO:1368	TSQAVTCQKPSAPK
SEQ ID NO:1334	VTCQKPSAPK	SEQ ID NO:1369	SQAVTCQKPSAPKP
SEQ ID NO:1335	TCQKPSAPKP	SEQ ID NO:1370	QAVTCQKPSAPKPK
SEQ ID NO:1336	CQKPSAPKPK	SEQ ID NO:1371	AVTCQKPSAPKPKD
SEQ ID NO:1337	QKPSAPKPKD	SEQ ID NO:1372	VTCQKPSAPKPKDD
SEQ ID NO:1338	KPSAPKPKDD	SEQ ID NO:1373	TCQKPSAPKPKDDP
SEQ ID NO:1339	PSAPKPKDDP	SEQ ID NO:1374	CQKPSAPKPKDDPL
SEQ ID NO:1340	QAVTCQKPSAP	SEQ ID NO:1375	QKPSAPKPKDDPLK
SEQ ID NO:1341	AVTCQKPSAPK	SEQ ID NO:1376	KPSAPKPKDDPLKN
SEQ ID NO:1342	VTCQKPSAPKP	SEQ ID NO:1377	PSAPKPKDDPLKNY
SEQ ID NO:1343	TCQKPSAPKPK	SEQ ID NO:1378	YVTSQAVTCQKPSAP
SEQ ID NO:1344	CQKPSAPKPKD	SEQ ID NO:1379	VTSQAVTCQKPSAPK
SEQ ID NO:1345	QKPSAPKPKDD	SEQ ID NO:1380	TSQAVTCQKPSAPKP
SEQ ID NO:1346	KPSAPKPKDDP	SEQ ID NO:1381	SQAVTCQKPSAPKPK
SEQ ID NO:1347	PSAPKPKDDPL	SEQ ID NO:1382	QAVTCQKPSAPKPKD
SEQ ID NO:1348	SQAVTCQKPSAP	SEQ ID NO:1383	AVTCQKPSAPKPKDD
SEQ ID NO:1349	QAVTCQKPSAPK	SEQ ID NO:1384	VTCQKPSAPKPKDDP
SEQ ID NO:1350	AVTCQKPSAPKP	SEQ ID NO:1385	TCQKPSAPKPKDDPL
SEQ ID NO:1351	VTCQKPSAPKPK	SEQ ID NO:1386	CQKPSAPKPKDDPLK
SEQ ID NO:1352	TCQKPSAPKPKD	SEQ ID NO:1387	QKPSAPKPKDDPLKN
SEQ ID NO:1353	CQKPSAPKPKDD	SEQ ID NO:1388	KPSAPKPKDDPLKNY
SEQ ID NO:1354	QKPSAPKPKDDP	SEQ ID NO:1389	PSAPKPKDDPLKNYT
SEQ ID NO:1355	KPSAPKPKDDPL	SEQ ID NO:1390	RYVTSQAVTCQKPSAP
SEQ ID NO:1356	PSAPKPKDDPLK	SEQ ID NO:1391	YVTSQAVTCQKPSAPK
SEQ ID NO:1392	VTSQAVTCQKPSAPKP	SEQ ID NO:1429	QKPSAPKPKDDPLKNYTF
SEQ ID NO:1393	TSQAVTCQKPSAPKPK	SEQ ID NO:1430	KPSAPKPKDDPLKNYTFW
SEQ ID NO:1394	SQAVTCQKPSAPKPKD	SEQ ID NO:1431	PSAPKPKDDPLKNYTFWE
SEQ ID NO:1395	QAVTCQKPSAPKPKDD	SEQ ID NO:1432	DTYRYVTSQAVTCQKPSAP
SEQ ID NO:1396	AVTCQKPSAPKPKDDP	SEQ ID NO:1433	TYRYVTSQAVTCQKPSAPK
SEQ ID NO:1397	VTCQKPSAPKPKDDPL	SEQ ID NO:1434	YRYVTSQAVTCQKPSAPKP
SEQ ID NO:1398	TCQKPSAPKPKDDPLK	SEQ ID NO:1435	RYVTSQAVTCQKPSAPKPK
SEQ ID NO:1399	CQKPSAPKPKDDPLKN	SEQ ID NO:1436	YVTSQAVTCQKPSAPKPKD
SEQ ID NO:1400	QKPSAPKPKDDPLKNY	SEQ ID NO:1437	VTSQAVTCQKPSAPKPKDD
SEQ ID NO:1401	KPSAPKPKDDPLKNYT	SEQ ID NO:1438	TSQAVTCQKPSAPKPKDDP
SEQ ID NO:1402	PSAPKPKDDPLKNYTF	SEQ ID NO:1439	SQAVTCQKPSAPKPKDDPL
SEQ ID NO:1403	YRYVTSQAVTCQKPSAP	SEQ ID NO:1440	QAVTCQKPSAPKPKDDPLK
SEQ ID NO:1404	RYVTSQAVTCQKPSAPK	SEQ ID NO:1441	AVTCQKPSAPKPKDDPLKN
SEQ ID NO:1405	YVTSQAVTCQKPSAPKP	SEQ ID NO:1442	VTCQKPSAPKPKDDPLKNY
SEQ ID NO:1406	VTSQAVTCQKPSAPKPK	SEQ ID NO:1443	TCQKPSAPKPKDDPLKNYT
SEQ ID NO:1407	TSQAVTCQKPSAPKPKD	SEQ ID NO:1444	CQKPSAPKPKDDPLKNYTF
SEQ ID NO:1408	SQAVTCQKPSAPKPKDD	SEQ ID NO:1445	QKPSAPKPKDDPLKNYTFW
SEQ ID NO:1409	QAVTCQKPSAPKPKDDP	SEQ ID NO:1446	KPSAPKPKDDPLKNYTFWE
SEQ ID NO:1410	AVTCQKPSAPKPKDDPL	SEQ ID NO:1447	PSAPKPKDDPLKNYTFWEV
SEQ ID NO:1411	VTCQKPSAPKPKDDPLK	SEQ ID NO:1448	EDTYRYVTSQAVTCQKPSAP
SEQ ID NO:1412	TCQKPSAPKPKDDPLKN	SEQ ID NO:1449	DTYRYVTSQAVTCQKPSAPK
SEQ ID NO:1413	CQKPSAPKPKDDPLKNY	SEQ ID NO:1450	TYRYVTSQAVTCQKPSAPKP
SEQ ID NO:1414	QKPSAPKPKDDPLKNYT	SEQ ID NO:1451	YRYVTSQAVTCQKPSAPKPK
SEQ ID NO:1415	KPSAPKPKDDPLKNYTF	SEQ ID NO:1452	RYVTSQAVTCQKPSAPKPKD
SEQ ID NO:1416	PSAPKPKDDPLKNYTFW	SEQ ID NO:1453	YVTSQAVTCQKPSAPKPKDD
SEQ ID NO:1417	TYRYVTSQAVTCQKPSAP	SEQ ID NO:1454	VTSQAVTCQKPSAPKPKDDP
SEQ ID NO:1418	YRYVTSQAVTCQKPSAPK	SEQ ID NO:1455	TSQAVTCQKPSAPKPKDDPL
SEQ ID NO:1419	RYVTSQAVTCQKPSAPKP	SEQ ID NO:1456	SQAVTCQKPSAPKPKDDPLK
SEQ ID NO:1420	YVTSQAVTCQKPSAPKPK	SEQ ID NO:1457	QAVTCQKPSAPKPKDDPLKN
SEQ ID NO:1421	VTSQAVTCQKPSAPKPKD	SEQ ID NO:1458	AVTCQKPSAPKPKDDPLKNY
SEQ ID NO:1422	TSQAVTCQKPSAPKPKDD	SEQ ID NO:1459	VTCQKPSAPKPKDDPLKNYT
SEQ ID NO:1423	SQAVTCQKPSAPKPKDDP	SEQ ID NO:1460	TCQKPSAPKPKDDPLKNYTF
SEQ ID NO:1424	QAVTCQKPSAPKPKDDPL	SEQ ID NO:1461	CQKPSAPKPKDDPLKNYTFW
SEQ ID NO:1425	AVTCQKPSAPKPKDDPLK	SEQ ID NO:1462	QKPSAPKPKDDPLKNYTFWE
SEQ ID NO:1426	VTCQKPSAPKPKDDPLKN	SEQ ID NO:1463	KPSAPKPKDDPLKNYTFWEV
SEQ ID NO:1427	TCQKPSAPKPKDDPLKNY	SEQ ID NO:1464	PSAPKPKDDPLKNYTFWEVD
SEQ ID NO:1428	CQKPSAPKPKDDPLKNYT

[0158]

TABLE 12
P(T/S)AP Motif Containing Peptides from Human Papillomavirus Type 6b
Minor Capsid Protein L2
(GenBank Accession No. NPe,uns  040303)
SEQ ID NO:1465	DITFPTAP	SEQ ID NO:1500	LQSGPDITFPTAP
SEQ ID NO:1466	ITFPTAPM	SEQ ID NO:1501	QSGPDITFPTAPM
SEQ ID NO:1467	TFPTAPMG	SEQ ID NO:1502	SGPDITFPTAPMG
SEQ ID NO:1468	FPTAPMGT	SEQ ID NO:1503	GPDITFPTAPMGT
SEQ ID NO:1469	PTAP MGTP	SEQ ID NO:1504	PDITFPTAPMGTP
SEQ ID NO:1470	PDITFPTAP	SEQ ID NO:1505	DITFPTAPMGTPF
SEQ ID NO:1471	DITFPTAPM	SEQ ID NO:1506	ITFPTAPMGTPFS
SEQ ID NO:1472	ITFPTAPMG	SEQ ID NO:1507	TFPTAPMGTPFSP
SEQ ID NO:1473	TFPTAPMGT	SEQ ID NO:1508	FPTAPMGTPFSPV
SEQ ID NO:1474	FPTAPMGTP	SEQ ID NO:1509	PTAP MGTPFSPVT
SEQ ID NO:1475	PTAP MGTPF	SEQ ID NO:1510	PLQSGPDITFPTAP
SEQ ID NO:1476	GPDITFPTAP	SEQ ID NO:1511	LQSGPDITFPTAPM
SEQ ID NO:1477	PDITFPTAPM	SEQ ID NO:1512	QSGPDITFPTAPMG
SEQ ID NO:1478	DITFPTAPMG	SEQ ID NO:1513	SGPDITFPTAPMGT
SEQ ID NO:1479	ITFPTAPMGT	SEQ ID NO:1514	GPDITFPTAPMGTP
SEQ ID NO:1480	TFPTAPMGTP	SEQ ID NO:1515	PDITFPTAPMGTPF
SEQ ID NO:1481	FPTAPMGTPF	SEQ ID NO:1516	DITFPTAPMGTPFS
SEQ ID NO:1482	PTAP MGTPFS	SEQ ID NO:1517	ITFPTAPMGTPFSP
SEQ ID NO:1483	SGPDITFPTAP	SEQ ID NO:1518	TFPTAPMGTPFSPV
SEQ ID NO:1484	GPDITFPTAPM	SEQ ID NO:1519	FPTAPMGTPFSPVT
SEQ ID NO:1485	PDITFPTAPMG	SEQ ID NO:1520	PTAP MGTPFSPVTP
SEQ ID NO:1486	DITFPTAPMGT	SEQ ID NO:1521	LFLQSGPDITFPTAP
SEQ ID NO:1487	ITFPTAPMGTP	SEQ ID NO:1522	FLQSGPDITFPTAPM
SEQ ID NO:1488	TFPTAPMGTPF	SEQ ID NO:1523	LQSGPDITFPTAPMG
SEQ ID NO:1489	FPTAPMGTPFS	SEQ ID NO:1524	QSGPDITFPTAPMGT
SEQ ID NO:1490	PTAP MGTPFSP	SEQ ID NO:1525	SGPDITFPTAPMGTP
SEQ ID NO:1491	QSGPDITFPTAP	SEQ ID NO:1526	GPDITFPTAPMGTPF
SEQ ID NO:1492	SGPDITFPTAPM SEQ ID NO:1527	PDITFPTAPMGTPFS
SEQ ID NO:1493	GPDITFPTAPMG	SEQ ID NO:1528	DITFPTAPMGTPFSP
SEQ ID NO:1494	PDITFPTAPMGT	SEQ ID NO:1529	ITFPTAPMGTPFSPV
SEQ ID NO:1495	DITFPTAPMGTP	SEQ ID NO:1530	TFPTAPMGTPFSPVT
SEQ ID NO:1496	ITFPTAPMGTPF	SEQ ID NO:1531	FPTAPMGTPFSPVTP
SEQ ID NO:1497	TFPTAPMGTPFS	SEQ ID NO:1532	PTAP MGTPFSPVTPA
SEQ ID NO:1498	FPTAPMGTPFSP	SEQ ID NO:1533	DLFLQSGPDITFPTAP
SEQ ID NO:1499	PTAP MGTPFSPV	SEQ ID NO:1534	LFLQSGPDITFPTAPM
SEQ ID NO:1535	FLQSGPDITFPTAPMG	SEQ ID NO:1572	TFPTAPMGTPFSPVTPAL
SEQ ID NO:1536	LQSGPDITFPTAPMGT	SEQ ID NO:1573	FPTAPMGTPFSPVTPALP
SEQ ID NO:1537	QSGPDITFPTAPMGTP	SEQ ID NO:1574	PTAP MGTPFSPVTPALPT
SEQ ID NO:1538	SGPDITFPTAPMGTPF	SEQ ID NO:1575	LPNDLFLQSGPDITFPTAP
SEQ ID NO:1539	GPDITFPTAPMGTPFS	SEQ ID NO:1576	PNDLFLQSGPDITFPTAPM
SEQ ID NO:1540	PDITFPTAPMGTPFSP	SEQ ID NO:1577	NDLFLQSGPDITFPTAPMG
SEQ ID NO:1541	DITFPTAPMGTPFSPV	SEQ ID NO:1578	DLFLQSGPDITFPTAPMGT
SEQ ID NO:1542	ITFPTAPMGTPFSPVT	SEQ ID NO:1579	LFLQSGPDITFPTAPMGTP
SEQ ID NO:1543	TFPTAPMGTPFSPVTP	SEQ ID NO:1580	FLQSGPDITFPTAPMGTPF
SEQ ID NO:1544	FPTAPMGTPFSPVTPA	SEQ ID NO:1581	LQSGPDITFPTAPMGTPFS
SEQ ID NO:1545	PTAP MGTPFSPVTPAL	SEQ ID NO:1582	QSGPDITFPTAPMGTPFSP
SEQ ID NO:1546	NDLFLQSGPDITFPTAP	SEQ ID NO:1583	SGPDITFPTAPMGTPFSPV
SEQ ID NO:1547	DLFLQSGPDITFPTAPM	SEQ ID NO:1584	GPDITFPTAPMGTPFSPVT
SEQ ID NO:1548	LFLQSGPDITFPTAPMG	SEQ ID NO:1585	PDITFPTAPMGTPFSPVTP
SEQ ID NO:1549	FLQSGPDITFPTAPMGT	SEQ ID NO:1586	DITFPTAPMGTPFSPVTPA
SEQ ID NO:1550	LQSGPDITFPTAPMGTP	SEQ ID NO:1587	ITFPTAPMGTPFSPVTPAL
SEQ ID NO:1551	QSGPDITFPTAPMGTPF	SEQ ID NO:1588	TFPTAPMGTPFSPVTPALP
SEQ ID NO:1552	SGPDITFPTAPMGTPFS	SEQ ID NO:1589	FPTAPMGTPFSPVTPALPT
SEQ ID NO:1553	GPDITFPTAPMGTPFSP	SEQ ID NO:1590	PTAP MGTPFSPVTPALPTG
SEQ ID NO:1554	PDITFPTAPMGTPFSPV	SEQ ID NO:1591	SLPNDLFLQSGPDITFPTAP
SEQ ID NO:1555	DITFPTAPMGTPFSPVT	SEQ ID NO:1592	LPNDLFLQSGPDITFPTAPM
SEQ ID NO:1556	ITFPTAPMGTPFSPVTP	SEQ ID NO:1593	PNDLFLQSGPDITFPTAPMG
SEQ ID NO:1557	TFPTAPMGTPFSPVTPA	SEQ ID NO:1594	NDLFLQSGPDITFPTAPMGT
SEQ ID NO:1558	FPTAPMGTPFSPVTPAL	SEQ ID NO:1595	DLFLQSGPDITFPTAPMGTP
SEQ ID NO:1559	PTAP MGTPFSPVTPALP	SEQ ID NO:1596	LFLQSGPDITFPTAPMGTPF
SEQ ID NO:1560	PNDLFLQSGPDITFPTAP	SEQ ID NO:1597	FLQSGPDITFPTAPMGTPFS
SEQ ID NO:1561	NDLFLQSGPDITFPTAPM	SEQ ID NO:1598	LQSGPDITFPTAPMGTPFSP
SEQ ID NO:1562	DLFLQSGPDITFPTAPMG	SEQ ID NO:1599	QSGPDITFPTAPMGTPFSPV
SEQ ID NO:1563	LFLQSGPDITFPTAPMGT	SEQ ID NO:1600	SGPDITFPTAPMGTPFSPVT
SEQ ID NO:1564	FLQSGPDITFPTAPMGTP	SEQ ID NO:1601	GPDITFPTAPMGTPFSPVTP
SEQ ID NO:1565	LQSGPDITFPTAPMGTPF	SEQ ID NO:1602	PDITFPTAPMGTPFSPVTPA
SEQ ID NO:1566	QSGPDITFPTAPMGTPFS	SEQ ID NO:1603	DITFPTAPMGTPFSPVTPAL
SEQ ID NO:1567	SGPDITFPTAPMGTPFSP	SEQ ID NO:1604	ITFPTAPMGTPFSPVTPALP
SEQ ID NO:1568	GPDITFPTAPMGTPFSPV	SEQ ID NO:1605	TFPTAPMGTPFSPVTPALPT
SEQ ID NO:1569	PDITFPTAPMGTPFSPVT	SEQ ID NO:1606	FPTAPMGTPFSPVTPALPTG
SEQ ID NO:1570	DITFPTAPMGTPFSPVTP	SEQ ID NO:1607	PTAP MGTPFSPVTPALPTGP
SEQ ID NO:1571	ITFPTAPMGTPFSPVTPA

[0159]

TABLE 13
P(TIS)AP Motif Containing Peptides from Human Papillomavirus Type 9
Late Protein
(GenBank Accession No. NP_041865)
SEQ ID NO:1608	RPIDPTAP	SEQ ID NO:1643	PLDTVRPIDPTAP
SEQ ID NO:1609	PIDPTAPS	SEQ ID NO:1644	LDTVRPIDPTAPS
SEQ ID NO:1610	IDPTAPSI	SEQ ID NO:1645	DTVRPIDPTAPSI
SEQ ID NO:1611	DPTAPSIV	SEQ ID NO:1646	TVRPIDPTAPSIV
SEQ ID NO:1612	PTAP SIVT	SEQ ID NO:1647	VRPIDPTAPSIVT
SEQ ID NO:1613	VRPIDPTAP	SEQ ID NO:1648	RPIDPTAPSIVTG
SEQ ID NO:1614	RPIDPTAPS	SEQ ID NO:1649	PIDPTAPSIVTGT
SEQ ID NO:1615	PIDPTAPSI	SEQ ID NO:1650	IDPTAPSIVTGTD
SEQ ID NO:1616	IDPTAPSIV	SEQ ID NO:1651	DPTAPSIVTGTDS
SEQ ID NO:1617	DPTAPSIVT	SEQ ID NO:1652	PTAP SIVTGTDST
SEQ ID NO:1618	PTAP SIVTG	SEQ ID NO:1653	IPLDTVRPIDPTAP
SEQ ID NO:1619	TVRPIDPTAP	SEQ ID NO:1654	PLDTVRPIDPTAPS
SEQ ID NO:1620	VRPIDPTAPS	SEQ ID NO:1655	LDTVRPIDPTAPSI
SEQ ID NO:1621	RPIDPTAPSI	SEQ ID NO:1656	DTVRPIDPTAPSIV
SEQ ID NO:1622	PIDPTAPSIV	SEQ ID NO:1657	TVRPIDPTAPSIVT
SEQ ID NO:1623	IDPTAPSIVT	SEQ ID NO:1658	VRPIDPTAPSIVTG
SEQ ID NO:1624	DPTAPSIVTG	SEQ ID NO:1659	RPIDPTAPSIVTGT
SEQ ID NO:1625	PTAP SIVTGT	SEQ ID NO:1660	PIDPTAPSIVTGTD
SEQ ID NO:1626	DTVRPIDPTAP	SEQ ID NO:1661	IDPTAPSIVTGTDS
SEQ ID NO:1627	TVRPIDPTAPS	SEQ ID NO:1662	DPTAPSIVTGTDST
SEQ ID NO:1628	VRPIDPTAPSI	SEQ ID NO:1663	PTAP SIVTGTDSTV
SEQ ID NO:1629	RPIDPTAPSIV	SEQ ID NO:1664	LIPLDTVRPIDPTAP
SEQ ID NO:1630	PIDPTAPSIVT	SEQ ID NO:1665	IPLDTVRPIDPTAPS
SEQ ID NO:1631	IDPTAPSIVTG	SEQ ID NO:1666	PLDTVRPIDPTAPSI
SEQ ID NO:1632	DPTAPSIVTGT	SEQ ID NO:1667	LDTVRPIDPTAPSIV
SEQ ID NO:1633	PTAP SIVTGTD	SEQ ID NO:1668	DTVRPIDPTAPSIVT
SEQ ID NO:1634	LDTVRPIDPTAP	SEQ ID NO:1669	TVRPIDPTAPSIVTG
SEQ ID NO:1635	DTVRPIDPTAPS	SEQ ID NO:1670	VRPIDPTAPSIVTGT
SEQ ID NO:1636	TVRPIDPTAPSI	SEQ ID NO:1671	RPIDPTAPSIVTGTD
SEQ ID NO:1637	VRPIDPTAPSIV	SEQ ID NO:1672	PIDPTAPSIVTGTDS
SEQ ID NO:1638	RPIDPTAPSIVT	SEQ ID NO:1673	IDPTAPSIVTGTDST
SEQ ID NO:1639	PIDPTAPSIVTG	SEQ ID NO:1674	DPTAPSIVTGTDSTV
SEQ ID NO:1640	IDPTAPSIVTGT	SEQ ID NO:1675	PTAP SIVTGTDSTVD
SEQ ID NO:1641	DPTAPSIVTGTD	SEQ ID NO:1676	DLIPLDTVRPIDPTAP
SEQ ID NO:1642	PTAP SIVTGTDS	SEQ ID NO:1677	LIPLDTVRPIDPTAPS
SEQ ID NO:1678	IPLDTVRPIDPTAPSI	SEQ ID NO:1715	IDPTAPSIVTGTDSTVDL
SEQ ID NO:1679	PLDTVRPIDPTAPSIV	SEQ ID NO:1716	DPTAPSIVTGTDSTVDLL
SEQ ID NO:1680	LDTVRPIDPTAPSIVT	SEQ ID NO:1717	PTAP SIVTGTDSTVDLLP
SEQ ID NO:1681	DTVRPIDPTAPSIVTG	SEQ ID NO:17I8	GPTDLIPLDTVRPIDPTAP
SEQ ID NO:1682	TVRPIDPTAPSIVTGT	SEQ ID NO:1719	PTDLIPLDTVRPIDPTAPS
SEQ ID NO:1683	VRPIDPTAPSIVTGTD	SEQ ID NO:1720	TDLIPLDTVRPIDPTAPSI
SEQ ID NO:1684	RPIDPTAPSIVTGTDS	SEQ ID NO:1721	DLIPLDTVRPIDPTAPSIV
SEQ ID NO:1685	PIDPTAPSIVTGTDST	SEQ ID NO:1722	LIPLDTVRPIDPTAPSIVT
SEQ ID NO:1686	IDPTAPSIVTGTDSTV	SEQ ID NO:1723	IPLDTVRPIDPTAPSIVTG
SEQ ID NO:1687	DPTAPSIVTGTDSTVD	SEQ ID NO:1724	PLDTVRPIDPTAPSIVTGT
SEQ ID NO:1688	PTAP SIVTGTDSTVDL	SEQ ID NO:1725	LDTVRPIDPTAPSIVTGTD
SEQ ID NO:1689	TDLIPLDTVRPIDPTAP	SEQ ID NO:1726	DTVRPIDPTAPSIVTGTDS
SEQ ID NO:1690	DLIPLDTVRPIDPTAPS	SEQ ID NO:1727	TVRPIDPTAPSIVTGTDST
SEQ ID NO:1691	LIPLDTVRPIDPTAPSI	SEQ ID NO:1728	VRPIDPTAPSIVTGTDSTV
SEQ ID NO:1692	IPLDTVRPIDPTAPSIV	SEQ ID NO:1729	RPIDPTAPSIVTGTDSTVD
SEQ ID NO:1693	PLDTVRPIDPTAPSIVT	SEQ ID NO:1730	PIDPTAPSIVTGTDSTVDL
SEQ ID NO:1694	LDTVRPIDPTAPSIVTG	SEQ ID NO:1731	IDPTAPSIVTGTDSTVDLL
SEQ ID NO:1695	DTVRPIDPTAPSIVTGT	SEQ ID NO:1732	DPTAPSIVTGTDSTVDLLP
SEQ ID NO:1696	TVRPIDPTAPSIVTGTD	SEQ ID NO:1733	PTAP SIVTGTDSTVDLLPG
SEQ ID NO:1697	VRPIDPTAPSIVTGTDS	SEQ ID NO:1734	IGPTDLIPLDTVRPIDPTAP
SEQ ID NO:1698	RPIDPTAPSIVTGTDST	SEQ ID NO:1735	GPTDLIPLDTVRPIDPTAPS
SEQ ID NO:1699	PIDPTAPSIVTGTDSTV	SEQ ID NO:1736	PTDLIPLDTVRPIDPTAPSI
SEQ ID NO:1700	IDPTAPSIVTGTDSTVD	SEQ ID NO:1737	TDLIPLDTVRPIDPTAPSIV
SEQ ID NO:1701	DPTAPSIVTGTDSTVDL	SEQ ID NO:1738	DLIPLDTVRPIDPTAPSIVT
SEQ ID NO:1702	PTAP SIVTGTDSTVDLL	SEQ ID NO:1739	LIPLDTVRPIDPTAPSIVTG
SEQ ID NO:1703	PTDLIPLDTVRPIDPTAP	SEQ ID NO:1740	IPLDTVRPIDPTAPSIVTGT
SEQ ID NO:1704	TDLIPLDTVRPIDPTAPS	SEQ ID NO:1741	PLDTVRPIDPTAPSIVTGTD
SEQ ID NO:1705	DLIPLDTVRPIDPTAPSI	SEQ ID NO:1742	LDTVRPIDPTAPSIVTGTDS
SEQ ID NO:1706	LIPLDTVRPIDPTAPSIV	SEQ ID NO:1743	DTVRPIDPTAPSIVTGTDST
SEQ ID NO:1707	IPLDTVRPIDPTAPSIVT	SEQ ID NO:1744	TVRPIDPTAPSIVTGTDSTV
SEQ ID NO:1708	PLDTVRPIDPTAPSIVTG	SEQ ID NO:1745	VRPIDPTAPSIVTGTDSTVD
SEQ ID NO:1709	LDTVRPIDPTAPSIVTGT	SEQ ID NO:1746	RPIDPTAPSIVTGTDSTVDL
SEQ ID NO:1710	DTVRPIDPTAPSIVTGTD	SEQ ID NO:1747	PIDPTAPSIVTGTDSTVDLL
SEQ ID NO:1711	TVRPIDPTAPSIVTGTDS	SEQ ID NO:1748	IDPTAPSIVTGTDSTVDLLP
SEQ ID NO:1712	VRPIDPTAPSIVTGTDST	SEQ ID NO:1749	DPTAPSIVTGTDSTVDLLPG
SEQ ID NO:1713	RPIDPTAPSIVTGTDSTV	SEQ ID NO:1750	PTAP SIVTGTDSTVDLLPGE
SEQ ID NO:1714	PIDPTAPSIVTGTDSTVD

[0160]

TABLE 14
P(T/S)AP Motif Containing Peptides from Human T-Cell Lymphotropic Virus Type
Gag Protein
(GenBank Accession No. CAA61543)
SEQ ID NO:1751	NQVSPSAP	SEQ ID NO:1786	NILVKNQVSPSAP
SEQ ID NO:1752	QVSPSAPA	SEQ ID NO:1787	ILVKNQVSPSAPA
SEQ ID NO:1753	VSPSAPAA	SEQ ID NO:1788	LVKNQVSPSAPAA
SEQ ID NO:1754	SPSAPAAP	SEQ ID NO:1789	VKNQVSPSAPAAP
SEQ ID NO:1755	PSAP AAPV	SEQ ID NO:1790	KNQVSPSAPAAPV
SEQ ID NO:1756	KNQVSPSAP	SEQ ID NO:1791	NQVSPSAPAAPVP
SEQ ID NO:1757	NQVSPSAPA	SEQ ID NO:1792	QVSPSAPAAPVPT
SEQ ID NO:1758	QVSPSAPAA	SEQ ID NO:1793	VSPSAPAAPVPTP
SEQ ID NO:1759	VSPSAPAAP	SEQ ID NO:1794	SPSAPAAPVPTPI
SEQ ID NO:1760	SPSAPAAPV	SEQ ID NO:1795	PSAP AAPVPTPIC
SEQ ID NO:1761	PSAP AAPVP	SEQ ID NO:1796	INILVKNQVSPSAP
SEQ ID NO:1762	VKNQVSPSAP	SEQ ID NO:1797	NILVKNQVSPSAPA
SEQ ID NO:1763	KNQVSPSAPA	SEQ ID NO:1798	ILVKNQVSPSAPAA
SEQ ID NO:1764	NQVSPSAPAA	SEQ ID NO:1799	LVKNQVSPSAPAAP
SEQ ID NO:1765	QVSPSAPAAP	SEQ ID NO:1800	VKNQVSPSAPAAPV
SEQ ID NO:1766	VSPSAPAAPV	SEQ ID NO:1801	KNQVSPSAPAAPVP
SEQ ID NO:1767	SPSAPAAPVP	SEQ ID NO:1802	NQVSPSAPAAPVPT
SEQ ID NO:1768	PSAP AAPVPT	SEQ ID NO:1803	QVSPSAPAAPVPTP
SEQ ID NO:1769	LVKNQVSPSAP	SEQ ID NO:1804	VSPSAPAAPVPTPI
SEQ ID NO:1770	VKNQVSPSAPA	SEQ ID NO:1805	SPSAPAAPVPTPIC
SEQ ID NO:1771	KNQVSPSAPAA	SEQ ID NO:1806	PSAP AAPVPTPICP
SEQ ID NO:1772	NQVSPSAPAAP	SEQ ID NO:1807	IINILVKNQVSPSAP
SEQ ID NO:1773	QVSPSAPAAPV	SEQ ID NO:1808	INILVKNQVSPSAPA
SEQ ID NO:1774	VSPSAPAAPVP	SEQ ID NO:1809	NILVKNQVSPSAPAA
SEQ ID NO:1775	SPSAPAAPVPT	SEQ ID NO:1810	ILVKNQVSPSAPAAP
SEQ ID NO:1776	PSAP AAPVPTP	SEQ ID NO:1811	LVKNQVSPSAPAAPV
SEQ ID NO:1777	ILVKNQVSPSAP	SEQ ID NO:1812	VKNQVSPSAPAAPVP
SEQ ID NO:1778	LVKNQVSPSAPA	SEQ ID NO:1813	KNQVSPSAPAAPVPT
SEQ ID NO:1779	VKNQVSPSAPAA	SEQ ID NO:I814	NQVSPSAPAAPVPTP
SEQ ID NO:1780	KNQVSPSAPAAP	SEQ ID NO:1815	QVSPSAPAAPVPTPI
SEQ ID NO:1781	NQVSPSAPAAPV	SEQ ID NO:1816	VSPSAPAAPVPTPIC
SEQ ID NO:1782	QVSPSAPAAPVP	SEQ ID NO:1817	SPSAPAAPVPTPICP
SEQ ID NO:1783	VSPSAPAAPVPT	SEQ ID NO:1818	PSAP AAPVPTPICPT
SEQ ID NO:1784	SPSAPAAPVPTP	SEQ ID NO:1819	EIINILVKNQVSPSAP
SEQ ID NO:1785	PSAP AAPVPTPI	SEQ ID NO:1820	IINILVKNQVSPSAPA
SEQ ID NO:1821	INILVKNQVSPSAPAA	SEQ ID NO:1858	VSPSAPAAPVPTPICPTT
SEQ ID NO:1822	NILVKNQVSPSAPAAP	SEQ ID NO:1859	SPSAPAAPVPTPICPTTT
SEQ ID NO:1823	ILVKNQVSPSAPAAPV	SEQ ID NO:1860	PSAP AAPVPTPICPTTTP
SEQ ID NO:1824	LVKNQVSPSAPAAPVP	SEQ ID NO:1861	RVVEIINILVKNQVSPSAP
SEQ ID NO:1825	VKNQVSPSAPAAPVPT	SEQ ID NO:1862	VVEIINILVKNQVSPSAPA
SEQ ID NO:1826	KNQVSPSAPAAPVPTP	SEQ ID NO:1863	VEIINILVKNQVSPSAPAA
SEQ ID NO:1827	NQVSPSAPAAPVPTPI	SEQ ID NO:1864	EIINILVKNQVSPSAPAAP
SEQ ID NO:1828	QVSPSAPAAPVPTPIC	SEQ ID NO:1865	IINILVKNQVSPSAPAAPV
SEQ ID NO:1829	VSPSAPAAPVPTPICP	SEQ ID NO:1866	INILVKNQVSPSAPAAPVP
SEQ ID NO:1830	SPSAPAAPVPTPICPT	SEQ ID NO:1867	NILVKNQVSPSAPAAPVPT
SEQ ID NO:1831	PSAP AAPVPTPICPTT	SEQ ID NO:1868	ILVKNQVSPSAPAAPVPTP
SEQ ID NO:1832	VEIINILVKNQVSPSAP	SEQ ID NO:1869	LVKNQVSPSAPAAPVPTPI
SEQ ID NO:1833	EIINILVKNQVSPSAPA	SEQ ID NO:1870	VKNQVSPSAPAAPVPTPIC
SEQ ID NO:1834	IINILVKNQVSPSAPAA	SEQ ID NO:1871	KNQVSPSAPAAPVPTPICP
SEQ ID NO:1835	INILVKNQVSPSAPAAP	SEQ ID NO:1872	NQVSPSAPAAPVPTPICPT
SEQ ID NO:1836	NILVKNQVSPSAPAAPV	SEQ ID NO:1873	QVSPSAPAAPVPTPICPTT
SEQ ID NO:1837	ILVKNQVSPSAPAAPVP	SEQ ID NO:1874	VSPSAPAAPVPTPICPTTT
SEQ ID NO:1838	LVKNQVSPSAPAAPVPT	SEQ ID NO:1875	SPSAPAAPVPTPICPTTTP
SEQ ID NO:1839	VKNQVSPSAPAAPVPTP	SEQ ID NO:1876	PSAP AAPVPTPICPTTTPP
SEQ ID NO:1840	KNQVSPSAPAAPVPTPI	SEQ ID NO:1877	GRVVEIINILVKNQVSPSAP
SEQ ID NO:1841	NQVSPSAPAAPVPTPIC	SEQ ID NO:1878	RVVEIINILVKNQVSPSAPA
SEQ ID NO:1842	QVSPSAPAAPVPTPICP	SEQ ID NO:1879	VVEIINILVKNQVSPSAPAA
SEQ ID NO:1843	VSPSAPAAPVPTPICPT	SEQ ID NO:1880	VEIINILVKNQVSPSAPAAP
SEQ ID NO:1844	SPSAPAAPVPTPICPTT	SEQ ID NO:1881	EIINILVKNQVSPSAPAAPV
SEQ ID NO:1845	PSAP AAPVPTPICPTTT	SEQ ID NO:1882	IINILVKNQVSPSAPAAPVP
SEQ ID NO:1846	VVEIINILVKNQVSPSAP	SEQ ID NO:1883	INILVKNQVSPSAPAAPVPT
SEQ ID NO:1847	VEIINILVKNQVSPSAPA	SEQ ID NO:1884	NILVKNQVSPSAPAAPVPTP
SEQ ID NO:1848	EIINILVKNQVSPSAPAA	SEQ ID NO:1885	ILVKNQVSPSAPAAPVPTPI
SEQ ID NO:1849	IINILVKNQVSPSAPAAP	SEQ ID NO:1886	LVKNQVSPSAPAAPVPTPIC
SEQ ID NO:1850	INILVKNQVSPSAPAAPV	SEQ ID NO:1887	VKNQVSPSAPAAPVPTPICP
SEQ ID NO:1851	NILVKNQVSPSAPAAPVP	SEQ ID NO:1888	KNQVSPSAPAAPVPTPICPT
SEQ ID NO:1852	ILVKNQVSPSAPAAPVPT	SEQ ID NO:1889	NQVSPSAPAAPVPTPICPTT
SEQ ID NO:1853	LVKNQVSPSAPAAPVPTP	SEQ ID NO:1890	QVSPSAPAAPVPTPICPTTT
SEQ ID NO:1854	VKNQVSPSAPAAPVPTPI	SEQ ID NO:1891	VSPSAPAAPVPTPICPTTTP
SEQ ID NO:1855	KNQVSPSAPAAPVPTPIC	SEQ ID NO:1892	SPSAPAAPVPTPICPTTTPP
SEQ ID NO:1856	NQVSPSAPAAPVPTPICP	SEQ ID NO:1893	PSAP AAPVPTPICPTTTPPP
SEQ ID NO:1857	QVSPSAPAAPVPTPICPT

[0161]

TABLE 15
P(T/S)AP Motif Containing Peptides from West Nile Virus
Polyprotein
(GenBank Accession No. NP_041724)
SEQ ID NO:1894	FSITPSAP	SEQ ID NO:1929	TQAGRFSITPSAP
SEQ ID NO:1895	SITPSAPS	SEQ ID NO:1930	QAGRFSITPSAPS
SEQ ID NO:1896	ITPSAPSY	SEQ ID NO:1931	AGRFSITPSAPSY
SEQ ID NO:1897	TPSAPSYT	SEQ ID NO:1932	GRFSITPSAPSYT
SEQ ID NO:1898	PSAP SYTL	SEQ ID NO:1933	RFSITPSAPSYTL
SEQ ID NO:1899	RFSITPSAP	SEQ ID NO:1934	FSITPSAPSYTLK
SEQ ID NO:1900	FSITPSAPS	SEQ ID NO:1935	SITPSAPSYTLKL
SEQ ID NO:1901	SITPSAPSY	SEQ ID NO:1936	LTPSAPSYTLKLG
SEQ ID NO:1902	ITPSAPSYT	SEQ ID NO:1937	TPSAPSYTLKLGE
SEQ ID NO:1903	TPSAPSYTL	SEQ ID NO:1938	PSAP SYTLKLGEY
SEQ ID NO:1904	PSAP SYTLK	SEQ ID NO:1939	ATQAGRFSITPSAP
SEQ ID NO:1905	GRFSITPSAP	SEQ ID NO:1940	TQAGRFSITPSAPS
SEQ ID NO:1906	RPSITPSAPS	SEQ ID NO:1941	QAGRFSITPSAPSY
SEQ ID NO:1907	FSITPSAPSY	SEQ ID NO:1942	AGRFSITPSAPSYT
SEQ ID NO:1908	SITPSAPSYT	SEQ ID NO:1943	GRFSITPSAPSYTL
SEQ ID NO:1909	ITPSAPSYTL	SEQ ID NO:1944	RFSITPSAPSYTLK
SEQ ID NO:1910	TPSAPSYTLK	SEQ ID NO:1945	FSITPSAPSYTLKL
SEQ ID NO:1911	PSAP SYTLKL	SEQ ID NO:1946	SITPSAPSYTLKLG
SEQ ID NO:1912	AGRFSITPSAP	SEQ ID NO:1947	ITPSAPSYTLKLGE
SEQ ID NO:1913	GRFSITPSAPS	SEQ ID NO:1948	TPSAPSYTLKLGEY
SEQ ID NO:1914	RFSITPSAPSY	SEQ ID NO:1949	PSAP SYTLKLGEYG
SEQ ID NO:1915	FSITPSAPSYT	SEQ ID NO:1950	GATQAGRFSITPSAP
SEQ ID NO:1916	SITPSAPSYTL	SEQ ID NO:1951	ATQAGRFSITPSAPS
SEQ ID NO:1917	ITPSAPSYTLK	SEQ ID NO:1952	TQAGRFSITPSAPSY
SEQ ID NO:1918	TPSAPSYTLKL	SEQ ID NO:1953	QAGRFSITPSAPSYT
SEQ ID NO:1919	PSAP SYTLKLG	SEQ ID NO:1954	AGRFSITPSAPSYTL
SEQ ID NO:1920	QAGRFSITPSAP	SEQ ID NO:1955	GRFSITPSAPSYTLK
SEQ ID NO:1921	AGRFSITPSAPS	SEQ ID NO:1956	RFSITPSAPSYTLKL
SEQ ID NO:1922	GRFSITPSAPSY	SEQ ID NO:1957	FSITPSAPSYTLKLG
SEQ ID NO:1923	RFSITPSAPSYT	SEQ ID NO:1958	SITPSAPSYTLKLGE
SEQ ID NO:1924	FSITPSAPSYTL	SEQ ID NO:1959	ITPSAPSYTLKLGEY
SEQ ID NO:1925	SITPSAPSYTLK	SEQ ID NO:1960	TPSAPSYTLKLGEYG
SEQ ID NO:1926	ITPSAPSYTLKL	SEQ ID NO:1961	PSAP SYTLKLGEYGE
SEQ ID NO:1927	TPSAPSYTLKLG	SEQ ID NO:1962	IGATQAGRFSITPSAP
SEQ ID NO:1928	PSAP SYTLKLGE	SEQ ID NO:1963	GATQAGRFSITPSAPS
SEQ ID NO:1964	ATQAGRFSITPSAPSY	SEQ ID NO:2001	ITPSAPSYTLKLGEYGEV
SEQ ID NO:1965	TQAGRFSITPSAPSYT	SEQ ID NO:2002	TPSAPSYTLKLGEYGEVT
SEQ ID NO:1966	QAGRFSITPSAPSYTL	SEQ ID NO:2003	PSAP SYTLKLGEYGEVTV
SEQ ID NO:1967	AGRFSITPSAPSYTLK	SEQ ID NO:2004	HGKLGATQAGRFSITPSAP
SEQ ID NO:1968	GRFSITPSAPSYTLKL	SEQ ID NO:2005	GKIGATQAGRFSITPSAPS
SEQ ID NO:1969	RFSITPSAPSYTLKLG	SEQ ID NO:2006	KIGATQAGRFSITPSAPSY
SEQ ID NO:1970	FSITPSAPSYTLKLGE	SEQ ID NO:2007	IGATQAGRFSITPSAPSYT
SEQ ID NO:1971	SLTPSAPSYTLKLGEY	SEQ ID NO:2008	GATQAGRFSITPSAPSYTL
SEQ ID NO:1972	ITPSAPSYTLKLGEYG	SEQ ID NO:2009	ATQAGRFSITPSAPSYTLK
SEQ ID NO:1973	TPSAPSYTLKLGEYGE	SEQ ID NO:2010	TQAGRFSITPSAPSYTLKL
SEQ ID NO:1974	PSAP SYTLKLGEYGEV	SEQ ID NO:2011	QAGRFSITPSAPSYTLKLG
SEQ ID NO:1975	KIGATQAGRFSITPSAP	SEQ ID NO:2012	AGRFSITPSAPSYTLKLGE
SEQ ID NO:1976	IGATQAGRFSITPSAPS	SEQ ID NO:2013	GRFSITPSAPSYTLKLGEY
SEQ ID NO:1977	GATQAGRFSITPSAPSY	SEQ ID NO:2014	RFSITPSAPSYTLKLGEYG
SEQ ID NO:1978	ATQAGRFSITPSAPSYT	SEQ ID NO:2015	FSITPSAPSYTLKLGEYGE
SEQ ID NO:1979	TQAGRFSITPSAPSYTL	SEQ ID NO:2016	SITPSAPSYTLKLGEYGEV
SEQ ID NO:1980	QAGRFSITPSAPSYTLK	SEQ ID NO:2017	ITPSAPSYTLKLGEYGEVT
SEQ ID NO:1981	AGRFSITPSAPSYTLKL	SEQ ID NO:2018	TPSAPSYTLKLGEYGEVTV
SEQ ID NO:1982	GRFSITPSAPSYTLKLG	SEQ ID NO:2019	PSAP SYTLKLGEYGEVTVD
SEQ ID NO:1983	RFSITPSAPSYTLKLGE	SEQ ID NO:2020	SHGKIGATQAGRFSITPSAP
SEQ ID NO:1984	FSITPSAPSYTLKLGEY	SEQ ID NO:2021	HGKIGATQAGRFSITPSAPS
SEQ ID NO:1985	SITPSAPSYTLKLGEYG	SEQ ID NO:2022	GKIGATQAGRFSITPSAPSY
SEQ ID NO:1986	ITPSAPSYTLKLGEYGE	SEQ ID NO:2023	KIGATQAGRFSITPSAPSYT
SEQ ID NO:1987	TPSAPSYTLKLGEYGEV	SEQ ID NO:2024	IGATQAGRFSITPSAPSYTL
SEQ ID NO:1988	PSAP SYTLKLGEYGEVT	SEQ ID NO:2025	GATQAGRFSITPSAPSYTLK
SEQ ID NO:1989	GKIGATQAGRFSITPSAP	SEQ ID NO:2026	ATQAGRFSITPSAPSYTLKL
SEQ ID NO:1990	KIGATQAGRFSITPSAPS	SEQ ID NO:2027	TQAGRFSITPSAPSYTLKLG
SEQ ID NO:1991	IGATQAGRFSITPSAPSY	SEQ ID NO:2028	QAGRFSITPSAPSYTLKLGE
SEQ ID NO:1992	GATQAGRFSITPSAPSYT	SEQ ID NO:2029	AGRFSITPSAPSYTLKLGEY
SEQ ID NO:1993	ATQAGRFSITPSAPSYTL	SEQ ID NO:2030	GRFSITPSAPSYTLKLGEYG
SEQ ID NO:1994	TQAGRFSITPSAPSYTLK	SEQ ID NO:2031	RESITPSAPSYTLKLGEYGE
SEQ ID NO:1995	QAGRFSITPSAPSYTLKL	SEQ ID NO:2032	FSITPSAPSYTLKLGEYGEV
SEQ ID NO:1996	AGRFSITPSAPSYTLKLG	SEQ ID NO:2033	SITPSAPSYTLKLGEYGEVT
SEQ ID NO:1997	GRFSITPSAPSYTLKLGE	SEQ ID NO:2034	ITPSAPSYTLKLGEYGEVTV
SEQ ID NO:1998	RFSITPSAPSYTLKLGEY	SEQ ID NO:2035	TPSAPSYTLKLGEYGEVTVD
SEQ ID NO:1999	FSITPSAPSYTLKLGEYG	SEQ ID NO:2036	PSAP SYTLKLGEYGEVTVDC
SEQ ID NO:2000	SITPSAPSYTLKLGEYGE

[0162]

TABLE 16
P(T/S)AP Motif Containing Peptides from Measles Virus
Matrix protein
(GenBank Accession No. CAA34587)
SEQ ID NO:2037	AAPQPSAP	SEQ ID NO:2072	TARIQAAPQPSAP
SEQ ID NO:2038	APQPSAPQ	SEQ ID NO:2073	ARIQAAPQPSAPQ
SEQ ID NO:2039	PQPSAPQE	SEQ ID NO:2074	RIQAAPQPSAPQE
SEQ ID NO:2040	QPSAPQEP	SEQ ID NO:2075	IQAAPQPSAPQEP
SEQ ID NO:2041	PSAP QEPR	SEQ ID NO:2076	QAAPQPSAPQEPR
SEQ ID NO:2042	QAAPQPSAP	SEQ ID NO:2077	AAPQPSAPQEPRT
SEQ ID NO:2043	AAPQPSAPQ	SEQ ID NO:2078	APQPSAPQEPRTH
SEQ ID NO:2044	APQPSAPQE	SEQ ID NO:2079	PQPSAPQEPRTHD
SEQ ID NO:2045	PQPSAPQEP	SEQ ID NO:2080	QPSAPQEPRTHDD
SEQ ID NO:2046	QPSAPQEPR	SEQ ID NO:2081	PSAP QEPRTHDDA
SEQ ID NO:2047	PSAP QEPRT	SEQ ID NO:2082	KTARIQAAPQPSAP
SEQ ID NO:2048	IQAAPQPSAP	SEQ ID NO:2083	TARIQAAPQPSAPQ
SEQ ID NO:2049	QAAPQPSAPQ	SEQ ID NO:2084	ARIQAAPQPSAPQE
SEQ ID NO:2050	AAPQPSAPQE	SEQ ID NO:2085	RIQAAPQPSAPQEP
SEQ ID NO:2051	APQPSAPQEP	SEQ ID NO:2086	IQAAPQPSAPQEPR
SEQ ID NO:2052	PQPSAPQEPR	SEQ ID NO:2087	QAAPQPSAPQEPRT
SEQ ID NO:2053	QPSAPQEPRT	SEQ ID NO:2088	AAPQPSAPQEPRTH
SEQ ID NO:2054	PSAP QEPRTH	SEQ ID NO:2089	APQPSAPQEPRTHD
SEQ ID NO:2055	RIQAAPQPSAP	SEQ ID NO:2090	PQPSAPQEPRTHDD
SEQ ID NO:2056	IQAAPQPSAPQ	SEQ ID NO:2091	QPSAPQEPRTHDDA
SEQ ID NO:2057	QAAPQPSAPQE	SEQ ID NO:2092	PSAP QEPRTHDDAI
SEQ ID NO:2058	AAPQPSAPQEP	SEQ ID NO:2093	RKTARIQAAPQPSAP
SEQ ID NO:2059	APQPSAPQEPR	SEQ ID NO:2094	KTARIQAAPQPSAPQ
SEQ ID NO:2060	PQPSAPQEPRT	SEQ ID NO:2095	TARIQAAPQPSAPQE
SEQ ID NO:2061	QPSAPQEPRTH	SEQ ID NO:2096	ARIQAAPQPSAPQEP
SEQ ID NO:2062	PSAP QEPRTHD	SEQ ID NO:2097	RIQAAPQPSAPQEPR
SEQ ID NO:2063	ARIQAAPQPSAP	SEQ ID NO:2098	LQAAPQPSAPQEPRT
SEQ ID NO:2064	RIQAAPQPSAPQ	SEQ ID NO:2099	QAAPQPSAPQEPRTH
SEQ ID NO:2065	IQAAPQPSAPQE	SEQ ID NO:2100	AAPQPSAPQEPRTHD
SEQ ID NO:2066	QAAPQPSAPQEP	SEQ ID NO:2101	APQPSAPQEPRTHDD
SEQ ID NO:2067	AAPQPSAPQEPR	SEQ ID NO:2102	PQPSAPQEPRTHDDA
SEQ ID NO:2068	APQPSAPQEPRT	SEQ ID NO:2103	QPSAPQEPRTHDDAI
SEQ ID NO:2069	PQPSAPQEPRTH	SEQ ID NO:2104	PSAP QEPRTHDDAIT
SEQ ID NO:2070	QPSAPQEPRTHD	SEQ ID NO:2105	RRKTARIQAAPQPSAP
SEQ ID NO:2071	PSAP QEPRTHDD	SEQ ID NO:2106	RKTARIQAAPQPSAPQ
SEQ ID NO:2107	KTARIQAAPQPSAPQE	SEQ ID NO:2144	PQPSAPQEPRTHDDAITN
SEQ ID NO:2108	TARIQAAPQPSAPQEP	SEQ ID NO:2145	QPSAPQEPRTHDDAITND
SEQ ID NO:2109	ARIQAAPQPSAPQEPR	SEQ ID NO:2146	PSAP QEPRTHDDAITNDD
SEQ ID NO:2110	RIQAAPQPSAPQEPRT	SEQ ID NO:2147	WRSRRKTARIQAAPQPSAP
SEQ ID NO:2111	IQAAPQPSAPQEPRTH	SEQ ID NO:2148	RSRRKTARIQAAPQPSAPQ
SEQ ID NO:2112	QAAPQPSAPQEPRTHD	SEQ ID NO:2149	SRRKTARIQAAPQPSAPQE
SEQ ID NO:2113	AAPQPSAPQEPRTHDD	SEQ ID NO:2150	RRKTARIQAAPQPSAPQEP
SEQ ID NO:2114	APQPSAPQEPRTHDDA	SEQ ID NO:2151	RKTARIQAAPQPSAPQEPR
SEQ ID NO:2115	PQPSAPQEPRTHDDAI	SEQ ID NO:2152	KTARIQAAPQPSAPQEPRT
SEQ ID NO:2116	QPSAPQEPRTHDDAIT	SEQ ID NO:2153	TARIQAAPQPSAPQEPRTH
SEQ ID NO:2117	PSAP QEPRTHDDAITN	SEQ ID NO:2154	ARIQAAPQPSAPQEPRTHD
SEQ ID NO:2118	SRRKTARIQAAPQPSAP	SEQ ID NO:2155	RIQAAPQPSAPQEPRTHDD
SEQ ID NO:2119	RRKTARIQAAPQPSAPQ	SEQ ID NO:2156	IQAAPQPSAPQEPRTHDDA
SEQ ID NO:2120	RKTARIQAAPQPSAPQE	SEQ ID NO:2157	QAAPQPSAPQEPRTHDDAI
SEQ ID NO:2121	KTARIQAAPQPSAPQEP	SEQ ID NO:2158	AAPQPSAPQEPRTHDDAIT
SEQ ID NO:2122	TARIQAAPQPSAPQEPR	SEQ ID NO:2159	APQPSAPQEPRTHDDAITN
SEQ ID NO:2123	ARIQAAPQPSAPQEPRT	SEQ ID NO:2160	PQPSAPQEPRTHDDAITND
SEQ ID NO:2124	RIQAAPQPSAPQEPRTH	SEQ ID NO:2161	QPSAPQEPRTHDDAITNDD
SEQ ID NO:2125	IQAAPQPSAPQEPRTHD	SEQ ID NO:2162	PSAP QEPRTHDDAITNDDQ
SEQ ID NO:2126	QAAPQPSAPQEPRTHDD	SEQ ID NO:2163	LWRSRRKTARIQAAPQPSAP
SEQ ID NO:2127	AAPQPSAPQEPRTHDDA	SEQ ID NO:2164	WRSRRKTARIQAAPQPSAPQ
SEQ ID NO:2128	APQPSAPQEPRTHDDAI	SEQ ID NO:2165	RSRRKTARIQAAPQPSAPQE
SEQ ID NO:2129	PQPSAPQEPRTHDDAIT	SEQ ID NO:2166	SRRKTARIQAAPQPSAPQEP
SEQ ID NO:2130	QPSAPQEPRTHDDAITN	SEQ ID NO:2167	RRKTARIQAAPQPSAPQEPR
SEQ ID NO:2131	PSAP QEPRTHDDAITND	SEQ ID NO:2168	RKTARIQAAPQPSAPQEPRT
SEQ ID NO:2132	RSRRKTARIQAAPQPSAP	SEQ ID NO:2169	KTARIQAAPQPSAPQEPRTH
SEQ ID NO:2133	SRRKTARIQAAPQPSAPQ	SEQ ID NO:2170	TARIQAAPQPSAPQEPRTHD
SEQ ID NO:2134	RRKTARIQAAPQPSAPQE	SEQ ID NO:2171	ARIQAAPQPSAPQEPRTHDD
SEQ ID NO:2135	RKTARIQAAPQPSAPQEP	SEQ ID NO:2I72	RIQAAPQPSAPQEPRTHDDA
SEQ ID NO:2136	KTARIQAAPQPSAPQEPR	SEQ ID NO:2173	IQAAPQPSAPQEPRTHDDAI
SEQ ID NO:2137	TARIQAAPQPSAPQEPRT	SEQ ID NO:2174	QAAPQPSAPQEPRTHDDAIT
SEQ ID NO:2138	ARIQAAPQPSAPQEPRTH	SEQ ID NO:2175	AAPQPSAPQEPRTHDDAITN
SEQ ID NO:2139	RIQAAPQPSAPQEPRTHD	SEQ ID NO:2176	APQPSAPQEPRTHDDAITND
SEQ ID NO:2140	IQAAPQPSAPQEPRTHDD	SEQ ID NO:2177	PQPSAPQEPRTHDDAITNDD
SEQ ID NO:2141	QAAPQPSAPQEPRTHDDA	SEQ ID NO:2178	QPSAPQEPRTHDDAITNDDQ
SEQ ID NO:2142	AAPQPSAPQEPRTHDDAI	SEQ ID NO:2179	PSAP QEPRTHDDAITNDDQG
SEQ ID NO:2143	APQPSAPQEPRTHDDAIT

[0163]

TABLE 17
P(T/S)AP Motif Containing Peptides from Rubella Virus
Non-Structural Protein
(GenBank Accession No. BAB32473)
SEQ ID NO:2180	PRERPSAP	SEQ ID NO:2215	PRCDAPRERPSAP
SEQ ID NO:2181	RERPSAPA	SEQ ID NO:2216	RCDAPRERPSAPA
SEQ ID NO:2182	ERPSAPAG	SEQ ID NO:2217	CDAPRERPSAPAG
SEQ ID NO:2183	RPSAPAGP	SEQ ID NO:2218	DAPRERPSAPAGP
SEQ ID NO:2184	PSAP AGPP	SEQ ID NO:2219	APRERPSAPAGPP
SEQ ID NO:2185	APRERPSAP	SEQ ID NO:2220	PRERPSAPAGPPD
SEQ ID NO:2186	PRERPSAPA	SEQ ID NO:2221	RERPSAPAGPPDD
SEQ ID NO:2187	RERPSAPAG	SEQ ID NO:2222	ERPSAPAGPPDDE
SEQ ID NO:2188	ERPSAPAGP	SEQ ID NO:2223	RPSAPAGPPDDEA
SEQ ID NO:2189	RPSAPAGPP	SEQ ID NO:2224	PSAP AGPPDDEAL
SEQ ID NO:2190	PSAP AGPPD	SEQ ID NO:2225	APRCDAPRERPSAP
SEQ ID NO:2191	DAPRERPSAP	SEQ ID NO:2226	PRCDAPRERPSAPA
SEQ ID NO:2192	APRERPSAPA	SEQ ID NO:2227	RCDAPRERPSAPAG
SEQ ID NO:2193	PRERPSAPAG	SEQ ID NO:2228	CDAPRERPSAPAGP
SEQ ID NO:2194	RERPSAPAGP	SEQ ID NO:2229	DAPRERPSAPAGPP
SEQ ID NO:2195	ERPSAPAGPP	SEQ ID NO:2230	APRERPSAPAGPPD
SEQ ID NO:2196	RPSAPAGPPD	SEQ ID NO:2231	PRERPSAPAGPPDD
SEQ ID NO:2197	PSAP AGPPDD	SEQ ID NO:2232	RERPSAPAGPPDDE
SEQ ID NO:2198	CDAPRERPSAP	SEQ ID NO:2233	ERPSAPAGPPDDEA
SEQ ID NO:2199	DAPRERPSAPA	SEQ ID NO:2234	RPSAPAGPPDDEAL
SEQ ID NO:2200	APRERPSAPAG	SEQ ID NO:2235	PSAP AGPPDDEALI
SEQ ID NO:2201	PRERPSAPAGP	SEQ ID NO:2236	CAPRCDAPRERPSAP
SEQ ID NO:2202	RERPSAPAGPP	SEQ ID NO:2237	APRCDAPRERPSAPA
SEQ ID NO:2203	ERPSAPAGPPD	SEQ ID NO:2238	PRCDAPRERPSAPAG
SEQ ID NO:2204	RPSAPAGPPDD	SEQ ID NO:2239	RCDAPRERPSAPAGP
SEQ ID NO:2205	PSAP AGPPDDE	SEQ ID NO:2240	CDAPRERPSAPAGPP
SEQ ID NO:2206	RCDAPRERPSAP	SEQ ID NO:2241	DAPRERPSAPAGPPD
SEQ ID NO:2207	CDAPRERPSAPA	SEQ ID NO:2242	APRERPSAPAGPPDD
SEQ ID NO:2208	DAPRERPSAPAG	SEQ ID NO:2243	PRERPSAPAGPPDDE
SEQ ID NO:2209	APRERPSAPAGP	SEQ ID NO:2244	RERPSAPAGPPDDEA
SEQ ID NO:2210	PRERPSAPAGPP	SEQ ID NO:2245	ERPSAPAGPPDDEAL
SEQ ID NO:2211	RERPSAPAGPPD	SEQ ID NO:2246	RPSAPAGPPDDEALI
SEQ ID NO:2212	ERPSAPAGPPDD	SEQ ID NO:2247	PSAP AGPPDDEALIP
SEQ ID NO:2213	RPSAPAGPPDDE	SEQ ID NO:2248	ACAPRCDAPRERPSAP
SEQ ID NO:2214	PSAP AGPPDDEA	SEQ ID NO:2249	CAPRCDAPRERPSAPA
SEQ ID NO:2250	APRCDAPRERPSAPAG	SEQ ID NO:2287	ERPSAPAGPPDDEALIPP
SEQ ID NO:2251	PRCDAPRERPSAPAGP	SEQ ID NO:2288	RPSAPAGPPDDEALIPPW
SEQ ID NO:2252	RCDAPRERPSAPAGPP	SEQ ID NO:2289	PSAP AGPPDDEALIPPWL
SEQ ID NO:2253	CDAPRERPSAPAGPPD	SEQ ID NO:2290	RHCACAPRCDAPRERPSAP
SEQ ID NO:2254	DAPRERPSAPAGPPDD	SEQ ID NO:2291	HCACAPRCDAPRERPSAPA
SEQ ID NO:2255	APRERPSAPAGPPDDE	SEQ ID NO:2292	CACAPRCDAPRERPSAPAG
SEQ ID NO:2256	PRERPSAPAGPPDDEA	SEQ ID NO:2293	ACAPRCDAPRERPSAPAGP
SEQ ID NO:2257	RERPSAPAGPPDDEAL	SEQ ID NO:2294	CAPRCDAPRERPSAPAGPP
SEQ ID NO:2258	ERPSAPAGPPDDEALI	SEQ ID NO:2295	APRCDAPRERPSAPAGPPD
SEQ ID NO:2259	RPSAPAGPPDDEALIP	SEQ ID NO:2296	PRCDAPRERPSAPAGPPDD
SEQ ID NO:2260	PSAP AGPPDDEALIPP	SEQ ID NO:2297	RCDAPRERPSAPAGPPDDE
SEQ ID NO:2261	CACAPRCDAPRERPSAP	SEQ ID NO:2298	CDAPRERPSAPAGPPDDEA
SEQ ID NO:2262	ACAPRCDAPRERPSAPA	SEQ ID NO:2299	DAPRERPSAPAGPPDDEAL
SEQ ID NO:2263	CAPRCDAPRERPSAPAG	SEQ ID NO:2300	APRERPSAPAGPPDDEALI
SEQ ID NO:2264	APRCDAPRERPSAPAGP	SEQ ID NO:2301	PRERPSAPAGPPDDEALIP
SEQ ID NO:2265	PRCDAPRERPSAPAGPP	SEQ ID NO:2302	RERPSAPAGPPDDEALIPP
SEQ ID NO:2266	RCDAPRERPSAPAGPPD	SEQ ID NO:2303	ERPSAPAGPPDDEALIPPW
SEQ ID NO:2267	CDAPRERPSAPAGPPDD	SEQ ID NO:2304	RPSAPAGPPDDEALIPPWL
SEQ ID NO:2268	DAPRERPSAPAGPPDDE	SEQ ID NO:2305	PSAP AGPPDDEALIPPWLF
SEQ ID NO:2269	APRERPSAPAGPPDDEA	SEQ ID NO:2306	DRHCACAPRCDAPRERPSAP
SEQ ID NO:2270	PRERPSAPAGPPDDEAL	SEQ ID NO:2307	RHCACAPRCDAPRERPSAPA
SEQ ID NO:2271	RERPSAPAGPPDDEALI	SEQ ID NO:2308	HCACAPRCDAPRERPSAPAG
SEQ ID NO:2272	ERPSAPAGPPDDEALIP	SEQ ID NO:2309	CACAPRCDAPRERPSAPAGP
SEQ ID NO:2273	RPSAPAGPPDDEALIPP	SEQ ID NO:2310	ACAPRCDAPRERPSAPAGPP
SEQ ID NO:2274	PSAP AGPPDDEALIPPW	SEQ ID NO:2311	CAPRCDAPRERPSAPAGPPD
SEQ ID NO:2275	HCACAPRCDAPRERPSAP	SEQ ID NO:2312	APRCDAPRERPSAPAGPPDD
SEQ ID NO:2276	CACAPRCDAPRERPSAPA	SEQ ID NO:2313	PRCDAPRERPSAPAGPPDDE
SEQ ID NO:2277	ACAPRCDAPRERPSAPAG	SEQ ID NO:2314	RCDAPRERPSAPAGPPDDEA
SEQ ID NO:2278	CAPRCDAPRERPSAPAGP	SEQ ID NO:2315	CDAPRERPSAPAGPPDDEAL
SEQ ID NO:2279	APRCDAPRERPSAPAGPP	SEQ ID NO:2316	DAPRERPSAPAGPPDDEALI
SEQ ID NO:2280	PRCDAPRERPSAPAGPPD	SEQ ID NO:2317	APRERPSAPAGPPDDEALIP
SEQ ID NO:2281	RCDAPRERPSAPAGPPDD	SEQ ID NO:2318	PRERPSAPAGPPDDEALIPP
SEQ ID NO:2282	CDAPRERPSAPAGPPDDE	SEQ ID NO:2319	RERPSAPAGPPDDEALIPPW
SEQ ID NO:2283	DAPRERPSAPAGPPDDEA	SEQ ID NO:2320	ERPSAPAGPPDDEALIPPWL
SEQ ID NO:2284	APRERPSAPAGPPDDEAL	SEQ ID NO:2321	RPSAPAGPPDDEALIPPWLF
SEQ ID NO:2285	PRERPSAPAGPPDDEALI	SEQ ID NO:2322	PSAP AGPPDDEALIPPWLFA
SEQ ID NO:2286	RERPSAPAGPPDDEALIP

[0164]

TABLE 18
P(T/S)AP Motif Containing Peptides from Colorado Tick Fever Virus
VP12
(GenBank Accession No. AAB02025)
SEQ ID NO:2323	TRVAPSAP	SEQ ID NO:2358	ETPLSTRVAPSAP
SEQ ID NO:2324	RVAPSAPS	SEQ ID NO:2359	TPLSTRVAPSAPS
SEQ ID NO:2325	VAPSAPSA	SEQ ID NO:2360	PLSTRVAPSAPSA
SEQ ID NO:2326	APSAPSAS	SEQ ID NO:2361	LSTRVAPSAPSAS
SEQ ID NO:2327	PSAP SASL	SEQ ID NO:2362	STRVAPSAPSASL
SEQ ID NO:2328	STRVAPSAP	SEQ ID NO:2363	TRVAPSAPSASLF
SEQ ID NO:2329	TRVAPSAPS	SEQ ID NO:2364	RVAPSAPSASLFT
SEQ ID NO:2330	RVAPSAPSA	SEQ ID NO:2365	VAPSAPSASLFTA
SEQ ID NO:2331	VAPSAPSAS	SEQ ID NO:2366	APSAPSASLFTAG
SEQ ID NO:2332	APSAPSASL	SEQ ID NO:2367	PSAP SASLFTAGG
SEQ ID NO:2333	PSAP SASLF	SEQ ID NO:2368	CETPLSTRVAPSAP
SEQ ID NO:2334	LSTRVAPSAP	SEQ ID NO:2369	ETPLSTRVAPSAPS
SEQ ID NO:2335	STRVAPSAPS	SEQ ID NO:2370	TPLSTRVAPSAPSA
SEQ ID NO:2336	TRVAPSAPSA	SEQ ID NO:2371	PLSTRVAPSAPSAS
SEQ ID NO:2337	RVAPSAPSAS	SEQ ID NO:2372	LSTRVAPSAPSASL
SEQ ID NO:2338	VAPSAPSASL	SEQ ID NO:2373	STRVAPSAPSASLF
SEQ ID NO:2339	APSAPSASLF	SEQ ID NO:2374	TRVAPSAPSASLFT
SEQ ID NO:2340	PSAP SASLFT	SEQ ID NO:2375	RVAPSAPSASLFTA
SEQ ID NO:2341	PLSTRVAPSAP	SEQ ID NO:2376	VAPSAPSASLFTAG
SEQ ID NO:2342	LSTRVAPSAPS	SEQ ID NO:2377	APSAPSASLFTAGG
SEQ ID NO:2343	STRVAPSAPSA	SEQ ID NO:2378	PSAP SASLFTAGGI
SEQ ID NO:2344	TRVAPSAPSAS	SEQ ID NO:2379	ICETPLSTRVAPSAP
SEQ ID NO:2345	RVAPSAPSASL	SEQ ID NO:2380	CETPLSTRVAPSAPS
SEQ ID NO:2346	VAPSAPSASLF	SEQ ID NO:2381	ETPLSTRVAPSAPSA
SEQ ID NO:2347	APSAPSASLFT	SEQ ID NO:2382	TPLSTRVAPSAPSAS
SEQ ID NO:2348	PSAP SASLFTA	SEQ ID NO:2383	PLSTRVAPSAPSASL
SEQ ID NO:2349	TPLSTRVAPSAP	SEQ ID NO:2384	LSTRVAPSAPSASLF
SEQ ID NO:2350	PLSTRVAPSAPS	SEQ ID NO:2385	STRVAPSAPSASLFT
SEQ ID NO:2351	LSTRVAPSAPSA	SEQ ID NO:2386	TRVAPSAPSASLFTA
SEQ ID NO:2352	STRVAPSAPSAS	SEQ ID NO:2387	RVAPSAPSASLFTAG
SEQ ID NO:2353	TRVAPSAPSASL	SEQ ID NO:2388	VAPSAPSASLFTAGG
SEQ ID NO:2354	RVAPSAPSASLF	SEQ ID NO:2389	APSAPSASLFTAGGI
SEQ ID NO:2355	VAPSAPSASLFT	SEQ ID NO:2390	PSAP SASLFTAGGIG
SEQ ID NO:2356	APSAPSASLFTA	SEQ ID NO:2391	HICETPLSTRVAPSAP
SEQ ID NO:2357	PSAP SASLFTAG	SEQ ID NO:2392	ICETPLSTRVAPSAPS
SEQ ID NO:2393	CETPLSTRVAPSAPSA	SEQ ID NO:2427	STRVAPSAPSASLFTAGG
SEQ ID NO:2394	ETPLSTRVAPSAPSAS	SEQ ID NO:2428	TRVAPSAPSASLFTAGGI
SEQ ID NO:2395	TPLSTRVAPSAPSASL	SEQ ID NO:2429	RVAPSAPSASLFTAGGIG
SEQ ID NO:2396	PLSTRVAPSAPSASLF	SEQ ID NO:2430	VAPSAPSASLFTAGGIGL
SEQ ID NO:2397	LSTRVAPSAPSASLFT	SEQ ID NO:2431	APSAPSASLFTAGGIGLP
SEQ ID NO:2398	STRVAPSAPSASLFTA	SEQ ID NO:2432	ASPHICETPLSTRVAPSAP
SEQ ID NO:2399	TRVAPSAPSASLFTAG	SEQ ID NO:2433	SPHICETPLSTRVAPSAPS
SEQ ID NO:2400	RVAPSAPSASLFTAGG	SEQ ID NO:2434	PHICETPLSTRVAPSAPSA
SEQ ID NO:2401	VAPSAPSASLFTAGGI	SEQ ID NO:2435	HICETPLSTRVAPSAPSAS
SEQ ID NO:2402	APSAPSASLFTAGGIG	SEQ ID NO:2436	ICETPLSTRVAPSAPSASL
SEQ ID NO:2403	PSAP SASLFTAGGIGL	SEQ ID NO:2437	CETPLSTRVAPSAPSASLF
SEQ ID NO:2404	PHICETPLSTRVAPSAP	SEQ ID NO:2438	ETPLSTRVAPSAPSASLFT
SEQ ID NO:2405	HICETPLSTRVAPSAPS	SEQ ID NO:2439	TPLSTRVAPSAPSASLFTA
SEQ ID NO:2406	ICETPLSTRVAPSAPSA	SEQ ID NO:2440	PLSTRVAPSAPSASLFTAG
SEQ ID NO:2407	CETPLSTRVAPSAPSAS	SEQ ID NO:2441	LSTRVAPSAPSASLFTAGG
SEQ ID NO:2408	ETPLSTRVAPSAPSASL	SEQ ID NO:2442	STRVAPSAPSASLFTAGGI
SEQ ID NO:2409	TPLSTRVAPSAPSASLF	SEQ ID NO:2443	TRVAPSAPSASLFTAGGIG
SEQ ID NO:2410	PLSTRVAPSAPSASLFT	SEQ ID NO:2444	RVAPSAPSASLFTAGGIGL
SEQ ID NO:2411	LSTRVAPSAPSASLFTA	SEQ ID NO:2445	VAPSAPSASLFTAGGIGLP
SEQ ID NO:2412	STRVAPSAPSASLFTAG	SEQ ID NO:2446	PASPHICETPLSTRVAPSAP
SEQ ID NO:2413	TRVAPSAPSASLFTAGG	SEQ ID NO:2447	ASPHICETPLSTRVAPSAPS
SEQ ID NO:2414	RVAPSAPSASLFTAGGI	SEQ ID NO:2448	SPHICETPLSTRVAPSAPSA
SEQ ID NO:2415	VAPSAPSASLFTAGGIG	SEQ ID NO:2449	PHICETPLSTRVAPSAPSAS
SEQ ID NO:2416	APSAPSASLFTAGGIGL	SEQ ID NO:2450	HICETPLSTRVAPSAPSASL
SEQ ID NO:2417	PSAP SASLFTAGGIGLP	SEQ ID NO:2451	ICETPLSTRVAPSAPSASLF
SEQ ID NO:2418	SPHICETPLSTRVAPSAP	SEQ ID NO:2452	CETPLSTRVAPSAPSASLFT
SEQ ID NO:2419	PHICETPLSTRVAPSAPS	SEQ ID NO:2453	ETPLSTRVAPSAPSASLFTA
SEQ ID NO:2420	HICETPLSTRVAPSAPSA	SEQ ID NO:2454	TPLSTRVAPSAPSASLFTAG
SEQ ID NO:2421	ICETPLSTRVAPSAPSAS	SEQ ID NO:2455	PLSTRVAPSAPSASLFTAGG
SEQ ID NO:2422	CETPLSTRVAPSAPSASL	SEQ ID NO:2456	LSTRVAPSAPSASLFTAGGI
SEQ ID NO:2423	ETPLSTRVAPSAPSASLF	SEQ ID NO:2457	STRVAPSAPSASLFTAGGIG
SEQ ID NO:2424	TPLSTRVAPSAPSASLFT	SEQ ID NO:2458	TRVAPSAPSASLFTAGGIGL
SEQ ID NO:2425	PLSTRVAPSAPSASLFTA	SEQ ID NO:2459	RVAPSAPSASLFTAGGIGLP
SEQ ID NO:2426	LSTRVAPSAPSASLFTAG

[0165]

TABLE 19
P(T/S)AP Motif Containing Peptides from Foot and Mouth Disease Virus
VP1 Capsid Protein
(GenBank Accession No. AAA42637)
SEQ ID NO:2460	RLALPTAP	SEQ ID NO:2495	AKALTRLALPTAP
SEQ ID NO:2461	LALPTAPR	SEQ ID NO:2496	KALTRLALPTAPR
SEQ ID NO:2462	ALPTAPRV	SEQ ID NO:2497	ALTRLALPTAPRV
SEQ ID NO:2463	LPTAPRVL	SEQ ID NO:2498	LTRLALPTAPRVL
SEQ ID NO:2464	PTAP RVLA	SEQ ID NO:2499	TRLALPTAPRVLA
SEQ ID NO:2465	TRLALPTAP	SEQ ID NO:2500	RLALPTAPRVLAT
SEQ ID NO:2466	RLALPTAPR	SEQ ID NO:2501	LALPTAPRVLATV
SEQ ID NO:2467	LALPTAPRV	SEQ ID NO:2502	ALPTAPRVLATVG
SEQ ID NO:2468	ALPTAPRVL	SEQ ID NO:2503	LPTAPRVLATVGE
SEQ ID NO:2469	LPTAPRVLA	SEQ ID NO:2504	PTAP RVLATVGEC
SEQ ID NO:2470	PTAP RVLAT	SEQ ID NO:2505	TAKALTRLALPTAP
SEQ ID NO:2471	LTRLALPTAP	SEQ ID NO:2506	AKALTRLALPTAPR
SEQ ID NO:2472	TRLALPTAPR	SEQ ID NO:2507	KALTRLALPTAPRV
SEQ ID NO:2473	RLALPTAPRV	SEQ ID NO:2508	ALTRLALPTAPRVL
SEQ ID NO:2474	LALPTAPRVL	SEQ ID NO:2509	LTRLALPTAPRVLA
SEQ ID NO:2475	ALPTAPRVLA	SEQ ID NO:2510	TRLALPTAPRVLAT
SEQ ID NO:2476	LPTAPRVLAT	SEQ ID NO:2511	RLALPTAPRVLATV
SEQ ID NO:2477	PTAP RVLATV	SEQ ID NO:2512	LALPTAPRVLATVG
SEQ ID NO:2478	ALTRLALPTAP	SEQ ID NO:2513	ALPTAPRVLATVGE
SEQ ID NO:2479	LTRLALPTAPR	SEQ ID NO:2514	LPTAPRVLATVGEC
SEQ ID NO:2480	TRLALPTAPRV	SEQ ID NO:2515	PTAP RVLATVGECR
SEQ ID NO:2481	RLALPTAPRVL	SEQ ID NO:2516	DTAKALTRLALPTAP
SEQ ID NO:2482	LALPTAPRVLA	SEQ ID NO:2517	TAKALTRLALPTAPR
SEQ ID NO:2483	ALPTAPRVLAT	SEQ ID NO:2518	AKALTRLALPTAPRV
SEQ ID NO:2484	LPTAPRVLATV	SEQ ID NO:2519	KALTRLALPTAPRVL
SEQ ID NO:2485	PTAP RVLATVG	SEQ ID NO:2520	ALTRLALPTAPRVLA
SEQ ID NO:2486	KALTRLALPTAP	SEQ ID NO:2521	LTRLALPTAPRVLAT
SEQ ID NO:2487	ALTRLALPTAPR	SEQ ID NO:2522	TRLALPTAPRVLATV
SEQ ID NO:2488	LTRLALPTAPRV	SEQ ID NO:2523	RLALPTAPRVLATVG
SEQ ID NO:2489	TRLALPTAPRVL	SEQ ID NO:2524	LALPTAPRVLATVGE
SEQ ID NO:2490	RLALPTAPRVLA	SEQ ID NO:2525	ALPTAPRVLATVGEC
SEQ ID NO:2491	LALPTAPRVLAT	SEQ ID NO:2526	LPTAPRVLATVGECR
SEQ ID NO:2492	ALPTAPRVLATV	SEQ ID NO:2527	PTAP RVLATVGECRY
SEQ ID NO:2493	LPTAPRVLATVG	SEQ ID NO:2528	LDTAKALTRLALPTAP
SEQ ID NO:2494	PTAP RVLATVGE	SEQ ID NO:2529	DTAKALTRLALPTAPR
SEQ ID NO:2530	TAKALTRLALPTAPRV	SEQ ID NO:2567	ALPTAPRVLATVGECRYS
SEQ ID NO:2531	AKALTRLALPTAPRVL	SEQ ID NO:2568	LPTAPRVLATVGECRYSR
SEQ ID NO:2532	KALTRLALPTAPRVLA	SEQ ID NO:2569	PTAP RVLATVGECRYSRN
SEQ ID NO:2533	ALTRLALPTAPRVLAT	SEQ ID NO:2570	EKALDTAKALTRLALPTAP
SEQ ID NO:2534	LTRLALPTAPRVLATV	SEQ ID NO:2571	KALDTAKALTRLALPTAPR
SEQ ID NO:2535	TRLALPTAPRVLATVG	SEQ ID NO:2572	ALDTAKALTRLALPTAPRV
SEQ ID NO:2536	RLALPTAPRVLATVGE	SEQ ID NO:2573	LDTAKALTRLALPTAPRVL
SEQ ID NO:2537	LALPTAPRVLATVGEC	SEQ ID NO:2574	DTAKALTRLALPTAPRVLA
SEQ ID NO:2538	ALPTAPRVLATVGECR	SEQ ID NO:2575	TAKALTRLALPTAPRVLAT
SEQ ID NO:2539	LPTAPRVLATVGECRY	SEQ ID NO:2576	AKALTRLALPTAPRVLATV
SEQ ID NO:2540	PTAP RVLATVGECRYS	SEQ ID NO:2577	KALTRLALPTAPRVLATVG
SEQ ID NO:2541	ALDTAKALTRLALPTAP	SEQ ID NO:2578	ALTRLALPTAPRVLATVGE
SEQ ID NO:2542	LDTAKALTRLALPTAPR	SEQ ID NO:2579	LTRLALPTAPRVLATVGEC
SEQ ID NO:2543	DTAKALTRLALPTAPRV	SEQ ID NO:2580	TRLALPTAPRVLATVGECR
SEQ ID NO:2544	TAKALTRLALPTAPRVL	SEQ ID NO:2581	RLALPTAPRVLATVGECRY
SEQ ID NO:2545	AKALTRLALPTAPRVLA	SEQ ID NO:2582	LALPTAPRVLATVGECRYS
SEQ ID NO:2546	KALTRLALPTAPRVLAT	SEQ ID NO:2583	ALPTAPRVLATVGECRYSR
SEQ ID NO:2547	ALTRLALPTAPRVLATV	SEQ ID NO:2584	LPTAPRVLATVGECRYSRN
SEQ ID NO:2548	LTRLALPTAPRVLATVG	SEQ ID NO:2585	PTAP RVLATVGECRYSRNA
SEQ ID NO:2549	TRLALPTAPRVLATVGE	SEQ ID NO:2586	PEKALDTAKALTRLALPTAP
SEQ ID NO:2550	RLALPTAPRVLATVGEC	SEQ ID NO:2587	EKALDTAKALTRLALPTAPR
SEQ ID NO:2551	LALPTAPRVLATVGECR	SEQ ID NO:2588	KALDTAKALTRLALPTAPRV
SEQ ID NO:2552	ALPTAPRVLATVGECRY	SEQ ID NO:2589	ALDTAKALTRLALPTAPRVL
SEQ ID NO:2553	LPTAPRVLATVGECRYS	SEQ ID NO:2590	LDTAKALTRLALPTAPRVLA
SEQ ID NO:2554	PTAP RVLATVGECRYSR	SEQ ID NO:2591	DTAKALTRLALPTAPRVLAT
SEQ ID NO:2555	KALDTAKALTRLALPTAP	SEQ ID NO:2592	TAKALTRLALPTAPRVLATV
SEQ ID NO:2556	ALDTAKALTRLALPTAPR	SEQ ID NO:2593	AKALTRLALPTAPRVLATVG
SEQ ID NO:2557	LDTAKALTRLALPTAPRV	SEQ ID NO:2594	KALTRLALPTAPRVLATVGE
SEQ ID NO:2558	DTAKALTRLALPTAPRVL	SEQ ID NO:2595	ALTRLALPTAPRVLATVGEC
SEQ ID NO:2559	TAKALTRLALPTAPRVLA	SEQ ID NO:2596	LTRLALPTAPRVLATVGECR
SEQ ID NO:2560	AKALTRLALPTAPRVLAT	SEQ ID NO:2597	TRLALPTAPRVLATVGECRY
SEQ ID NO:2561	KALTRLALPTAPRVLATV	SEQ ID NO:2598	RLALPTAPRVLATVGECRYS
SEQ ID NO:2562	ALTRLALPTAPRVLATVG	SEQ ID NO:2599	LALPTAPRVLATVGECRYSR
SEQ ID NO:2563	LTRLALPTAPRVLATVGE	SEQ ID NO:2600	ALPTAPRVLATVGECRYSRN
SEQ ID NO:2564	TRLALPTAPRVLATVGEC	SEQ ID NO:2601	LPTAPRVLATVGECRYSRNA
SEQ ID NO:2565	RLALPTAPRVLATVGECR	SEQ ID NO:2602	PTAP RVLATVGECRYSRNAP
SEQ ID NO:2566	LALPTAPRVLATVGECRY

[0166]

TABLE 20
P(T/S)AP Motif Containing Peptides from Human Foamy Virus
Gag Protein
(GenBank Accession No. NP_044279)
SEQ ID NO:2603	PAPVPSAP	SEQ ID NO:2638 RREILPAPVPSAP
SEQ ID NO:2604	APVPSAPP	SEQ ID NO:2639 REILPAPVPSAPP
SEQ ID NO:2605	PVPSAPPM	SEQ ID NO:2640 EILPAPVPSAPPM
SEQ ID NO:2606	VPSAPPMI	SEQ ID NO:2641 ILPAPVPSAPPMI
SEQ ID NO:2607	PSAP PMIQ	SEQ ID NO:2642 LPAPVPSAPPMIQ
SEQ ID NO:2608	LPAPVPSAP	SEQ ID NO:2643 PAPVPSAPPMIQY
SEQ ID NO:2609	PAPVPSAPP	SEQ ID NO:2644 APVPSAPPMIQYI
SEQ ID NO:2610	APVPSAPPM	SEQ ID NO:2645 PVPSAPPMIQYIP
SEQ ID NO:2611	PVPSAPPMI	SEQ ID NO:2646 VPSAPPMIQYIPV
SEQ ID NO:2612	VPSAPPMIQ	SEQ ID NO:2647 PSAPPMIQYIPVP
SEQ ID NO:2613	PSAP PMIQY	SEQ ID NO:2648 RRREILPAPVPSAP
SEQ ID NO:2614	ILPAPVPSAP	SEQ ID NO:2649 RREILPAPVPSAPP
SEQ ID NO:2615	LPAPVPSAPP	SEQ ID NO:2650 REILPAPVPSAPPM
SEQ ID NO:2616	PAPVPSAPPM	SEQ ID NO:2651 EILPAPVPSAPPMI
SEQ ID NO:2617	APVPSAPPMI	SEQ ID NO:2652 ILPAPVPSAPPMIQ
SEQ ID NO:2618	PVPSAPPMIQ	SEQ ID NO:2653 LPAPVPSAPPMIQY
SEQ ID NO:2619	VPSAPPMIQY	SEQ ID NO:2654 PAPVPSAPPMIQYI
SEQ ID NO:2620	PSAP PMIQYI	SEQ ID NO:2655 APVPSAPPMIQYIP
SEQ ID NO:2621	EILPAPVPSAP	SEQ ID NO:2656 PVPSAPPMIQYIPV
SEQ ID NO:2622	ILPAPVPSAPP	SEQ ID NO:2657 VPSAPPMIQYIPVP
SEQ ID NO:2623	LPAPVPSAPPM	SEQ ID NO:2658 PSAPPMIQYIPVPP
SEQ ID NO:2624	PAPVPSAPPMI	SEQ ID NO:2659 ERRREILPAPVPSAP
SEQ ID NO:2625	APVPSAPPMIQ	SEQ ID NO:2660 RRREWPAPVPSAPP
SEQ ID NO:2626	PVPSAPPMIQY	SEQ ID NO:2661 RREILPAPVPSAPPM
SEQ ID NO:2627	VPSAPPMIQYI	SEQ ID NO:2662 REILPAPVPSAPPMI
SEQ ID NO:2628	PSAP PMIQYIP	SEQ ID NO:2663 EILPAPVPSAPPMIQ
SEQ ID NO:2629	REILPAPVPSAP	SEQ ID NO:2664 ILPAPVPSAPPMIQY
SEQ ID NO:2630	EILPAPVPSAPP	SEQ ID NO:2665 LPAPVPSAPPMIQYI
SEQ ID NO:2631	ILPAPVPSAPPM	SEQ ID NO:2666 PAPVPSAPPMIQYIP
SEQ ID NO:2632	LPAPVPSAPPMI	SEQ ID NO:2667 APVPSAPPMIQYIPV
SEQ ID NO:2633	PAPVPSAPPMIQ	SEQ ID NO:2668 PVPSAPPMIQYIPVP
SEQ ID NO:2634	APVPSAPPMIQY	SEQ ID NO:2669 VPSAPPMIQYIPVPP
SEQ ID NO:2635	PVPSAPPMIQYI	SEQ ID NO:2670 PSAPPMIQYIPVPPP
SEQ ID NO:2636	VPSAPPMIQYIP	SEQ ID NO:2671 RERRREILPAPVPSAP
SEQ ID NO:2637	PSAP PMIQYIPV	SEQ ID NO:2672 ERRREILPAPVPSAPP
SEQ ID NO:2673	RRREILPAPVPSAPPM	SEQ ID NO:2710 PVPSAPPMIQYIPVPPPP
SEQ ID NO:2674	RREILPAPVPSAPPMI	SEQ ID NO:2711 VPSAPPMIQYIPVPPPPP
SEQ ID NO:2675	REILPAPVPSAPPMIQ	SEQ ID NO:2712 PSAPPMIQYIPVPPPPPI
SEQ ID NO:2676	EILPAPVPSAPPMIQY	SEQ ID NO:2713 SQSRERRREILPAPVPSAP
SEQ ID NO:2677	ILPAPVPSAPPMIQYI	SEQ ID NO:2714 QSRERRREILPAPVPSAPP
SEQ ID NO:2678	LPAPVPSAPPMIQYIP	SEQ ID NO:2715 SRERRREILPAPVPSAPPM
SEQ ID NO:2679	PAPVPSAPPMIQYIPV	SEQ ID NO:2716 RERRREILPAPVPSAPPMI
SEQ ID NO:2680	APVPSAPPMIQYIPVP	SEQ ID NO:2717 ERRREILPAPVPSAPPMIQ
SEQ ID NO:2681	PVPSAPPMIQYIPVPP	SEQ ID NO:2718 RRREILPAPVPSAPPMIQY
SEQ ID NO:2682	VPSAPPMIQYIPVPPP	SEQ ID NO:2719 RREILPAPVPSAPPMIQYI
SEQ ID NO:2683	PSAP PMIQYIPVPPPP	SEQ ID NO:2720 REILPAPVPSAPPMIQYIP
SEQ ID NO:2684	SRERRREILPAPVPSAP	SEQ ID NO:2721 EILPAPVPSAPPMIQYIPV
SEQ ID NO:2685	RERRREILPAPVPSAPP	SEQ ID NO:2722 ILPAPVPSAPPMIQYIPVP
SEQ ID NO:2686	ERRREILPAPVPSAPPM	SEQ ID NO:2723 LPAPVPSAPPMIQYIPVPP
SEQ ID NO:2687	RRREILPAPVPSAPPMI	SEQ ID NO:2724 PAPVPSAPPMIQYIPVPPP
SEQ ID NO:2688	RREILPAPVPSAPPMIQ	SEQ ID NO:2725 APVPSAPPMIQYIPVPPPP
SEQ ID NO:2689	REILPAPVPSAPPMIQY	SEQ ID NO:2726 PVPSAPPMIQYIPVPPPPP
SEQ ID NO:2690	EILPAPVPSAPPMIQYI	SEQ ID NO:2727 VPSAPPMIQYIPVPPPPPI
SEQ ID NO:2691	IILPAPVPSAPPMIQYIP	SEQ ID NO:2728 PSAPPMIQYIPVPPPPPIG
SEQ ID NO:2692	LPAPVPSAPPMIQYIPV	SEQ ID NO:2729 RSQSRERRREILPAPVPSAP
SEQ ID NO:2693	PAPVPSAPPMIQYIPVP	SEQ ID NO:2730 SQSRERRREILPAPVPSAPP
SEQ ID NO:2694	APVPSAPPMIQYIPVPP	SEQ ID NO:2731 QSRERRREILPAPVPSAPPM
SEQ ID NO:2695	PVPSAPPMIQYIPVPPP	SEQ ID NO:2732 SRERRREILPAPVPSAPPMI
SEQ ID NO:2696	VPSAPPMIQYIPVPPPP	SEQ ID NO:2733 RERRREILPAPVPSAPPMIQ
SEQ ID NO:2697	PSAP PMIQYIPVPPPPP	SEQ ID NO:2734 ERRREILPAPVPSAPPMIQY
SEQ ID NO:2698	QSRERRREILPAPVPSAP	SEQ ID NO:2735 RRREILPAPVPSAPPMIQYI
SEQ ID NO:2699	SRERRREILPAPVPSAPP	SEQ ID NO:2736 RREILPAPVPSAPPMIQYIP
SEQ ID NO:2700	RERRREILPAPVPSAPPM	SEQ ID NO:2737 REILPAPVPSAPPMIQYIPV
SEQ ID NO:2701	ERRREILPAPVPSAPPMI	SEQ ID NO:2738 EILPAPVPSAPPMIQYIPVP
SEQ ID NO:2702	RRREILPAPVPSAPPMIQ	SEQ ID NO:2739 ILPAPVPSAPPMIQYIPVPP
SEQ ID NO:2703	RREILPAPVPSAPPMIQY	SEQ ID NO:2740 LPAPVPSAPPMIQYIPVPPP
SEQ ID NO:2704	REILPAPVPSAPPMIQYI	SEQ ID NO:2741 PAPVPSAPPMIQYIPVPPPP
SEQ ID NO:2705	EILPAPVPSAPPMIQYIP	SEQ ID NO:2742 APVPSAPPMIQYIPVPPPPP
SEQ ID NO:2706	ILPAPVPSAPPMIQYIPV	SEQ ID NO:2743 PVPSAPPMIQYIPVPPPPPI
SEQ ID NO:2707	LPAPVPSAPPMIQYIPVP	SEQ ID NO:2744 VPSAPPMIQYIPVPPPPPIG
SEQ ID NO:2708	PAPVPSAPPMIQYIPVPP	SEQ ID NO:2745 PSAPPMIQYIPVPPPPPIGT
SEQ ID NO:2709	APVPSAPPMIQYIPVPPP

[0167]

TABLE 21
P(T/S)AP Motif Containing Peptides from Hepatitis E Virus
ORF-3 Protein
(GenBank Accession No. AAC35758)
SEQ ID NO:2746	GVTRPSAP	SEQ ID NO:2781 HSAPLGVTRPSAP
SEQ ID NO:2747	VTRPSAPP	SEQ ID NO:2782	SAPLGVTRPSAPP
SEQ ID NO:2748	TRPSAPPL	SEQ ID NO:2783	APLGVTRPSAPPL
SEQ ID NO:2749	RPSAPPLP	SEQ ID NO:2784	PLGVTRPSAPPLP
SEQ ID NO:275O	PSAP PLPH	SEQ ID NO:2785	LGVTRPSAPPLPH
SEQ ID NO:2751	LGVTRPSAP	SEQ ID NO:2786	GVTRPSAPPLPHV
SEQ ID NO:2752	GVTRPSAPP	SEQ ID NO:2787	VTRPSAPPLPHVV
SEQ ID NO:2753	VTRPSAPPL	SEQ ID NO:2788	TRPSAPPLPHVVD
SEQ ID NO:2754	TRPSAPPLP	SEQ ID NO:2789	RPSAPPLPHVVDL
SEQ ID NO:2755	RPSAPPLPH	SEQ ID NO:2790	PSAP PLPHVVDLP
SEQ ID NO:2756	PSAP PLPHV	SEQ ID NO:2791	DHSAPLGVTRPSAP
SEQ ID NO:2757	PLGVTRPSAP	SEQ ID NO:2792	HSAPLGVTRPSAPP
SEQ ID NO:2758	LGVTRPSAPP	SEQ ID NO:2793	SAPLGVTRPSAPPL
SEQ ID NO:2759	GVTRPSAPPL	SEQ ID NO:2794	APLGVTRPSAPPLP
SEQ ID NO:2760	VTRPSAPPLP	SEQ ID NO:2795	PLGVTRPSAPPLPH
SEQ ID NO:2761	TRPSAPPLPH	SEQ ID NO:2796	LGVTRPSAPPLPHV
SEQ ID NO:2762	RPSAPPLPHV	SEQ ID NO:2797	GVTRPSAPPLPHVV
SEQ ID NO:2763	PSAP PLPHVV	SEQ ID NO:2798	VTRPSAPPLPHVVD
SEQ ID NO:2764	APLGVTRPSAP	SEQ ID NO:2799	TRPSAPPLPHVVDL
SEQ ID NO:2765	PLGVTRPSAPP	SEQ ID NO:2800	RPSAPPLPHVVDLP
SEQ ID NO:2766	LGVTRPSAPPL	SEQ ID NO:2801	PSAP PLPHVVDLPQ
SEQ ID NO:2767	GVTRPSAPPLP	SEQ ID NO:2802	PDHSAPLGVTRPSAP
SEQ ID NO:2768	VTRPSAPPLPH	SEQ ID NO:2803	DHSAPLGVTRPSAPP
SEQ ID NO:2769	TRPSAPPLPHV	SEQ ID NO:2804	HSAPLGVTRPSAPPL
SEQ ID NO:2770	RPSAPPLPHVV	SEQ ID NO:2805	SAPLGVTRPSAPPLP
SEQ ID NO:2771	PSAP PLPHVVD	SEQ ID NO:2806	APLGVTRPSAPPLPH
SEQ ID NO:2772	SAPLGVTRPSAP	SEQ ID NO:2807	PLGVTRPSAPPLPHV
SEQ ID NO:2773	APLGVTRPSAPP	SEQ ID NO:2808	LGVTRPSAPPLPHVV
SEQ ID NO:2774	PLGVTRPSAPPL	SEQ ID NO:2809	GVTRPSAPPLPHVVD
SEQ ID NO:2775	LGVTRPSAPPLP	SEQ ID NO:2810	VTRPSAPPLPHVVDL
SEQ ID NO:2776	GVTRPSAPPLPH	SEQ ID NO:2811	TRPSAPPLPHVVDLP
SEQ ID NO:2777	VTRPSAPPLPHV	SEQ ID NO:2812	RPSAPPLPHVVDLPQ
SEQ ID NO:2778	TRPSAPPLPHVV	SEQ ID NO:2813	PSAP PLPHVVDLPQL
SEQ ID NO:2779	RPSAPPLPHVVD	SEQ ID NO:2814	LPDHSAPLGVTRPSAP
SEQ ID NO:2780	PSAP PLPHVVDL	SEQ ID NO:2815	PDHSAPLGVTRPSAPP
SEQ ID NO:2816	DHSAPLGVTRPSAPPL	SEQ ID NO:2853	TRPSAPPLPHVVDLPQLG
SEQ ID NO:2817	HSAPLGVTRPSAPPLP	SEQ ID NO:2854	RPSAPPLPHVVDLPQLGP
SEQ ID NO:2818	SAPLGVTRPSAPPLPH	SEQ ID NO:2855	PSAP PLPHVVDLPQLGPR
SEQ ID NO:2819	APLGVTRPSAPPLPHV	SEQ ID NO:2856	FANLPDHSAPLGVTRPSAP
SEQ ID NO:2820	PLGVTRPSAPPLPHVV	SEQ ID NO:2857	ANLPDHSAPLGVTRPSAPP
SEQ ID NO:2821	LGVTRPSAPPLPHVVD	SEQ ID NO:2858	NLPDHSAPLGVTRPSAPPL
SEQ ID NO:2822	GVTRPSAPPLPHVVDL	SEQ ID NO:2859	LPDHSAPLGVTRPSAPPLP
SEQ ID NO:2823	VTRPSAPPLPHVVDLP	SEQ ID NO:2860	PDHSAPLGVTRPSAPPLPH
SEQ ID NO:2824	TRPSAPPLPHVVDLPQ	SEQ ID NO:2861	DHSAPLGVTRPSAPPLPHV
SEQ ID NO:2825	RPSAPPLPHVVDLPQL	SEQ ID NO:2862	HSAPLGVTRPSAPPLPHVV
SEQ ID NO:2826	PSAP PLPHVVDLPQLG	SEQ ID NO:2863	SAPLGVTRPSAPPLPHVVD
SEQ ID NO:2827	NLPDHSAPLGVTRPSAP	SEQ ID NO:2864	APLGVTRPSAPPLPHVVDL
SEQ ID NO:2828	LPDHSAPLGVTRPSAPP	SEQ ID NO:2865	PLGVTRPSAPPLPHVVDLP
SEQ ID NO:2829	PDHSAPLGVTRPSAPPL	SEQ ID NO:2866	LGVTRPSAPPLPHVVDLPQ
SEQ ID NO:2830	DHSAPLGVTRPSAPPLP	SEQ ID NO:2867	GVTRPSAPPLPHVVDLPQL
SEQ ID NO:2831	HSAPLGVTRPSAPPLPH	SEQ ID NO:2868	VTRPSAPPLPHVVDLPQLG
SEQ ID NO:2832	SAPLGVTRPSAPPLPHV	SEQ ID NO:2869	TRPSAPPLPHVVDLPQLGP
SEQ ID NO:2833	APLGVTRPSAPPLPHVV	SEQ ID NO:2870	RPSAPPLPHVVDLPQLGPR
SEQ ID NO:2834	PLGVTRPSAPPLPHVVD	SEQ ID NO:2871	PSAP PLPHVVDLPQLGPRR
SEQ ID NO:2835	LGVTRPSAPPLPHVVDL	SEQ ID NO:2872	VFANLPDHSAPLGVTRPSAP
SEQ ID NO:2836	GVTRPSAPPLPHVVDLP	SEQ ID NO:2873	FANLPDHSAPLGVTRPSAPP
SEQ ID NO:2837	VTRPSAPPLPHVVDLPQ	SEQ ID NO:2874	ANLPDHSAPLGVTRPSAPPL
SEQ ID NO:2838	TRPSAPPLPHVVDLPQL	SEQ ID NO:2875	NLPDHSAPLGVTRPSAPPLP
SEQ ID NO:2839	RPSAPPLPHVVDLPQLG	SEQ ID NO:2876	LPDHSAPLGVTRPSAPPLPH
SEQ ID NO:2840	PSAP PLPHVVDLPQLGP	SEQ ID NO:2877	PDHSAPLGVTRPSAPPLPHV
SEQ ID NO:2841	ANLPDHSAPLGVTRPSAP	SEQ ID NO:2878	DHSAPLGVTRPSAPPLPHVV
SEQ ID NO:2842	NLPDHSAPLGVTRPSAPP	SEQ ID NO:2879	HSAPLGVTRPSAPPLPHVVD
SEQ ID NO:2843	LPDHSAPLGVTRPSAPPL	SEQ ID NO:2880	SAPLGVTRPSAPPLPHVVDL
SEQ ID NO:2844	PDHSAPLGVTRPSAPPLP	SEQ ID NO:2881	APLGVTRPSAPPLPHVVDLP
SEQ ID NO:2845	DHSAPLGVTRPSAPPLPH	SEQ ID NO:2882	PLGVTRPSAPPLPHVVDLPQ
SEQ ID NO:2846	HSAPLGVTRPSAPPLPHV	SEQ ID NO:2883	LGVTRPSAPPLPHVVDLPQL
SEQ ID NO:2847	SAPLGVTRPSAPPLPHVV	SEQ ID NO:2884	GVTRPSAPPLPHVVDLPQLG
SEQ ID NO:2848	APLGVTRPSAPPLPHVVD	SEQ ID NO:2885	VTRPSAPPLPHVVDLPQLGP
SEQ ID NO:2849	PLGVTRPSAPPLPHVVDL	SEQ ID NO:2886	TRPSAPPLPHVVDLPQLGPR
SEQ ID NO:2850	LGVTRPSAPPLPHVVDLP	SEQ ID NO:2887	RPSAPPLPHVVDLPQLGPRR
SEQ ID NO:2851	GVTRPSAPPLPHVVDLPQ
SEQ ID NO:2852	VTRPSAPPLPHVVDLPQL

[0168]

TABLE 22
P(T/S)AP Motif Containing Peptides from Hepatitis
G Virus
Polyprotein
(GenBank Accession No. AAB65834)
PGFVPTAP                         SEQ ID NO: 2888
GFVPTAPV                         SEQ ID NO: 2889
FVPTAPVV                         SEQ ID NO: 2890
VPTAPVVI                         SEQ ID NO: 2891
PTAP                  VVIR       SEQ ID NO: 2892
PPGFVPTAP                        SEQ ID NO: 2893
PGFVPTAPV                        SEQ ID NO: 2894
GFVPTAPVV                        SEQ ID NO: 2895
FVPTAPVVI                        SEQ ID NO: 2896
VPTAPVVIR                        SEQ ID NO: 2897
PTAP                  VVIRR      SEQ ID NO: 2898
LPPGFVPTAP                       SEQ ID NO: 2899
PPGFVPTAPV                       SEQ ID NO: 2900
PGFVPTAPVV                       SEQ ID NO: 2901
GFVPTAPVVI                       SEQ ID NO: 2902
FVPTAPVVIR                       SEQ ID NO: 2903
VPTAPVVIRR                       SEQ ID NO: 2904
PTAP                  VVIRRC     SEQ ID NO: 2905
HLPPGFVPTAP                      SEQ ID NO: 2906
LPPGFVPTAPV                      SEQ ID NO: 2907
PPGFVPTAPVV                      SEQ ID NO: 2908
PGFVPTAPVVI                      SEQ ID NO: 2909
GFVPTAPVVIR                      SEQ ID NO: 2910
FVPTAPVVIRR                      SEQ ID NO: 2911
VPTAPVVIRRC                      SEQ ID NO: 2912
PTAP                  VVIRRCG    SEQ ID NO: 2913
NHLPPGFVPTAP                     SEQ ID NO: 2914
HLPPGFVPTAPV                     SEQ ID NO: 2915
LPPGFVPTAPVV                     SEQ ID NO: 2916
PPGFVPTAPVVI                     SEQ ID NO: 2917
PGFVPTAPVVIR                     SEQ ID NO: 2918
GFVPTAPVVIRR                     SEQ ID NO: 2919
FVPTAPVVIRRC                     SEQ ID NO: 2920
VPTAPVVIRRCG                     SEQ ID NO: 2921
PTAP                  VVIRRCGK   SEQ ID NO: 2922
VNHLPPGFVPTAP                    SEQ ID NO: 2923
NHLPPGFVPTAPV                    SEQ ID NO: 2924
HLPPGFVPTAPVV                    SEQ ID NO: 2925
LPPGFVPTAPVVI                    SEQ ID NO: 2926
PPGFVPTAPVVIR                    SEQ ID NO: 2927
PGFVPTAPVVIRR                    SEQ ID NO: 2928
GFVPTAPVV1RRC                    SEQ ID NO: 2929
FVPTAPVVIRRCG                    SEQ ID NO: 2930
VPTAPVVIRRCGK                    SEQ ID NO: 2931
PTAP                  VVIRRCGKG  SEQ ID NO: 2932
DVNHLPPGFVPTAP                   SEQ ID NO: 2933
VNHLPPGFVPTAPV                   SEQ ID NO: 2934
NHLPPGFVPTAPVV                   SEQ ID NO: 2935
HLPPGFVPTAPVVI                   SEQ ID NO: 2936
LPPGFVPTAPVVIR                   SEQ ID NO: 2937
PPGFVPTAPVVJRR                   SEQ ID NO: 2938
PGFVPTAPVVIRRC                   SEQ ID NO: 2939
GFVPTAPVVJRRCG                   SEQ ID NO: 2940
FVPTAPVVIRRCGK                   SEQ ID NO: 2941
VPTAPVVLRRCGKG                   SEQ ID NO: 2942
PTAP                  VVIRRCGKGF SEQ ID NO: 2943
QDVNHLPPGFVPTAP                  SEQ ID NO: 2944
DVNHLPPGFVPTAPV                  SEQ ID NO: 2945
VNHLPPGFVPTAPVV                  SEQ ID NO: 2946
NHLPPGFVPTAPVVI                  SEQ ID NO: 2947
HLPPGFVPTAPVVIR                  SEQ ID NO: 2948
LPPGFVPTAPVVIRR                  SEQ ID NO: 2949
PPGFVPTAPVVIRRC                  SEQ ID NO: 2950
PGFVPTAPVVIRRCG                  SEQ ID NO: 2951
GFVPTAPVVIRRCGK                  SEQ ID NO: 2952
FVPTAPVVIRRCGKG                  SEQ ID NO: 2953
VPTAPVVIRRCGKGF                  SEQ ID NO: 2954
PTAP                  VVIRRCGKGFL SEQ ID NO: 2955
FQDVNHLPPGFVPTAP                 SEQ ID NO: 2956
QDVNHLPPGFVPTAPV                 SEQ ID NO: 2957
DVNHLPPGFVPTAPVV                 SEQ ID NO: 2958
VNhLPPGFVPTAPVVI                 SEQ ID NO: 2959
NHLPPGFVPTAPVVIR                 SEQ ID NO: 2960
HLPPGFVPTAPVVIRR                 SEQ ID NO: 2961
LPPGFVPTAPVVIRRC                 SEQ ID NO: 2962
PPGFVPTAPVVIRRCG                 SEQ ID NO: 2963
PGFVPTAPVVIRRCGK                 SEQ ID NO: 2964
GFVPTAPVVIRRCGKG                 SEQ ID NO: 2965
FVPTAPVVIRRCGKGF                 SEQ ID NO: 2966
VPTAPVVIRRCGKGFL                 SEQ ID NO: 2967
PTAP                  VVIRRCGKGFLG SEQ ID NO: 2968
VFQDVNHLPPGFVPTAP                SEQ ID NO: 2969
FQDVNHLPPGFVPTAPV                SEQ ID NO: 2970
QDVNHLPPGFVPTAPVV                SEQ ID NO: 2971
DVNHLPPGFVPTAPVVI                SEQ ID NO: 2972
VNHLPPGFVPTAPVVIR                SEQ ID NO: 2973
NHLPPGFVPTAPVVIRR                SEQ ID NO: 2974
HLPPGFVPTAPVVIRRC                SEQ ID NO: 2975
LPPGFVPTAPVVIRRCG                SEQ ID NO: 2976
PPGFVPTAPVVIRRCGK                SEQ ID NO: 2977
PGFVPTAPVVIRRCGKG                SEQ ID NO: 2978
GFVPTAPVVIRRCGKGF                SEQ ID NO: 2979
FVPTAPVVIRRCGKGFL                SEQ ID NO: 2980
VPTAPVVIRRCGKGFLG                SEQ ID NO: 2981
PTAP                  VVTRRCGKGFLGV SEQ ID NO: 2982
GVFQDVNHLPPGFVPTAP               SEQ ID NO: 2983
VFQDVNHLPPGFVPTAPV               SEQ ID NO: 2984
FQDVNHLPPGFVPTAPVV               SEQ ID NO: 2985
QDVNHLPPGFVPTAPVVI               SEQ ID NO: 2986
DVNHLPPGFVPTAPVVIR               SEQ ID NO: 2987
VNHLPPGFVPTAPVVIRR               SEQ ID NO: 2988
NHLPPGFVPTAPVVIRRC               SEQ ID NO: 2989
HLPPGFVPTAPVVIRRCG               SEQ ID NO: 2990
LPPGFVPTAPVVIRRCGK               SEQ ID NO: 2991
PPGFVPTAPVVIRRCGKG               SEQ ID NO: 2992
PGFVPTAPVVIRRCGKGF               SEQ ID NO: 2993
GFVPTAPVVIRRCGKGFL               SEQ ID NO: 2994
FVPTAPVVIRRCGKGFLG               SEQ ID NO: 2995
VPTAPVVIRRCGKGFLGV               SEQ ID NO: 2996
PTAP                  VVIRRCGKGFLGVT SEQ ID NO: 2997
IGVFQDVNHLPPGFVPTAP              SEQ ID NO: 2998
GVFQDVNHLPPGFVPTAPV              SEQ ID NO: 2999
VFQDVNHLPPGFVPTAPVV              SEQ ID NO: 3000
FQDVNHLPPGFVPTAPVVI              SEQ ID NO: 3001
QDVNHLPPGFVPTAPVVIR              SEQ ID NO: 3002
DVNHLPPGFVPTAPVVIRR              SEQ ID NO: 3003
VNHLPPGFVPTAPVVIRRC              SEQ ID NO: 3004
NHLPPGFVPTAPVVIRRCG              SEQ ID NO: 3005
HLPPGFVPTAPVVIRRCGK              SEQ ID NO: 3006
LPPGFVPTAPVVLRRCGKG              SEQ ID NO: 3007
PPGFVPTAPVVIRRCGKGF              SEQ ID NO: 3008
PGFVPTAPVVIRRCGKGFL              SEQ ID NO: 3009
GFVPTAPVVIRRCGKGFLG              SEQ ID NO: 3010
FVPTAPVVIRRCGKGFLGV              SEQ ID NO: 3011
VPTAPVVIRRCGKGFLGVT              SEQ ID NO: 3012
PTAP                  VVIRRCGKGFLGVTK SEQ ID NO: 3013
LIGVFQDVNHLPPGFVPTAP             SEQ ID NO: 3014
IGVFQDVNHLPPGFVPTAPV             SEQ ID NO: 3015
GVFQDVNHLPPGFVPTAPVV             SEQ ID NO: 3016
VFQDVNHLPPGFVPTAPVVI             SEQ ID NO: 3017
FQDVNHLPPGFVPTAPVVIR             SEQ ID NO: 3018
QDVNHLPPGFVPTAPVVIRR             SEQ ID NO: 3019
DVNHLPPGFVPTAPVVIRRC             SEQ ID NO: 3020
VNHLPPGFVPTAPVVIRRCG             SEQ ID NO: 3021
NHLPPGFVPTAPVVIRRCGK             SEQ ID NO: 3022
HLPPGFVPTAPVVIRRCGKG             SEQ ID NO: 3023
LPPGFVPTAPVVIRRCGKGF             SEQ ID NO: 3024
PPGFVPTAPVVIRRCGKGFL             SEQ ID NO: 3025
PGFVPTAPVVIRRCGKGFLG             SEQ ID NO: 3026
GFVPTAPVVLRRCGKGFLGV             SEQ ID NO: 3027
FVPTAPVVIRRCGKGFLGVT             SEQ ID NO: 3028
VPTAPVVIRRCGKGFLGVTK             SEQ ID NO: 3029
PTAP                  VVTRRCGKGFLGVTKA SEQ ID NO: 3030

[0169]

TABLE 23
P(T/S)AP Motif Containing Peptides from Human Herp-
esvirus 5
UL32
(GenBank Accession No. AAG31644)
SPWAPPTAP                        SEQ ID NO: 3031
PWAPTAPL                         SEQ ID NO: 3032
WAPTAPLP                         SEQ ID NO: 3033
APTAPLPG                         SEQ ID NO: 3034
PTAP                  LPGD       SEQ ID NO: 3035
NSPWAPTAP                        SEQ ID NO: 3036
SPWAPTAPL                        SEQ ID NO: 3037
PWAPTAPLP                        SEQ ID NO: 3038
WAPTAPLPG                        SEQ ID NO: 3039
APTAPLPGD                        SEQ ID NO: 3040
PTAP                  LPGDM      SEQ ID NO: 3041
GNSPWAPTAP                       SEQ ID NO: 3042
NSPWAPTAPL                       SEQ ID NO: 3043
SPWAPTAPLP                       SEQ ID NO: 3044
PWAPTAPLPG                       SEQ ID NO: 3045
WAPTAPLPGD                       SEQ ID NO: 3046
APTAPLPGDM                       SEQ ID NO: 3047
PTAP                  LPGDMN     SEQ ID NO: 3048
NGNSPWAPTAP                      SEQ ID NO: 3049
GNSPWAPTAPL                      SEQ ID NO: 3050
NSPWAPTAPLP                      SEQ ID NO: 3051
SPWAPTAPLPG                      SEQ ID NO: 3052
PWAPTAPLPGD                      SEQ ID NO: 3053
WAPTAPLPGDM                      SEQ ID NO: 3054
APTAPLPGDMN                      SEQ ID NO: 3055
PTAP                  LPGDMNP    SEQ ID NO: 3056
VNGNSPWAPTAP                     SEQ ID NO: 3057
NGNSPWAPTAPL                     SEQ ID NO: 3058
GNSPWAPTAPLP                     SEQ ID NO: 3059
NSPWAPTAPLPG                     SEQ ID NO: 3060
SPWAPTAPLPGD                     SEQ ID NO: 3061
PWAPTAPLPGDM                     SEQ ID NO: 3062
WAPTAPLPGDMN                     SEQ ID NO: 3063
APTAPLPGDMNP                     SEQ ID NO: 3064
PTAP                  LPGDMNPA   SEQ ID NO: 3065
PVNGNSPWAPTAP                    SEQ ID NO: 3066
VNGNSPWAPTAPL                    SEQ ID NO: 3067
NGNSPWAPTAPLP                    SEQ ID NO: 3068
GNSPWAPTAPLPG                    SEQ ID NO: 3069
NSPWAPTAPLPGD                    SEQ ID NO: 3070
SPWAPTAPLPGDM                    SEQ ID NO: 3071
PWAPTAPLPGDMN                    SEQ ID NO: 3072
WAPTAPLPGDMNP                    SEQ ID NO: 3073
APTAPLPGDMNPA                    SEQ ID NO: 3074
PTAP                  LPGDMNPAN  SEQ ID NO: 3075
TPVNGNSPWAPTAP                   SEQ ID NO: 3076
PVNGNSPWAPTAPL                   SEQ ID NO: 3077
VNGNSPWAPTAPLP                   SEQ ID NO: 3078
NGNSPWAPTAPLPG                   SEQ ID NO: 3079
GNSPWAPTAPLPGD                   SEQ ID NO: 3080
NSPWAPTAPLPGDM                   SEQ ID NO: 3081
SPWAPTAPLPGDMN                   SEQ ID NO: 3082
PWAPTAPLPGDMNP                   SEQ ID NO: 3083
WAPTAPLPGDMNPA                   SEQ ID NO: 3084
APTAPLPGDMNPAN                   SEQ ID NO: 3085
PTAP                  LPGDMNPANW SEQ ID NO: 3086
QTPVNGNSPWAPTAP                  SEQ ID NO: 3087
TPVNGNSPWAPTAPL                  SEQ ID NO: 3088
PVNGNSPWAPTAPLP                  SEQ ID NO: 3089
VNGNSPWAPTAPLPG                  SEQ ID NO: 3090
NGNSPWAPTAPLPGD                  SEQ ID NO: 3091
GNSPWAPTAPLPGDM                  SEQ ID NO: 3092
NSPWAPTAPLPGDMN                  SEQ ID NO: 3093
SPWAPTAPLPGDMNP                  SEQ ID NO: 3094
PWAPTAPLPGDMNPA                  SEQ ID NO: 3095
WAPTAPLPGDMNPAN                  SEQ ID NO: 3096
APTAPLPGDMNPANW                  SEQ ID NO: 3097
PTAP                  LPGDMNPANWP SEQ ID NO: 3098
TQTPVNGNSPWAPTAP                 SEQ ID NO: 3099
QTPVNGNSPWAPTAPL                 SEQ ID NO: 3100
TPVNGNSPWAPTAPLP                 SEQ ID NO: 3101
PVNGNSPWAPTAPLPG                 SEQ ID NO: 3102
VNGNSPWAPTAPLPGD                 SEQ ID NO: 3103
NGNSPWAPTAPLPGDM                 SEQ ID NO: 3104
GNSPWAPTAPLPGDMN                 SEQ ID NO: 3105
NSPWAPTAPLPGDMNP                 SEQ ID NO: 3106
SPWAPTAPLPGDMNPA                 SEQ ID NO: 3107
PWAPTAPLPGDMNPAN                 SEQ ID NO: 31O8
WAPTAPLPGDMNPANW                 SEQ ID NO: 3109
APTAPLPGDMNPANWP                 SEQ ID NO: 3110
PTAP                  LPGDMNPANWPR SEQ ID NO: 3111
GTQTPVNGNSPWAPTAP                SEQ ID NO: 3112
TQTPVNGNSPWAPTAPL                SEQ ID NO: 3113
QTPVNGNSPWAPTAPLP                SEQ ID NO: 3114
TPVNGNSPWAPTAPLPG                SEQ ID NO: 3115
PVNGNSPWAPTAPLPGD                SEQ ID NO: 3116
VNGNSPWAPTAPLPGDM                SEQ ID NO: 3117
NGNSPWAPTAPLPGDMN                SEQ ID NO: 3118
GNSPWAPTAPLPGDMNP                SEQ ID NO: 3119
NSPWAPTAPLPGDMNPA                SEQ ID NO: 3120
SPWAPTAPLPGDMNPAN                SEQ ID NO: 3121
PWAPTAPLPGDMNPANW                SEQ ID NO: 3122
WAPTAPLPGDMNPANWP                SEQ ID NO: 3123
APTAPLPGDMNPANWPR                SEQ ID NO: 3124
PTAP                  LPGDMNPANWPRE SEQ ID NO: 3125
AGTQTPVNGNSPWAPTAP               SEQ ID NO: 3126
GTQTPVNGNSPWAPTAPL               SEQ ID NO: 3127
TQTPVNGNSPWAPTAPLP               SEQ ID NO: 3128
QTPVNGNSPWAPTAPLPG               SEQ ID NO: 3129
TPVNGNSPWAPTAPLPGD               SEQ ID NO: 3130
PVNGNSPWAPTAPLPGDM               SEQ ID NO: 3131
VNGNSPWAPTAPLPGDMN               SEQ ID NO: 3132
NGNSPWAPTAPLPGDMNP               SEQ ID NO: 3133
GNSPWAPTAPLPGDMNPA               SEQ ID NO: 3134
NSPWAPTAPLPGDMNPAN               SEQ ID NO: 3135
SPWAPTAPLPGDMNPANW               SEQ ID NO: 3136
PWAPTAPLPGDMNPANWP               SEQ ID NO: 3137
WAPTAPLPGDMNPANWPR               SEQ ID NO: 3138
APTAPLPGDMNPANWPRE               SEQ ID NO: 3139
PTAP                  LPGDMNPANWPRER SEQ ID NO: 3140
FAGTQTPVNGNSPWAPTAP              SEQ ID NO: 3141
AGTQTPVNGNSPWAPTAPL              SEQ ID NO: 3142
GTQTPVNGNSPWAPTAPLP              SEQ ID NO: 3143
TQTPVNGNSPWAPTAPLPG              SEQ ID NO: 3144
QTPVNGNSPWAPTAPLPGD              SEQ ID NO: 3145
TPVNGNSPWAPTAPLPGDM              SEQ ID NO: 3146
PVNGNSPWAPTAPLPGDMN              SEQ ID NO: 3147
VNGNSPWAPTAPLPGDMNP              SEQ ID NO: 3148
NGNSPWAPTAPLPGDMNPA              SEQ ID NO: 3149
GNSPWAPTAPLPGDMNPAN              SEQ ID NO: 3150
NSPWAPTAPLPGDMNPANW              SEQ ID NO: 3151
SPWAPTAPLPGDMNPANWP              SEQ ID NO: 3152
PWAPTAPLPGDMNPANWPR              SEQ ID NO: 3153
WAPTAPLPGDMNPANWPRE              SEQ ID NO: 3154
APTAPLPGDMNPANWPRER              SEQ ID NO: 3155
PTAP                  LPGDMNPANWPRERA SEQ ID NO: 3156
TFAGTQTPVNGNSPWAPTAP             SEQ ID NO: 3157
FAGTQTPVNGNSPWAPTAPL             SEQ ID NO: 3158
AGTQTPVNGNSPWAPTAPLP             SEQ ID NO: 3159
GTQTPVNGNSPWAPTAPLPG             SEQ ID NO: 3160
TQTPVNGNSPWAPTAPLPGD             SEQ ID NO: 3161
QTPVNGNSPWAPTAPLPGDM             SEQ ID NO: 3162
TPVNGNSPWAPTAPLPGDMN             SEQ ID NO: 3163
PVNGNSPWAPTAPLPGDMNP             SEQ ID NO: 3164
VNGNSPWAPTAPLPGDMNPA             SEQ ID NO: 3165
NGNSPWAPTAPLPGDMNPAN             SEQ ID NO: 3166
GNSPWAPTAPLPGDMNPANW             SEQ ID NO: 3167
NSPWAPTAPLPGDMNPANWP             SEQ ID NO: 3168
SPWAPTAPLPGDMNPANWPR             SEQ ID NO: 3169
PWAPTAPLPGDMNPANWPRE             SEQ ID NO: 3170
WAPTAPLPGDMNPANWPRER             SEQ ID NO: 3171
APTAPLPGDMNPANWPRERA             SEQ ID NO: 3172
PTAP                  LPGDMNPANWPRERAW SEQ ID NO: 3173

[0170]

TABLE 24
P(T/S)AP Motif Containing Peptides from Human Pare-
chovirus 2
Polyprotein
(GenBank Accession No. NP_046804)
LTQHPSAP                         SEQ ID NO: 3174
TQHPSAPT                         SEQ ID NO: 3175
QHPSAPTL                         SEQ ID NO: 3176
HPSAPTLP                         SEQ ID NO: 3177
PSAP                  TLPF       SEQ ID NO: 3178
NLTQHPSAP                        SEQ ID NO: 3179
LTQHPSAPT                        SEQ ID NO: 3180
TQHPSAPTL                        SEQ ID NO: 3181
QHPSAPTLP                        SEQ ID NO: 3182
HPSAPTLPF                        SEQ ID NO: 3183
PSAP                  TLPFT      SEQ ID NO: 3184
TNLTQHPSAP                       SEQ ID NO: 3185
NLTQHPSAPT                       SEQ ID NO: 3186
LTQHPSAPTL                       SEQ ID NO: 3187
TQHPSAPTLP                       SEQ ID NO: 3188
QHPSAPTLPF                       SEQ ID NO: 3189
HPSAPTLPFT                       SEQ ID NO: 3190
PSAP                  TLPFTP     SEQ ID NO: 3191
TTNLTQHPSAP                      SEQ ID NO: 3192
TNLTQHPSAPT                      SEQ ID NO: 3193
NLTQHPSAPTL                      SEQ ID NO: 3194
LTQHPSAPTLP                      SEQ ID NO: 3195
TQHPSAPTLPF                      SEQ ID NO: 3196
QHPSAPTLPFT                      SEQ ID NO: 3197
HPSAPTLPFTP                      SEQ ID NO: 3198
PSAP                  TLPFTPD    SEQ ID NO: 3199
NTTNLTQHPSAP                     SEQ ID NO: 3200
TTNLTQHPSAPT                     SEQ ID NO: 3201
TNLTQHPSAPTL                     SEQ ID NO: 3202
NLTQHPSAPTLP                     SEQ ID NO: 3203
LTQHPSAPTLPF                     SEQ ID NO: 3204
TQHPSAPTLPFT                     SEQ ID NO: 3205
QHPSAPTLPFTP                     SEQ ID NO: 3206
HPSAPTLPFTPD                     SEQ ID NO: 3207
PSAP                  TLPFTPDF   SEQ ID NO: 3208
VNTTNLTQHPSAP                    SEQ ID NO: 3209
NTTNLTQHPSAPT                    SEQ ID NO: 3210
TTNLTQHPSAPTL                    SEQ ID NO: 3211
TNLTQHPSAPTLP                    SEQ ID NO: 3212
NLTQHPSAPTLPF                    SEQ ID NO: 3213
LTQHPSAPTLPFT                    SEQ ID NO: 3214
TQHPSAPTLPFTP                    SEQ ID NO: 3215
QHPSAPTLPFTPD                    SEQ ID NO: 3216
HPSAPTLPFTPDF                    SEQ ID NO: 3217
PSAP                  TLPFTPDFS  SEQ ID NO: 3218
TVNTTNLTQHPSAP                   SEQ ID NO: 3219
VNTTNLTQHPSAPT                   SEQ ID NO: 3220
NTTNLTQHPSAPTL                   SEQ ID NO: 3221
TTNLTQHPSAPTLP                   SEQ ID NO: 3222
TNLTQHPSAPTLPF                   SEQ ID NO: 3223
NLTQHPSAPTLPFT                   SEQ ID NO: 3224
LTQHPSAPTLPFTP                   SEQ ID NO: 3225
TQHPSAPTLPFTPD                   SEQ ID NO: 3226
QHPSAPTLPFTPDF                   SEQ ID NO: 3227
HPSAPTLPFTPDFS                   SEQ ID NO: 3228
PSAP                  TLPFTPDFSN SEQ ID NO: 3229
TTVNTTNLTQHPSAP                  SEQ ID NO: 3230
TVNTTNLTQHPSAPT                  SEQ ID NO: 3231
VNTTNLTQHPSAPTL                  SEQ ID NO: 3232
NTTNLTQHPSAPTLP                  SEQ ID NO: 3233
TTNLTQHPSAPTLPF                  SEQ ID NO: 3234
TNLTQHPSAPTLPFT                  SEQ ID NO: 3235
NLTQHPSAPTLPFTP                  SEQ ID NO: 3236
LTQHPSAPTLPFTPD                  SEQ ID NO: 3237
TQHPSAPTLPFTPDF                  SEQ ID NO: 3238
QHPSAPTLPFTPDFS                  SEQ ID NO: 3239
HPSAPTLPFTPDFSN                  SEQ ID NO: 3240
PSAP                  TLPFTPDFSNV SEQ ID NO: 3241
TTTVNTTNLTQHPSAP                 SEQ ID NO: 3242
TTVNTTNLTQHPSAPT                 SEQ ID NO: 3243
TVNTTNLTQHPSAPTL                 SEQ ID NO: 3244
VNTTNLTQHPSAPTLP                 SEQ ID NO: 3245
NTTNLTQHPSAPTLPF                 SEQ ID NO: 3246
TTNLTQHPSAPTLPFT                 SEQ ID NO: 3247
TNLTQHPSAPTLPFTP                 SEQ ID NO: 3248
NLTQHPSAPTLPFTPD                 SEQ ID NO: 3249
LTQHPSAPTLPFTPDF                 SEQ ID NO: 3250
TQHPSAPTLPFTPDFS                 SEQ ID NO: 3251
QHPSAPTLPFTPDFSN                 SEQ ID NO: 3252
HPSAPTLPFTPDFSNV                 SEQ ID NO: 3253
PSAP                  TLPFTPDFSNVD SEQ ID NO: 3254
ATTTVNTTNLTQHPSAP                SEQ ID NO: 3255
TTTVNTTNLTQHPSAPT                SEQ ID NO: 3256
TTVNTTNLTQHPSAPTL                SEQ ID NO: 3257
TVNTTNLTQHPSAPTLP                SEQ ID NO: 3258
VNTTNLTQHPSAPTLPF                SEQ ID NO: 3259
NTTNLTQHPSAPTLPFT                SEQ ID NO: 3260
TTNLTQHPSAPTLPFTP                SEQ ID NO: 3261
TNLTQHPSAPTLPFTPD                SEQ ID NO: 3262
NLTQHPSAPTLPFTPDF                SEQ ID NO: 3263
LTQHPSAPTLPFTPDFS                SEQ ID NO: 3264
TQHPSAPTLPFTPDFSN                SEQ ID NO: 3265
QHPSAPTLPFTPDFSNV                SEQ ID NO: 3266
HPSAPTLPFTPDFSNVD                SEQ ID NO: 3267
PSAP                  TLPFTPDFSNVDT SEQ ID NO: 3268
QATTTVNTTNLTQHPSAP               SEQ ID NO: 3269
ATTTVNTTNLTQHPSAPT               SEQ ID NO: 3270
TTTVNTTNLTQHPSAPTL               SEQ ID NO: 3271
TTVNTTNLTQHPSAPTLP               SEQ ID NO: 3272
TVNTTNLTQHPSAPTLPF               SEQ ID NO: 3273
VNTTNLTQHPSAPTLPFT               SEQ ID NO: 3274
NTTNLTQHPSAPTLPFTP               SEQ ID NO: 3275
TTNLTQHPSAPTLPFTPD               SEQ ID NO: 3276
TNLTQHPSAPTLPFTPDF               SEQ ID NO: 3277
NLTQHPSAPTLPFTPDFS               SEQ ID NO: 3278
LTQHPSAPTLPFTPDPSN               SEQ ID NO: 3279
TQHPSAPTLPFTPDFSNV               SEQ ID NO: 3280
QHPSAPTLPFTPDFSNVD               SEQ ID NO: 3281
HPSAPTLPFTPDFSNVDT               SEQ ID NO: 3282
PSAP                  TLPFTPDFSNVDTF SEQ ID NO: 3283
VQATTTVNTTNLTQHPSAP              SEQ ID NO: 3284
QATTTVNTTNLTQHPSAPT              SEQ ID NO: 3285
ATTTVNTTNLTQHPSAPTL              SEQ ID NO: 3286
TTTVNTTNLTQHPSAPTLP              SEQ ID NO: 3287
TTVNTTNLTQHPSAPTLPF              SEQ ID NO: 3288
TVNTTNLTQHPSAPTLPFT              SEQ ID NO: 3289
VNTTNLTQHPSAPTLPFTP              SEQ ID NO: 3290
NTTNLTQHPSAPTLPFTPD              SEQ ID NO: 3291
TTNLTQHPSAPTLPFTPDF              SEQ ID NO: 3292
TNLTQHPSAPTLPFTPDFS              SEQ ID NO: 3293
NLTQHPSAPTLPFTPDFSN              SEQ ID NO: 3294
LTQHPSAPTLPFTPDFSNV              SEQ ID NO: 3295
TQHPSAPTLPFTPDFSNVD              SEQ ID NO: 3296
QHPSAPTLPFTPDFSNVDT              SEQ ID NO: 3297
HPSAPTLPFTPDFSNVDTF              SEQ ID NO: 3298
PSAP                  TLPFTPDFSNVDTFH SEQ ID NO: 3299
VVQATTTVNTTNLTQHPSAP             SEQ ID NO: 3300
VQATTTVNTTNLTQHPSAPT             SEQ ID NO: 3301
QATTTVNTTNLTQHPSAPTL             SEQ ID NO: 3302
ATTTVNTTNLTQHPSAPTLP             SEQ ID NO: 3303
TTTVNTTNLTQHPSAPTLPF             SEQ ID NO: 3304
TTVNTTNLTQHPSAPTLPFT             SEQ ID NO: 3305
TVNTTNLTQHPSAPTLPFTP             SEQ ID NO: 3306
VNTTNLTQHPSAPTLPFTPD             SEQ ID NO: 3307
NTTNLTQHPSAPTLPFTPDF             SEQ ID NO: 3308
TTNLTQHPSAPTLPFTPDFS             SEQ ID NO: 3309
TNLTQHPSAPTLPFTPDFSN             SEQ ID NO: 3310
NLTQHPSAPTLPFTPDFSNV             SEQ ID NO: 3311
LTQHPSAPTLPFTPDFSNVD             SEQ ID NO: 3312
TQHPSAPTLPFTPDFSNVDT             SEQ ID NO: 3313
QHPSAPTLPFTPDFSNVDTF             SEQ ID NO: 3314
HPSAPTLPFTPDFSNVDTFH             SEQ ID NO: 3315
PSAP                  TLPFTPDFSNVDTFHS SEQ ID NO: 3316

[0171]

TABLE 25
P(T/S)AP Motif Containing Peptides from Semliki Forest Virus
Polyprotein
(GenBank Accession No. CAA76683)
LKIRPSAP                         SEQ ID NO: 3317
KIRPSAPY                         SEQ ID NO: 3318
IRPSAPYK                         SEQ ID NO: 3319
RPSAPYKT                         SEQ ID NO: 3320
PSAP                  YKTT       SEQ ID NO: 3321
GLKIRPSAP                        SEQ ID NO: 3322
LKIRPSAPY                        SEQ ID NO: 3323
KIRPSAPYK                        SEQ ID NO: 3324
IRPSAPYKT                        SEQ ID NO: 3325
RPSAPYKTT                        SEQ ID NO: 3326
PSAP                  YKTTV      SEQ ID NO: 3327
EGLKIRPSAP                       SEQ ID NO: 3328
GLKIRPSAPY                       SEQ ID NO: 3329
LKIRPSAPYK                       SEQ ID NO: 3330
KIRPSAPYKT                       SEQ ID NO: 3331
IRPSAPYKTT                       SEQ ID NO: 3332
RPSAPYKTTV                       SEQ ID NO: 3333
PSAP                  YKTTVV     SEQ ID NO: 3334
YEGLKIRPSAP                      SEQ ID NO: 3335
EGLKIRPSAPY                      SEQ ID NO: 3336
GLKIRPSAPYK                      SEQ ID NO: 3337
LKIRPSAPYKT                      SEQ ID NO: 3338
KIRPSAPYKTT                      SEQ ID NO: 3339
IRPSAPYKTTV                      SEQ ID NO: 3340
RPSAPYKTTVV                      SEQ ID NO: 3341
PSAP                  YKTTVVG    SEQ ID NO: 3342
AYEGLKIRPSAP                     SEQ ID NO: 3343
YEGLKIRPSAPY                     SEQ ID NO: 3344
EGLKIRPSAPYK                     SEQ ID NO: 3345
GLKIRPSAPYKT                     SEQ ID NO: 3346
LKIRPSAPYKTT                     SEQ ID NO: 3347
KIRPSAPYKTTV                     SEQ ID NO: 3348
IRPSAPYKTTVV                     SEQ ID NO: 3349
RPSAPYKTTVVG                     SEQ ID NO: 3350
PSAP                  YKTTVVGV   SEQ ID NO: 3351
FAYEGLKIRPSAP                    SEQ ID NO: 3352
AYEGLKIRPSAPY                    SEQ ID NO: 3353
YEGLKIRPSAPYK                    SEQ ID NO: 3354
EGLKIRPSAPYKT                    SEQ ID NO: 3355
GLKIRPSAPYKTT                    SEQ ID NO: 3356
LKIRPSAPYKTTV                    SEQ ID NO: 3357
KIRPSAPYKTTVV                    SEQ ID NO: 3358
IRPSAPYKTTVVG                    SEQ ID NO: 3359
RPSAPYKTTVVGV                    SEQ ID NO: 3360
PSAP                  YKTTVVGVF  SEQ ID NO: 3361
EFAYEGLKIRPSAP                   SEQ ID NO: 3362
FAYEGLK1RPSAPY                   SEQ ID NO: 3363
AYEGLKIRPSAPYK                   SEQ ID NO: 3364
YEGLKIRPSAPYKT                   SEQ ID NO: 3365
EGLKIRPSAPYKTT                   SEQ ID NO: 3366
GLKIRPSAPYKTTV                   SEQ ID NO: 3367
LKIRPSAPYKTTVV                   SEQ ID NO: 3368
KIRPSAPYKTTVVG                   SEQ ID NO: 3369
IRPSAPYKTTVVGV                   SEQ ID NO: 3370
RPSAPYKTTVVGVF                   SEQ ID NO: 3371
PSAP                  YKTTVVGVFG SEQ ID NO: 3372
HEFAYEGLKIRPSAP                  SEQ ID NO: 3373
EFAYEGLKIRPSAPY                  SEQ ID NO: 3374
FAYEGLKIRPSAPYK                  SEQ ID NO: 3375
AYEGLKIRPSAPYKT                  SEQ ID NO: 3376
YEGLKIRPSAPYKTT                  SEQ ID NO: 3377
EGLKIRPSAPYKTTV                  SEQ ID NO: 3378
GLKIRPSAPYKTTVV                  SEQ ID NO: 3379
LKIRPSAPYKTTVVG                  SEQ ID NO: 3380
KIRPSAPYKTTVVGV                  SEQ ID NO: 3381
IRPSAPYKTTVVGVF                  SEQ ID NO: 3382
RPSAPYKTTVVGVFG                  SEQ ID NO: 3383
PSAP                  YKTTVVGVFGV SEQ ID NO: 3384
FHEFAYEGLKIRPSAP                 SEQ ID NO: 3385
HEFAYEGLKIRPSAPY                 SEQ ID NO: 3386
EFAYEGLKIRPSAPYK                 SEQ ID NO: 3387
FAYEGLKIRPSAPYKT                 SEQ ID NO: 3388
AYEGLKIRPSAPYKTT                 SEQ ID NO: 3389
YEGLKIRPSAPYKTTV                 SEQ ID NO: 3390
EGLKIRPSAPYKTTVV                 SEQ ID NO: 3391
GLKIRPSAPYKTTVVG                 SEQ ID NO: 3392
LKIRPSAPYKTTVVGV                 SEQ ID NO: 3393
KIRPSAPYKTTVVGVF                 SEQ ID NO: 3394
IRPSAPYKTTVVGVFG                 SEQ ID NO: 3395
RPSAPYKTTVVGVFGV                 SEQ ID NO: 3396
PSAP                  YKTTVVGVFGVP SEQ ID NO: 3397
PFHEFAYEGLKIRPSAP                SEQ ID NO: 3398
FHEFAYEGLKIRPSAPY                SEQ ID NO: 3399
HEFAYEGLKLRPSAPYK                SEQ ID NO: 3400
EFAYEGLKIRPSAPYKT                SEQ ID NO: 3401
FAYEGLKIRPSAPYKTT                SEQ ID NO: 3402
AYEGLKIRPSAPYKTTV                SEQ ID NO: 3403
YEGLKIRPSAPYKTTVV                SEQ ID NO: 3404
EGLKIRPSAPYKTTVVG                SEQ ID NO: 3405
GLKIRPSAPYKTTVVGV                SEQ ID NO: 3406
LKIRPSAPYKTTVVGVF                SEQ ID NO: 3407
KIRPSAPYKTTVVGVEG                SEQ ID NO: 3408
IRPSAPYKTTVVGVFGV                SEQ ID NO: 3409
RPSAPYKTTVVGVFGVP                SEQ ID NO: 3410
PSAP                  YKTTVVGVFGVPG SEQ ID NO: 3411
PPFHEFAYEGLKIRPSAP               SEQ ID NO: 3412
PFHEFAYEGLKIRPSAPY               SEQ ID NO: 3413
FHEFAYEGLKIRPSAPYK               SEQ ID NO: 3414
UEFAYEGLKIRPSAPYKT               SEQ ID NO: 3415
EFAYEGLKIRPSAPYKTT               SEQ ID NO: 3416
FAYEGLKTRPSAPYKTTV               SEQ ID NO: 3417
AYEGLKIRPSAPYKTTVV               SEQ ID NO: 3418
YEGLKIRPSAPYKTTVVG               SEQ ID NO: 3419
EGLKIRPSAPYKTTVVGV               SEQ ID NO: 3420
GLKIRPSAPYKTTVVGVF               SEQ ID NO: 3421
LKIRPSAPYKTTVVGVFG               SEQ ID NO: 3422
KIRPSAPYKTTVVGVFGV               SEQ ID NO: 3423
IRPSAPYKTTVVGVFGVP               SEQ ID NO: 3424
RPSAPYKTTVVGVFGVPG               SEQ ID NO: 3425
PSAP                  YKTTVVGVFGVPGS SEQ ID NO: 3426
NPPFHEFAYEGLKIRPSAP              SEQ ID NO: 3427
PPFHEFAYEGLKIRPSAPY              SEQ ID NO: 3428
PFHEFAYEGLKIRPSAPYK              SEQ ID NO: 3429
FHEFAYEGLKIRPSAPYKT              SEQ ID NO: 3430
HEFAYEGLKIRPSAPYKTT              SEQ ID NO: 3431
EFAYEGLKIRPSAPYKTTV              SEQ ID NO: 3432
FAYEGLKIRPSAPYKTTVV              SEQ ID NO: 3433
AYEGLKIRPSAPYKTTVVG              SEQ ID NO: 3434
YEGLKIRPSAPYKTTVVGV              SEQ ID NO: 3435
EGLKIRPSAPYKTTVVGVF              SEQ ID NO: 3436
GLKIRPSAPYKTTVVGVFG              SEQ ID NO: 3437
LKIRPSAPYKTTVVGVFGV              SEQ ID NO: 3438
KIRPSAPYKTTVVGVFGVP              SEQ ID NO: 3439
IRPSAPYKTTVVGVFGVPG              SEQ ID NO: 3440
RPSAPYKTTVVGVFGVPGS              SEQ ID NO: 3441
PSAP                  YKTTVVGVFGVPGSG SEQ ID NO: 3442
TNPPFHEFAYEGLKIRPSAP             SEQ ID NO: 3443
NPPFHEFAYEGLKIRPSAPY             SEQ ID NO: 3444
PPFHEFAYEGLKIRPSAPYK             SEQ ID NO: 3445
PFHEFAYEGLKIRPSAPYKT             SEQ ID NO: 3446
FHEFAYEGLKIRPSAPYKTT             SEQ ID NO: 3447
HEFAYEGLKIRPSAPYKTTV             SEQ ID NO: 3448
EFAYEGLKIRPSAPYKTTVV             SEQ ID NO: 3449
FAYEGLKIRPSAPYKTTVVG             SEQ ID NO: 3450
AYEGLKIRPSAPYKTTVVGV             SEQ ID NO: 3451
YEGLKIRPSAPYKTTVVGVF             SEQ ID NO: 3452
EGLKIRPSAPYKTTVVGVFG             SEQ ID NO: 3453
GLKIRPSAPYKTTVVGVFGV             SEQ ID NO: 3454
LKIRPSAPYKTTVVGVFGVP             SEQ ID NO: 3455
KIRPSAPYKTTVVGVFGVPG             SEQ ID NO: 3456
IRPSAPYKTTVVGVFGVPGS             SEQ ID NO: 3457
RPSAPYKTTVVGVFGVPGSG             SEQ ID NO: 3458
PSAP                  YKTTVVGVFGVPGSGK SEQ ID NO: 3459
(Ebola Virus Matrix Protein (AAL25816)):
MRRVILPTAPPEYMEAIYPVRSNSTIARGGNSNTGFLTPESVNGDTPSNPLRPIADDTID SEQ ID NO:3460
HASHIPGSVSSAFILEAMVNVISGPKVLMKQIPIWLPLGVADQKTYSFDSTTAAIMLASY
TITHFGKATNPLVRVNRLGPGIPDHPLRLLRTGNQAFLQEFVLPPVQLPQYFTFDLTALK
LITQPLPAATWTDDTPTGSNGALRPGTSFHPKLRPILLPNKSGKKGNSADLTSPEKTQAT
MTSLQDFKTVPIDPTKNIMGIEVPETLVHKLTGKKVTSKNGQPIIPVLLPKYIGLDPVAP
GDLTMVITQDCDTCHSPASLPAVIEK
(Hepatitis B Virus PreSl/PreS2/S Envelope
Protein (BAA85340))
MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFKANSDNPDWDLNPHKDNWPDSNKVGV SEQ ID NO:3461
GAFGPGFTPPHGGLLGWSPQAQGILTTVPTAPPPASTNRQLGRKPTPLSPPLRDTHPQAM
QWNSTTFHQTLQDPRVRALYFPAGGSSSGTVNPVQNTASSISSILSTTGDPVPNMENIAS
GLLGPLLVLQAGFFSLTKILTIPQSLDSWWTSLNFLGGTPVCLGQNSQSQISSHSPTCCP
PICPGYRWMCLRRFIIFLCILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCKTCTT
PAQGTSMFPSCCCIKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGL
SPTVWLSVIWMMWFWGPSLYNILSPFMPLLPIFFCLWAYI
(Human Herpesvirus 1 RL2 Protein (NP_044601))
MEPRPGASTRRPEGRPQREPAPDVWVFPCDRDLPDSSDSEAETEVGGRGDADHHDDDSAS SEQ ID NO:3462
EADSTDTELFETGLLGPQGVDGGAVSGGSPPREEDPGSCGGAPPREDGGSDEGDVCAVCT
DEIAPHLRCDTFPCMHRFCIPCMKTWMQLRNTCPLCNAKLVYLIVGVTPSGSFSTIPIVN
DPQTRMEAEEAVRAGTAVDFIWTGNQRFAPRYLTLGGHTVPALSPTHPEPTTDEDDDDLD
DADYVPPAPRRTPRAPPRRGAAAPPVTGGASHAAPQPAAARTAPPSAPIGPHGSSNTNTT
TNSSGGGGSRQSRAAAPRGASGPSGGVGVGVGVVEAEAGRPRGRTGPLVNRPAPLANNRD
PIVISDSPPASPHRPPAAPMPGSAPRPGPPASAAASGPARRRAAVAPCVRAPPPGPGPPA
PAPGAEPAARPADARRVPQSHSSLAQAANQEQSLCBARATVARGSGGPGVEGGHGPSRGA
APSGAAPLPSAASVEQEAAVRPRKRRGSGQENPSPQSTRPPLAPAGAKRAATHPPSDSGP
GGRGQGGPGTPLTSSAASASSSSASSSSAPTPAGAASSAAGAASSSASASSGGAVGALGG
RQEETSLGPRAASGPRGPRKCARKTRHAETSGAVPAGGLTRYLPISGVSSVVALSPYVNK
TITGDCLPILDMETGNIGAYVVLVDQTGNMATRLPAAVPGWSRRTLLPETAGNHVMPPEY
PTAP                  ASEWNSLWMTPVGNMLFDQGTLVGALDFRSLRSRHPWSGEQGASTRDEGKQ
(Human Herpesvirus 2 Virion Glycoprotein K
(NP_044524)
MLAVRSLQHLTTVIFITAYGLVLAWYIVFGASPLHRCIYAVRPAGAHNDTALVWMKINQT SEQ ID NO:3463
LLFLGPPTAPPGGAWTPHARVCYANIIEGRAVSLPAIPGAMSRRVMNVHEAVNCLEALWD
TQMRLVVVGWFLYLAFVALHQRRCMFGVVSPAHSMVAPATYLLNYAGRIVSSVFLQYPYT
KITRLLCELSVQRQTLVQLFEADPVTFLYHRPAIGVIVGCELLLRFVALGLIVGTALISR
GACAITHPLFLTITTWCFVSIIALTELYFILRRGSAPKNAEPAAPRGRSKGWSGVCGRCC
SIILSGIAVRLCYIAVVAGVVLVALRYEQEIQRRLFDL
(Human Herpesvirus 2 Strain 333 Glycoprotein
I (P06764))
MPGRSLQGLAILGLWVCATGLVVRGPTVSLVSDSLVDAGAVGPQGFVEEDLRVFGELHFV SEQ ID NO:3464
GAQVPHTNYYDGIIELFHYPLGNHCPRVVHVVTLTACPRRPAVAFTLCRSTHHAHSPAYP
TLELGLARQPLLRVRTATRDYAGLYVLRVWVGSATNASLFVLGVALSANGTFVYNGSDYG
SCDPAQLPFSAPRLGPSSVYTPGASRPTPPRTTTSPSSPRDPTPAPGDTGTPAPASGEPA
PPNSTRSASESRHRLTVAQVIQIAIPASIIAFVFLGSCTCFIHRCQRRYRRPRGQIYNPG
GVSCAVNEAAMARLGAELRSHPNTPPKPRRRSSSSTTMPSLTSIAEESEPGPVVLLSVSP
RPRSGPTAPQEV
(Human Herpesvirus 4 - Eptein Barr Virus
EBNA2 (NP_039845))
MPTFYLALHGGQTYHLIVDTDSLGNPSLSVIPSNPYQEQLSDTPLIPLTTFVGENTGVPP SEQ ID NO:3465
PLPPPPPPPPPPPPPPPPPPPPPPPPPPSPPPPPPPPPPPQRRDAWTQEPSPLDRDPLGY
DVGHGPLASAMRMLWMANYIVRQSRGDRGLILPQGPQTAPQARLVQPHVPPLRPTAPTIL
SPLSQPRLTPPQPLMMPPRPTPPTPLPPATLTVPPRPTRPTTLPPTPLLTVLQRPTELQP
TPSPPPRMLPVLHVPDQSMHPLTHQSTPNDPDSPEPRSPTVFYNIPPMPLPPSQLPPPAA
PAQPPPGVINDQQLHHLPSGPPWWPPICDPPQPSKTQGQSRGQSRGRGRGRGRGRGKGKS
RDKQRKPGGPWRPEPNTSSPSMPELSPVLGLHQGQGAGDSPTPGPSNAAPVCRNSHTATP
NVSPTHEPESHNSPEAPILFPDDWYPPSIDPADLDESWDYTFETTESPSSDEDYVEGPSK
RPRPSIQ
(Influenza A Virus (A/Pintail
Duck/Alberta/114/79 (H8N4) Hemagglutinin (AAG38554))
SKAGVTMEKLIVIAMLLASTNAYDRICIGYQSNNSTDTVNTLIEQNVPVTQTMELVETEK SEQ ID NO:3466
HPAYCNTDLGAPLELRDCKIEAVIYGNPKCDIHLKDQGWSYIVERPSAPEGMCYPGSIEN
LEELRFVFSSAASYKRIRLFDYSRWNVTRSGTSKACNASTGGQSFYRSINWLTKKKPDTY
DFNEGTYVNNEDGDIIFLWGIHHPPDTKEQTTLYKNANTLTSVTTNTINRNFQPNIGPRP
LVRGQQGRMDYYWGILKRGETLKIRTNGNLIAPEFGYLLKGESHGRIIQNEDIPIGNCNT
KCQTYAGAINSSKPFQNASRHYMGECPKYVKKASLRLAVGLRNTPSVEPRGLFGAIAGFI
EGGWSGMIDGWYGFHHSNSEGTGMAADQKSTQEAIDKITNKVNNIVDKMNRE
(Human Papilomavirus L1 Protein, My09/My11
Region (AAA67231))
AQGHNNGICWFNELFVTVVDTTRSTNITISAAATQANEYTASNFKEYLRHTEEYDLQVIL SEQ ID NO:3467
QLCKIHLTPEIMAYLHSMNEHLLDEWNFGVLPPPSTSLDDTYRYLQSRAITCQKGPSAPA
PKKDPYDGLVFWEVDLKDKLSTDLDQFPLGR
(Human Papilomavirus Type 23 Minor Capsid
Protein L2 (NP_043365)
MVRAQRTKRASVTDIYKGCKASGTCPPDVLNKVEQNTLADKILKYGSVGVFFGGLGIGTG SEQ ID NO:3468
KGTGGATGYVPLRPGVRVGGTPTVVRPAVIPEIIGPTELIPVDSIAPTDPEAPSIVSLTD
SGAAADLFPSEAETIAEVHPTPVDIGIDTPIVAGGRDAILEVVDTNPPTRFSVTRTQYDN
PSFQIISESTPITGEASLADHVFVFEGSGGQHVGAVTEEIELDTYPSRYSFEIEEATPPR
RTSTPIERISQEFRNLRRALYNRRLTEQVQVKNPLFLTTPSKLVRFQFDNPVFDEEVTQI
FERDVAEVEEPPDRDFLDIDRLGRPLLTESTEGRIRLSRLGQPASIQTRSGTRVGSRVHF
YTDLSTINTEEPIELELLGEHSGDASVIEEPLQSTVIDMNLDDVEAIQDTIDTADDYNSA
DLLLDNAIEEFNNSQLVFGTSDRSSSAYSIPRFESPRETTVYVQDIEGNQVIYPGPTERP
TIIFPLPSAPAVVIHTLDKSFDYYLHPSLRKKRRKRKYL
(Human Papilomavirus Type 35 Major Capsid
Protein L1 (P27232))
MSLWRSNEATVYLPPVSVSKVVSTDEYVTRTNIYYHAGSSRLLAVGHPYYAIKKQDSNKI SEQ ID NO:3469
AVPKVSGLQYRVFRVKLPDPNKFGFPDTSFYDPASQRLVWACTGVEVGRGQPLGVGISGH
PLLNKLDDTENSNKYVGNSGTDNRECISMDYKQTQLCLIGCRPPIGEHWGKGTPCNANQV
KAGECPPLELLNTVLQDGDMVDTGFGAMDFTTLQANKSDVPLDICSSICKYPDYLKMVSE
PYGDMLFFYLRREQMFVRHLFNRAGTVGETVPADLYIKGTTGTLPSTSYFPTPSGSMVTS
DAQIFNKPYWLQRAQGHNNGICWSNQLFVTVVDTTRSTNMSVCSAVSSSDSTYKNDNFKE
YLRHGEEYDLQFIFQLCKITLTADVMTYIHSMNPSILEDWNFGLTPPPSGTLEDTYRYVT
SQAVTCQKPSAPKPKDDPLKNYTFWEVDLKEKFSADLDQFPLGRKFLLQAGLKARPNFRL
GKRAAPASTSKKSSTKRRKVKS
(Human Papilomavirus Type 6b Minor Capsid
Protein L2 (NP_040303))
MAHSRARRRKPASATQLYQTCKLTGTCPPDVIPKVEHNTIADQILKWGSLGVFFGGLGIG SEQ ID NO:3470
TGSGTGGRTGYVPLQTSAKPSITSGPMARPPVVVEPVAPSDPSIVSLIEESAIINAGAPE
IVPPAHGGFTITSSETTTPAILDVSVTSHTTTSIFRNPVFTEPSVTQPQPPVEANGHILI
SAPTVTSHPIEEIPLDTFVVSSSDSGPTSSTPVPGTAPRPRVGLYSRALHQVQVTDPAFL
STPQRLITYDNPVYEGEDVSVQFSHDSIHNAPDEAFMDIIRLHRPAIASRRGLVRYSRIG
QRGSMHTRSGKHIGARIHYFYDISPIAQAAEEIEMHPLVAAQDDTFDIYAESFEPGINPT
QHPVTNISDTYLTSTPNTVTQPWGNTTVPLSLPNDLFLQSGPDITFPTAPMGTPFSPVTP
ALPTGPVFITGSGFYLHPAWYFARKRRKRIPLFFSDVAA
(Human Papilomavirus Type 9 Late Protein
(NP_041865))
MVRAKRTKRASVTDIYRGCKAAGTCPPDVINKVEHTTIADKILQYGSAGVFFGGLGISTG SEQ ID NO:3471
RGTGGATGYVPLGEGPGVRVGGTPTIVRPGVIPEIIGPTDLIPLDTVRPIDPTAPSIVTG
TDSTVDLLPGEIESIAEIHPVPVDNAVVDTPVVTEGRRGSSAILEVADPSPPMRTRVART
QYHNPAFQIISESTPMSGESSLADHIIVFEGSGGQLVGGPRESYTASSENIELQEFPSRY
SFEIDEGTPPRTSTPVQRAVQSLSSLRRALYNRRLTEQVAVTDPLFLSRPSRLVQFQFDN
PAFEDEVTQIFERDLSTVEEPPDRQFLDVQRLSRPLYTETPQGYVRVSRLGRRATIRTRS
GAQVGAQVHFYRDLSTTNTEEPIEMQLLGEHSGDSTIVQGPVESSIVDVNIDEPDGLEVG
RQETPSVEDVDFNSEDLLLDEGVEDFSGSQLVVGTRRSTNTLTVPRFETPRDTSFYIQDI
QGYTVSYPESRQTTDIIFPHPDTPTVVIHINDTSGDYYLHPSLQRKKRKRKYL
(Human T-cell Lymphotropic Virus Type 2 Gag
Protein (CAA61543))
MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPGPSDFDFQQLRRFLKLALKTPIWL SEQ ID NO:3472
NPIDYSLLASLVPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPE
AHVPPPYVEPTSTKCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSAPGSPQFMQTLRLA
VQQFDPTAKDLQDLLQYLCSSLVVSLHHQQLNTLITEAETRGVTGYNPMAGPLRMQANNP
AQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTP
KEPTLRSLAYSNANKECQKILQARGPTNSPLGEMLRACQAWTPKDKTKVLVVQPRRPPPT
QPCFRCGKTGHWSRDCTQPRPPPGPCPLCQDPSHWKRDCPQPKPPQEEGEPLLLDLSSTS
GTTEEKNSLRGEI
(West Nile Virus Polyprotein (NP_941724))
MSKKPGGPGKNRAVNMLKRGMPRGLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIA SEQ ID NO:3473
PTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSTKQKKRGGTAGFTILLGLIAC
AGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYLCEDTITYECPVLA
AGNDPEDIDCWCTKSSVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTKA
TRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAILLLLVAPAYSFNCLGNSNRD
FLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLADVRSYCYLASVSDLST
RAACPTMGEAHNEKPADPAFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACTTKATGWII
QKENIKYEVAIFVHGPTTVESHGKIGATQAGRFSITPSAPSYTLKLGEYGEVTVDCEPRS
GIDTSAYYVMSVGEKSFLVHREWFMDLNLPWSSAGSTTWRNRETLMEFEEPHATKQSVVA
LGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFART
PADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANSKVLIE
LEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLRGAQRLAALGDTAWDFGSVGGV
FTSVGKAIHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIAMTFLAVGGVLLF
LSVNVHADTGCAIDTGRQELRCGSGVFIHNDVEAWMDRYKFYPETPQGLAKIIQKAHAEG
VCGLRSVSRLEHQMWEAIKDELNTLLKENCVDLSVVVEKQNGMYKAAPKRLAATTEKLEM
GWKAWGKSIIFAPELANNTFVIDGPETEECPTANRAWNSMEVEDFGFGLTSTRMFLRIRE
TNTTECDSKIIGTAVKNNMAVHSDLSYWIESGLNDTWKLERAVLGEVKSCTWPETHTLWG
DGVLESDLITPITLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTISDSCEH
RGPAARTTTESGKLITDWCCRSCTLPPLRFQTENGCWYGMEIRPTRHDEKTLVQSRVNAY
NADMIDPFQLGLMVVFLATQEVLRKRWTAKISIPAIMLALLVLVFGGITYTDVLRYVILV
GAAFAEANSGGDVVHLALMATFKIQPVFLVASFLKARWTNQESILLMLAAAFFQMAYYDA
KNVLSWEVPDVLNSLSVAWMILRAISFTNTSNVVVPLLALLTPGLKCLNLDVYRILLLMV
GVGSLIKEKRSSAAKKKGACLICLALASTGVFNPMILAAGLMACDPNRKRGWPATEVMTA
VGLMFAIVGGLAELDIDSMATPMTIAGLMFAAFVISGKSTDMWIERTADITWESDAEITG
SSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVIGFWITLQYTK
RGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALM
SGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGHDEVQMIVVEPGKNVKNVQTKPGVFKTP
EGEIGAVTLDYPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMEEPAPAGF
EPEMLRKKQITVLDLHPGAGKTRKILPQIIKEAINKRLRTAVLAPTRVVAAEMSEALRGL
PIRYQTSAVHREHSGNEIVDVMCHATLTHRLMSPHRVPNYNLFIMDEAHFTDPASIAARG
YIATKVELGEAAAIFMTATPPGTSDPFPESNAPISDNQTEIPDRAWNTGYEWITEYVGKT
VWFVPSVKMGNEIALCLQPAGKKVIQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFK
ASRVIDSRKSVKPTIIEEGDGRVILGEPSAITAASAAQRRGRIGPNPSQVGDEYCYGGHT
NEDDSNFAHWTEARIMLDNINMPNGLVAQLYQPEREKVYTMDGEYRLRGEERKNFLEFLR
TADLPVWLAYKVAAAGISYHDRKWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWADA
RVYSDHQALKSFKDFASGKRSQIGLVEVLGRMPEHFMVKTWEALDTMYVVATAEKGGRAH
RMALEELPDALQTIVLIALLSVMSLGVFFLLMQRKGIGKIGLGGVILGAATFFCWMAEVP
GTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKN
DIGSLLGHRPEARETTLGVESFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLT
SINVQASALFTLARGFPFVDVGVSALLLAVGCWGQVTLTVTVTAAALLFCHYAYMVPGWQ
AEAMRSAQRRTAAGIMKNVVVDGIVATDVPELERTTPVMQKKVGQIILILVSMAAVVVNP
SVRTVREAGILTTAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSIMWTLIKNMEK
PGLKRGGAKGRTLGEVWKERLNHMTKEEFTRYRKEAITEVDRSAAKHARREGNITGGHPV
SRGTAKLRWLVERRFLEPVGKVVDLGCGRGGWCYYMATQKRVQEVKGYTKGGPGHEEPQL
VQSYGWNIVTNKSGVDVFYRPSEASDTLLCDIGESSSSAEVEEHRTVRVLEMVEDWLHRG
PKEFCIKVLCPYMPKVIEKMETLQRRYGGGLIRNPLSRNSTHEMYWVSHASGNIVHSVNM
TSQVLLGRMEKKTWKGPQFEEDVNLGSGTPAVGKPLLNSDTSKTKNRIERLKKEYSSTWH
QDANHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQR
VFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLARDKKPRMCSREEFIGKVNSNAALGANF
EEQNQWKNAREAVEDPKFWEMVDEEREAHLRGECNTCIYNMMGKREKKPGEFGKAKGSPA
IWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILKEVGTKPGGKVYAD
DTAGWDTRTTKADLENEAKVLELLDGEHRRLARSIIELTYRHKVVKVMRPAADGKTVMDV
ISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLGKGKGPKVRTWLFEN
GEERLSPMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCS
NHFTELIMKDGRTLVVPCRGQDELIGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRR
DLRLMANAICSAVPANWVPTGRTTWSIHAKGEWMTTEDMLAVWNRVWIEENEWMEDKTPV
ERWSDVPYSGKREDIWCGSLIGTRTRATWAENIHVAINQVRSVIGEEKYVDYMSSLRRYE
DTIVVEDTVIJ
(Measles Matrix Protein (CAA34587))
MHTPPPGAAEDSDPPGPPIGPAPGSPPPGAGRPTAKPEELPKEATEPDTVARRTAGPNEK SEQ ID NO:3474
PVLHNKTPPTLPTPRRKAPTTGSVPNANQVCNAANLTPLDTPQRLRAVYMSITRLSDNGY
YTVPRRMLEFRSVNAVALNLLATLRTDKAIGPGKTTDNAEQPPEATFLVHIGNPRRKKSE
VHSADHCKMKIEKMGPVSAPGGIGGTSLHIRSTGKTSKTLHAQLGLKKTPCYPPMDINED
LNRSLWRSRRKTARIQAAPQPSAPQEPRTHDDAITNDDQGPFKALQTAVTSNARKRPPSQ
RQPEGPDKKAPSEELHGPSERSASS
(Rubella Non-structural Protein (BAB32473))
MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQ SEQ ID NO:3475
MQVSDHPALHAISRYTRRHWIEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTAR
KLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHGGRAVADRCLLYYTPMQMCEL
MRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRH
VRSLQPSARVRLPDLVHLAAVGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNA
LSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNARLAGIMKSAKRCAADSLSVAG
WLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
AATWIVHAASADRHCACAPRCDAPRERPSAPAGPPDDEALIPPWLFAERRALRCREWDFE
ALRAPADTAAAPAPLAPRPARCPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLR
GPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARAWAKFFRGCAWAQRLLGEPAV
MHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDAHAVTAAVRAGPGQSAAT
SPPPGDPPPPRRARRSQRHLDARGTPPPAPARDPPPPAPSPPAPPPAGDPVLPTSAGPAD
RARHAELEVAYEPSDPPTPTKADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAA
NEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVATPGHGCGYTHIIHAVAPRRPR
DPAALEEGEALLERAYRSIVALAAARRWACVACPLLGAGVYGWSAAESLRAALAATPAEP
AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPA
TPLGDATAPEPRGCQGCELCRYTRVTNDPAYVNLWLERDRGATSWAMRIPEVVVYGPEHL
ATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQVRCTPSNAHAALCRTGVPPRV
STRGGELDPNTCWFPAAANVAQAAPACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SASHADASPDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHPAPNGPWGVVLE
VRARPEGGNPTGHFVCAVGGGPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLE
VRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTTRILAAFTREDLYVCPTNALL
HEIQAKLEARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
VGDRDQCGPHYANKCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFAC
NLWDGRQVDLHLAFSRETVRRLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALVR
DLATVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAELKEVPAGIDRVVAVEQAPPP
LPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRHT
YLRERIDLTDVYTQMGVAARELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAAL
GPRDTEDCHAAQGKAGLETRAWAKEWVQVMSPHFRATQKIIMRALRPQFLVAAGHTEPEV
DAWWQAHYTTNATEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSA
ALKWTPAEVGLFGFHIPVKHVSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLE
EQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVRELTAYARGRGLDHPATIGAL
EEIQTPYARANLHDAD
(Colorado Tick Fever Virus VP12 (AAB02025))
GAFVLALLISLQSVYFKLYEFYKNNETARNTSVAGFLKRHEVAVNVIVEFSFDTLFFLCG SEQ ID NO:3476
LLGFELSPTARRLIFRRTASAEKADTVELEHVSSRRRIWSRDDSTVBIWSKTSPLASQRS
RDHFDGDPREPAPPAYSPADFYPPPASPHICETPLSTRVAPSAPSASLFTAGGIGLP
(Human Foamy Virus Gag Protein (NP_044279))
MASGSNVEEYELDVEALVVILRDRNIPRNPLHGEVIGLRLTEGWWGQIERFQMVRLILQD SEQ ID NO:3478
DDNEPLQRPRYEVIQRAVNPHTMFMISGPLAELQLAFQDLDLPEGPLRFGPLANGHYVQG
DPYSSSYRPVTMAETAQMTRDELEDVLNTQSEIEIQMINLLELYEVETPALRRQLAERSS
TGQGGISPGAPRSRPPVSSFSGLPSLPSIPGIHPRAPSPPRATSTPGNIPWSLGDDSPPS
SSFPGPSQPRVSFHPGNPFVEEEGHRPRSQSRERRREILPAPVPSAPPMIQYIPVPPPPP
IGTVIPIQHIRSVTGEPPRNPREIPTWLGRNAPAIDGVFPVTTPDLRCRIINAILGGNIG
LSLTPGDCLTWDSAVATLFIRTHGTFPMHQLGNVIKGIVDQEGVATAYTLGMMLSGQNYQ
LVSGIIRGYLPGQAVVTALQQRLDQEIDDQTRAETFIQHLNAVYEILGLNARGQSIRASV
TPQPRPSRGRGRGQNTSRPSQGPANSGRGRQRPASGQSNRGSSTQNQNQDNLNQGGYNLR
PRTYQPQRYGGGRGRRWNDNTNNQESRPSDQGSQTPRPNQAGSGVRGNQSQTPRPAAGRG
GRGNHNRNQRSSGAGDSRAVNTVTQSATSSTDESSSAVTAASGGDQRD
(Hepatitis E Virus ORF3 (AAC35758))
MNNMSFAAPMGSRPCALGLFCCCSSCFCLCCPRHRPVSRLAAVVGGAAAVPAVVSGVTGL SEQ ID NO:3479
ILSPSQSPIFIQPTPSPPMSPLRPGLDLVFANLPDHSAPLGVTRPSAPPLPHVVDLPQLG
PRR
(Hepatitis G Virus Polyprotein Precursor
(AAB65834)
MAVLLLLLVVEAGAILAPATHVCRASGQYFLTNCCALENIGFCLEGGCLVPLGCTVCTDR SEQ ID NO:3480
CWPLYQAGLAVRPGKSAAQLVGELGSLYGPLSVSAYVAGILGLGEVYSGVLTVGVALTRR
AYPVPNLTCSVECELKWESEFWRWTEQLASNYWILEYLWKVPFDFWRGVMSLTPLLVCVA
ALLLLEQRIVMVFLLVTMAGMSQGAPASVLGSRPFEAGLTWQSCSCEANGSRVPTGERVW
DRGNVTLLCDCPNGPWVWLPAVCQAIGWGDPITHWSHGQNQWPLSCPQFVYGAVSVTCVW
GSVSWFASTGGRDSKIDVWSLVPVGSASCTIAALGSSDRDTVVELSEWGIPCATCILDRR
PASCGTCVRDCWPETGSVRFPFHRCGAGPRLTKDLEAVPFVNRTTPFTIRGPLGNQGKGN
PVRSPLGFGSYTMTKIRDSLHLVKCPTPAIEPPTGTFGFFPGTPPLNNCMLLGTEVSEVL
GGAGLTGGFYEPLVRRCSELAGRRNPVCPGFAWLSSGRPDGFIHVQGHLQEVGAGNFIPP
PRWLLLDFVFVLLYLVKLAEARLVPLILLLLWWWVNQLAVLGLPTAHAAVAGEVFAGPAL
SWCLGLPFVSMILGLANLVLYFRWMGPQRLMFLVLWKLARGAFPLALLMGIPATRGRTSV
LGAEFCFDVTFEVDTSVLGWVVASVVAWATALLSSMSAGGWRHKAVIYRTWCKGYQALRQ
RVVRSPLGEGRPTKPLTFAWCLASYIWPDAVMLVVVGLVLLFGLFDALDWALEELLVSRP
SLRRLARVVECCVMAGEKATTIRLVSKMCARGAYLFDHMGSLSRAVKERLPEWDAALEPL
SFTRTDCRTIRDAARTLSCGQCVMGLPVVARRGDEVLIGVFQDVNHLPPGFVPTAPVVIR
RCGKGFLGVTKAALTGRDPDLHPGNVMVLGTATSRSMGTCLNGLLFTTFHGASSRTIATP
VGALNPRWWSASDDVTVYPLPDGANSLTPCTCQAESCWVIRSDGALCHGLSKGDKVELDV
AMEVSDFRGSSGSPVLCDEGHAVGMLVSVLHSGGRVTAARFIRPWTQVPTDAKTTTEPPP
VPAKGVFKEAPLFMPTGAGKSTRVPLEYGNNGHKVLILNPSVATVRAMGPYMERLAGRHP
SIYCGHDTTAFTRITDSPLTYSTYGRFLANPRQMLRGVSVVICDECHSHDSTVLLGIGRV
RELARGCGVQLVLYATATPPGSPNVQHPSIIETKLDVGEIPFYGHGISLERMRTGRHLVF
CHSKAECERLAGQFSSRGVNAIAYYRGKDSSIIKDGDLVVCATDALSTGYTGNFDSVTDC
GLVVEEVVEVTLDPTITISLRTVPASAELSMQRRSRTGRGRSGRYYYAGVGKAPAGVVRS
GPVWSAVEAGMTWYGMEPDLTANLLRLYDDCPYTAATAADIGEAAVFFAGLAPLRMHPDV
SWAKVRGVNWPLLVGVQRTMCRETLSPGPSDDPQWAGLKGPNPVPLLLRWGNDLPSKVAG
HHIVDDLVRRLGVAEGYVRCDAGPILMVGLAIAGGMIYASYTGSLVVVTDWDVKGGGNPL
YRNGDQATPQPVVQVPPVDHRPGGESAPSDAKTVTDAVAATQVNCDWSVNTLSIGEVLAL
AQAKTAEAYTATAKWLAGCYTGTRAVPTVSIVDKLFAGGWAAVVGHCHSVIAAAVAAYGA
SRSPPLAAAASYLMGLGDGGNAQARLASALLLGAAGTALGTPVVGLTMAGAFMGGASVSP
SLVTVLLGAVGGWEGVVNAASLVFDFMAGKLSTDDLWYAIPVLTSPGAGLAGIALGLVLY
SANNSGTTTWLNRLLTTLPRSSCIPDSYFQQADYCDKVSAMLRRLSLTRTVVALVNREPR
VDEVQVGYVWDLWEWIMRQVRMVIARVRALCPVVSLPLWHCGEGWSGEWLLDGHVESRCL
CGCVITGDVFNGQLKDPVYSTKLCRHYWMGTVPVNMLGYGETSLLLASDTPKVVPFGTSG
WAEVVVTPTHVVIRRTSCYKLLRQQILSAAVAEPYYVDGIPVSWEADARAPAMVYGPGQS
ATIDGERYTLPHQLRMRNVAPSEVPSEVSIETGTETEDSELTEADLPPAAAALQAIENAA
RILEPHIDVTMEDCSTPSLCGSSREMPVWGEDVPRTPSPALISVTESSSDEKTPSASSSQ
EDTPSSDSFEVTQESDTAESEDSVFNVALSVPKALFPQSDATRKLTVPMSCCVEKSVTRF
FSLGLTVADVASLCEMEIQNHTAYCDKVRTPLELQVGCLVGNELTFECDKCEARQETLAS
FSYIWSGVPLTRATPAKPPVVRPVGSLLVADTTKVYVTNPHNVGRRVDNVTFWRAPRVHD
KFLVDSIERARRAAQACLSMGYTYEEATRTVRPHAAMGWGSKVSVKDLATPAGKMSVHDR
FQEIAEGTPVPFTLTVKKEVFFKDRKEEKAPRFIVFPPLNFRTAAKLILGDPARVPKAVL
GGAYAFQYTPNQRVKEMLKLWESKKTPCAICVDATCFDSSITEEDVALETELYALASDHP
EWVPALGKYYASGTMVTPEGVPVGERYCRSSGVLTTSASNCLTCYIKVKAACDRVGLKNV
SFLIAGDDCLIICERPMCDPSEALGPALASYGYACEPSYHASLDAAPFCSTWLAECNADG
KRHFFLTTDFRRPLARMSSEYSDPMASAIGYILLYPWHPITRWVIIPHVLTCAFRGGGTP
SDPVWCQVHGNYYKFPLDKLPNIIVALHGPAALRVTADTTKTKMEAGKVLSDLKLPGLAV
HRKKAGALRTRMLRSHDWAELARGLLWHPGLRLPPPEIAGTPGGFPLSPPYMGVVHQLDF
TAQRSRWWWLGFLTLLIVALFG
(Human Herpesvirus 5 UL32 (AAG31644))
MSLQFIGLQRRDVVALVNFLRHLTQKPDVDLEAHPKILKKCGEKRLHRRTVLFNELMLWL SEQ ID NO:3481
GYYRELRFHNPDLSSVLEEFEVRCAAVARRGYTYPFGDRGKARDHLAVLDRTEFDTDVRH
DAEIVERALVSAVILAKMSVRETLVTAIGQTEPIAFVHLKDTEVQRIEENLEGVRRNMFC
VKPLDLNLDRHANTALVNAVNKLVYTGRLIMNVRRSWEELERKCLARIQERCKLLVKELR
MCLSFDSNYCRNILKHAVENGDSADTLLELLIEDFDIYVDSFPQSAHTFLGARPPSLEFD
DDANLLSLGGGSAFSSVPKKHVPTQPLDGWSWIASPWKGHKPFRFEAHGSLAPAADAHAA
RSAAVGYYDEEEKRRERQKRVDDEVVQREKQQLKAWEERQQNLQQRQQQPPPPTRKPGAS
RRLFGSSADEDDDDDDDEKNIFTPIKKPGTSGKGAASGNGVSSIFSGMLSSGSQKPTSGP
LNIPQQQQRHAAFSLVSPQVTKASPGRVRRDSAWDVRPLTETRGDLFSGDEDSDSSDGYP
PNRQDPRFTDTPVDITDTETSAKPPVTTAYKFEQPTLTFGAGVNVPAGAGAAILTPTPVN
PSTAPAPAPTPTFAGTQTPVNGNSPWAPTAPLPGDMNPANWPRERAWALKNPHLAYNPFR
MPTTSTTSQNNVSTTPRRPSTPRAAVTQTASQNAADEVWALRDQTAESPVEDSEEEDDDS
SDTGSVVSLGHTTPSSDYNDVISPPSQTPEQSTPSRIRKAKLSSPMTTTSTSQKPVLGKR
VATPHASARAQTVTSTPVQGRVEKQVSGTPSTVPATLLQPQPASSKTTSSRNVTSGARTS
SASARQPSASASVLSPTEDDVVSPVTSPLSMLSSASPSPAKSAPPSPVKGRGSRVGVPSL
KPTLGGKAVVGRPPSVPVSGSAPGRLSGTSRAASTTPTYPAVTTVYPPSSTAKSSVSNAP
PVASPSILKPGASAALQSRRSTGTAAVGSPVKSTTGMKTVAFDLSSPQKSGTGPQPGSAG
MGGAKTPSDAVQNILQKTEKIKNTEE
(Human Parechovirus 2 Polyprotein
(NP_041865))
METIKSTADMATGVTKTIDATINSVNEIITNTDNASGGDTLTKVADDASNILGPNCYATT SEQ ID NO:3482
SEPENKDVVQATTTVNTTNLTQHPSAPTLPFTPDFSNVDTFHSMAYDTTTGSKNPNKLVR
LTTHAWASTLQRGHQIDHVNLPVDFWDEQRKPAYGHAKYFAAVRCGFHFQVQVNVNQGTA
GSALVVYEPKPVVDYDKDLEFGAFTNLPHVLNNLAETTQADLCIPYVADTNYVKTDSSDL
GQLKVYVWTPLSIPSGSSNQVDVTILGSLLQLDFQNPRVYGQNVDIYDTAPSKPIPLRKT
KYLTMSTKYKWTPNKVDIAEGPGSMNMANVLSTTAAQSVALVGEPAFYDPRTAGSKSRFD
DLVKISQLFSVMADSTTPSANHGIDQKGYFKWSANSDPQAIVHRNLVHLNLFPNLKVFEN
SYSYFRGSLIIRLSVYASTFNRGRLNGFFPNSSTDETSEIDNAIYTICDIGSDNSFEITI
PYSFSTWMRKTHGKPIGLFQIEVLNRLTYNYSSPNEVYCIVQGKNGQDAKFFCPTGSLVT
FQNSWGSQMDLTDPLCIEDSVEDCKQTITPTELGLTSAQDDGPLGNDKPNYFLNFKSMNV
DIFTVSHTKVDNIFGRAWFAHVHDFTNDGLWRQGLEFPKEGHGALSLLFAYFTGELNIHV
LFLSDRGFLRVGHTYDTETNRTNFLSSSGIITVPAGEQMTLSVPSYSNKPLRTVRSSNAL
GYLLCKPLLTGTSSGRIEIFLSLRCPNFFFPLPAPKPATRKYRGDLATWSDQSPYGRQGK
KQLMKLAYLDRGFYKHYGIVVGDDVYQLDSDDIFKTALTGKAKFTKTRLTPDWVVEEECE
LDYFRIKYLESSVNSEHIFSVDNNCETIAKDIFGSHSLSQHQQIGLIGTILLTAGLNSTI
KTPVNPTTIKEFFNHAIEGDEQGLSLLVQKCTTFFSSAATELLDNDLVKFIIKILVRILC
YMVLYCHKPNILTTACLSTLLVMDVTSSSVLSPSCKALMQCLMDGDVKKLAEVVAESMSN
TDDDEIKEQICDTVKYTKQILSNQGPFKGFNEISTAFRHIDWWIQTLLKIKDMVLSVFKP
SVEKRAVEWLERNKEHVCSILDYASDIIVKSKDQTKNKTQEFYQRYNDCLSKFKPIMAMC
FRSCHNSISNTVYRLFQELARIPNRMATQNDLIRVEPIGIWIQGEPGQGKSFLTHTLSKQ
LQKTCGLQGIYTNPTASEFMDGYDNQDIHLIDDLGQTRKERDIEMLCNCISSDPDIVPMA
HLEEKGKFYTSKLVIATTNKPDFSSTVLLDSGALRRRFPYIMHIEAAKHYSKSGKLNVSQ
ANPHMSTGECWEVSKNGRDWETLKLKELIDKITVDYKERIANYNTWKKQLEDQTLDDLDD
AVSYIKHNYPDAIPYIDEYLNIEMSTLIEQMEAFIEPKPSVFKCFASRVGDKIKEASREV
VKWFSDKLKSMLNFVERNKAWLTVVSAVTSAIGILLLVTKIFKKEESKDERAYNPTLPVA
KPKGTFPVSQREFKNEAPYDGQLEHIISQMAYITGSTTGHITHCAGYQHDEIILHGHSIK
YLEQEEELTLHYKNKVFPIEQPSVTQVTLGGKPMDLAIVKCKLPFRFKKNSKYYTNKIGT
ESMLIWMTEQGIITKEVQRVHHSGGIKTREGTESTKTISYTVKSCKGMCGGLLISKVEGN
FKILGMHIAGNGEHGVAIPFNFLKNDNSDQGIVTEVTPIQPMYINTKSQIHKSPVYGAVE
VKMGPAVLSKSDTRLEEPVDCLVKKSASKYRVNKFQVNNELWQGVKACVKSKFREIFGVN
GIVDMKTAILGTSHVNSMDLSTSAGYSFVKSGYKKKDLICLEPFSVSPMLEKLVQEKFHN
LLKGNQITTIFNTCLKDELRKLDKIATGKTRCIEACEIDYCIVYRMIMMEIYDKIYQTPC
YYSGLAVGINPYRDWHFMINALNDYNYEMDYSQYDGSLSSMLLWEAVQVLAYCHDSPDLV
MQLHKPVIDSDHVVFNERWLIHGGMPSGSPCTTVLNSLCNLMMCIYTTNLISPGIDCLPI
VYGDDVILSLDKEIEPERLQSTMAESFGAEVTGSRKDEPPSLKPRMEVEFLKRKPGYFPE
STFIVGKLDTENNIQHLMWNKNFSTFKQQLQSYLMELCLHGKDTYQHYVKILNPYLKEWN
IPVDDYEVVIGKLVPMVFD
(Semliki Forest Virus Polyprotein(CAA76683))
MAAKVHVDIEADSPFIKSLQKAFPSFEVESLQVTPNDHANARAFSHLATKLIEQETDKDT SEQ ID NO:3483
LILDIGSAPSRRMMSTHKYHCVCPMRSAEDPERLVCYAKKLAAASGKVLDREIAGKITDL
QTVMATPDAESPTFCLHTDVTCRTAAEVAVYQDVYAVHAPTSLYHQAMKGVRTAYWIGFD
TTPFNFDALAGAYPTYATNWADEQVLQARNIGLCAASLTEGRLGKLSILRKKQLKPSDTV
MFSVGSTLYTESRKLLRSWHLPSVFHLKGKQSFTCRCDTIVSCEGYVVKKITMCPGLYGK
TVGYAVTHHAEGFLVCKTTDTVKGERVSFPVCTYVPSTICDQMTGILATDVTPEDAQKLL
VGLNQRIVVNGRTQRNTNTMKNYLLPVVAVAFSKWAREYKADLDDEKPLGVRERSLTCCC
LWAFKTKKMHTMYKKPDTQTIVKVPSEFNSFVIPSLWSTGLAIPVRSRIKMLLAKKTKRE
LIPALDASSARDAEQEEKERLEAELTREALPPLVPIAPAETGVVDVDVEELEYRAGAGVV
ETPRSALKVTAQPNDVLLGNYVVLSPQTVLKSSKLAPVHPLAEQVKIITHNGRAGRYQVD
GYDGRVLLPCGSAIPVPEFQALSESATMVYNEREFVNRKLYHIAVHGPSLNTDEENYEKV
RAERTDAEYVFDVDKKCCIKREEASGLVLVGELTNPPFHEFAYEGLKIRPSAPYKTTVVG
VFGVPGSGKSAIIKSLVTKHDLVTSGKKENCQEIVNDVKKHRGLDIQAKTVDSILLNGCR
RAVDILYVDEAFACHSGTLLALIALVKPRSKVVLCGDPKQCGFFNNMQLKVNFNHNICTE
VCHKSISRRCTRPVTAIVSTLHYGGKMRTTNPCNKPIIIDTTGQTKPKPGDIVLTCFRGW
VKQLQLDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYAPASEHVNVLLTRTEDRLVW
KTLAGDPWIKVLSNIPQGNFTATLEEWQEEHDKIMKVIEGPAAPVDAFQNKAINCWAKSL
VPVLDTAGIRLTAEEWSTIITAFKEDRAYSPEVALNEICTKYYGVDLDSGLFSAPKVSLY
YENNHWDNRPGGRMYGFNAATAARLEARHTFLKGQWHTGKQAVIAERKIQPLSVLDNVIP
INRRLPHALVAEYKTVKGSRVEWLVNKVRGYHVLLVSEYNLALPRRRVTWLSPLNVTGAD
RCYDLSLGLPADAGRYDLVFVNIHTEFRIHHYQQCVDHAMKLQMLGGDALRLLKPGGNLL
MRAYGYADKISEAVVSSLSRKFSSARVLRPDCVTSNTEVFLLFSNFDNGKRPSTLHQMNT
KLSAVYAGEANHTAGC
(HIV GAG protein (AF324493))
MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQWGQLQ SEQ ID NO:3484
PSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAA
DTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVLPMFSALSEGAT
PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTT
STLQEQIGWMTHNPPIPVGEIYKRWIILNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKA
RVLAEAMSQVTNPATIMIQKGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEG
HQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTTPSQKQEPID
KELYPLASLRSLFGSDPSSQ
CTTCAGAGCAGACCAGAGCCAACAGCCCCACCAGAAGAGAGCTTCAGGTTTG SEQ ID NO:3485
GGGAAGAGACAACAACTCCCTCTCAGAAGCAGGAGCCGATAGACAAGGAAC
TGTATCCTTTAGCTTCCCTCAGATCACTCTTTGGCAGCGACCCCTCGTCACAA
T

Claims

1. A composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell, wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

2. The composition according to claim 1, wherein said peptide does not contain a contiguous amino acid sequence of 10 or more residues of an HIV GAG protein that encompasses the late domain motif of said GAG protein.

3. The composition according to claim 1, wherein X1 is threonine (T) or serine (S), and X2 is alanine (A).

4. The composition of claim 1, wherein said peptide is covalently linked to said transporter.

5. The composition of claim 4, wherein said transporter is selected from the group consisting of penetratins, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof.

6. The composition of claim 4, wherein said transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

7. The composition according to claim 1, wherein said transporter is selected from the group consisting of liposomes, dendrimers, and siderophores.

8. The composition according to claim 1, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

9. The composition according to claim 1, wherein said peptide includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein, said contiguous amino acid sequence encompassing the late domain motif of said Matrix protein.

10. The composition according to claim 1, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, said contiguous amino acid sequence encompassing the late domain motif of said first protein.

11. A composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

12. The composition according to claim 11, wherein said transporter is capable of increasing the uptake of said peptide by a mammalian cell by at least 300%.

13. The composition according to claim 11, wherein X1 is threonine (T) or serine (S), and X2 is alanine (A).

14. The composition of claim 11, wherein said peptide is covalently linked to said transporter.

15. The composition of claim 14, wherein said transporter is selected from the group consisting of penetratins, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof.

16. The composition of claim 14, wherein said transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

17. The composition according to claim 11, wherein said transporter is selected from the group consisting of liposomes, dendrimers, and siderophores.

18. The composition according to claim 11, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

19. The composition according to claim 11, wherein said peptide includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein, said contiguous amino acid sequence encompassing the late domain motif of said Matrix protein.

20. The composition according to claim 11, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

21. The composition according to claim 11, wherein said peptide consists of from 8 to about 50 amino acids.

22. The composition according to claim 11, wherein said peptide consists of from 10 to about 20 amino acids.

23. A composition comprising a hybrid polypeptide, said hybrid polypeptide consists of a peptide covalently linked to a peptidic transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, wherein said peptide consists of from about 8 to about 100 amino acid residues, comprises an amino acid sequence motif PX1X2P, and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

24. The composition according to claim 23, wherein said peptide consists of from about 9 to about 20 amino acid residues.

25. The composition according to claim 24, wherein said transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 300%.

26. The composition according to claim 23, wherein said transporter is selected from the group consisting of penetrating, l-Tat49-57, retro-inverso isomers of l-Tat49-57, L-arginine oligomers, L-lysine oligomers, L-histidine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, HSV-1 structural protein VP22 and fragments thereof, and peptides consisting of at least six contiguous amino acid residues that are L-arginine oligomers, L-lysine oligomers, L-histidine oligomers or a combination thereof.

27. An isolated nucleic acid encoding the hybrid polypeptide according to claim 23.

28. An isolated nucleic acid encoding the hybrid polypeptide according to claim 24.

29. An isolated nucleic acid encoding the hybrid polypeptide according to claim 25.

30. A host cell comprising the isolated nucleic acid according to claim 27.

31. A host cell comprising the isolated nucleic acid according to claim 28.

32. A host cell comprising the isolated nucleic acid according to claim 29.

33. An isolated peptide consisting of a contiguous amino acid sequence of from 8 to about 30 amino acid residues of a viral protein selected from the group consisting of HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, wherein said contiguous amino acid sequence encompasses the P(T/S)AP motif of said viral protein, wherein wherein said peptide is capable of binding the UEV domain of Tsg101, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein or Ebola virus Matrix (EbVp40) protein that is sufficient to impart an ability to bind the UEV domain of Tsg100 on said peptide.

34. The isolated peptide according to claim 33, wherein said isolated peptide consists of from 9 to about 20 amino acid residues.

35. The isolated peptide of claim 33, wherein said peptide comprises of an amino acid sequence selected from the group consisting of SEQ ID NOs: 38-125, SEQ ID NOs: 126-268, SEQ ID NOs: 269-554, SEQ ID NOs: 555-697, SEQ ID NOs: 698-749, SEQ ID NOs: 750-892, SEQ ID NOs: 893-1035, SEQ ID NOs: 1036-1178, SEQ ID NOs: 1179-1321, SEQ ID NOs: 1322-1464, SEQ ID NOs: 1465-1607, SEQ ID NOs: 1608-1750, SEQ ID NOs: 1751-1893, SEQ ID NOs: 1894-2036, SEQ ID NOs: 2037-2179, SEQ ID NOs: 2180-2322, SEQ ID NOs: 2323-2459, SEQ ID NOs: 2460-2602, SEQ ID NOs: 2603-2745, SEQ ID NOs: 2888-3030, SEQ ID NOs: 3174-3316, and SEQ ID NOs: 3317-3459.

36. An isolated nucleic acid encoding the isolated peptide according to claim 33.

37. An isolated nucleic acid encoding the isolated peptide according to claim 34.

38. An isolated nucleic acid encoding the isolated peptide according to claim 35.

39. A method for inhibiting HIV budding from cells, comprising: administering to cells a composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell, wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

40. A method for inhibiting HIV budding from cells, comprising: introducing into cells infected with HIV a peptide consisting of from 8 to about 30 amino acid residues and having an amino acid sequence motif PX1X2P, wherein X1 and X2 are amino acids, and X2 is not R, wherein said peptide is capable of binding the UEV domain of Tsg101, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

41. The method of claim 40, wherein said introducing step comprises administering to the cells a nucleic acid encoding said peptide.

42. The method of claim 41, wherein X1 is T or S, and X2 is A.

43. The method of claim 41, wherein said peptide includes a contiguous amino acid sequence of at least 9 residues of a viral protein selected from the group consisting of HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompasses the P(T/S)AP motif of said viral protein.

44. A method for treating HIV infection, comprising: introducing into a patient in need of such treatment a peptide consisting of from 8 to about 30 amino acid residues and having an amino acid sequence motif PX1X2P, wherein X1 and X2 are amino acids, and X2 is not R, wherein said peptide is capable of binding the UEV domain of Tsg101, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

45. The method of claim 44, wherein said introducing step comprises administering to the cells a nucleic acid encoding said peptide.

46. The method of claim 45, wherein X1 is T or S, and X2 is A.

47. The method of claim 45, wherein said peptide includes a contiguous amino acid sequence of at least 9 residues of a viral protein selected from the group consisting of HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompasses the P(T/S)AP motif of said viral protein.

48. A method for treating HIV infection, comprising: administering to a patient in need of such treatment a composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell, wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

49. The method according to claim 48, wherein X1 is threonine (T) or serine (S), and X2 is alanine (A).

50. The method according to claim 48, wherein said peptide is covalently linked to said transporter.

51. The method according to claim 50, wherein said transporter is selected from the group consisting of penetrating, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof.

52. A method according to claim 50, wherein said transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

53. A method according to claim 50, wherein said transporter is selected from the group consisting of liposomes, dendrimers, and siderophores.

54. A method according to claim 48, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of Ebola virus Matrix (EbVp40) protein, HBV PreS 1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

55. A method according to claim 48, wherein said peptide includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein, said contiguous amino acid sequence encompassing the late domain motif of said Matrix protein.

56. A method according to claim 48, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, said contiguous amino acid sequence encompassing the late domain motif of said first protein.

57. A method for treating HIV infection, comprising: administering to a patient in need of such treatment a composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

58. A method according to claim 57, wherein said transporter is capable of increasing the uptake of said peptide by a mammalian cell by at least 300%.

59. A method according to claim 57, wherein X1 is threonine (T) or serine (S), and X2 is alanine (A).

60. A method according to claim 57, wherein said peptide is covalently linked to said transporter.

61. A method according to claim 60, wherein said transporter is selected from the group consisting of penetrating, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof.

62. A method according to claim 60, wherein said transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

63. A method according to claim 57, wherein said transporter is selected from the group consisting of liposomes, dendrimers, and siderophores.

64. A method according to claim 57, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

65. A method according to claim 57, wherein said peptide includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein, said contiguous amino acid sequence encompassing the late domain motif of said Matrix protein.

66. A method according to claim 57, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

67. A method according to claim 57, wherein said peptide consists of from 8 to about 50 amino acids.

68. A method according to claim 57, wherein said peptide consists of from 10 to about 20 amino acids.

69. A method for treating HIV infection, comprising administering to a patient in need of such treatment a composition comprising a hybrid polypeptide, said hybrid polypeptide consists of a peptide covalently linked to a peptidic transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, wherein said peptide consists of from about 8 to about 100 amino acid residues, comprises an amino acid sequence motif PX1X2P, and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R, and wherein said peptide does not contain a contiguous amino acid sequence of an HIV GAG protein that is sufficient to impart an ability to bind the UEV domain of Tsg101 on said peptide.

70. A method according to claim 69, wherein said peptide consists of from about 9 to about 20 amino acid residues.

71. A method according to claim 70, wherein said transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 300%.

72. A method according to claim 69, wherein said transporter is selected from the group consisting of penetratins, l-Tat49-57, retro-inverso isomers of l-Tat49-57, L-arginine oligomers, L-lysine oligomers, L-histidine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, HSV-1 structural protein VP22 and fragments thereof, and peptides consisting of at least six contiguous amino acid residues that are L-arginine oligomers, L-lysine oligomers, L-histidine oligomers or a combination thereof.

73. A method for treating an infection caused by a virus, wherein the virus is a member of the group consisting of hepatitis B virus, human herpesvirus 1, and human herpesvirus 2, said method comprising: introducing into a patient in need of such treatment a peptide consisting of from 8 to about 30 amino acid residues and having an amino acid sequence motif PX1X2P, wherein X1 and X2 are amino acids, and X2 is not R, wherein said peptide is capable of binding the UEV domain of Tsg101.

74. The method of claim 73, wherein said introducing step comprises administering to the cells a nucleic acid encoding said peptide.

75. The method of claim 74, wherein X1 is T or S, and X2 is A.

76. The method of claim 74, wherein said peptide includes a contiguous amino acid sequence of at least 9 residues of a viral protein selected from the group consisting of HIV GAG protein, Ebola virus matrix protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, Hepatitis E Virus ORF-3 protein, and Semliki forest virus polyprotein, wherein said contiguous amino acid sequence encompasses the P(T/S)AP motif of said viral protein.

77. A method for treating an infection caused by a virus, wherein the virus is a member of the group consisting of hepatitis B virus, human herpesvirus 1, and human herpesvirus 2, said method comprising: administering to a patient in need of such treatment a composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell, and wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R.

78. The method according to claim 77, wherein X1 is threonine (T) or serine (S), and X2 is alanine (A).

79. The method according to claim 77, wherein said peptide is covalently linked to said transporter.

80. The method according to claim 79, wherein said transporter is selected from the group consisting of penetratins, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof.

81. A method according to claim 79, wherein said transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

82. A method according to claim 79, wherein said transporter is selected from the group consisting of liposomes, dendrimers, and siderophores.

83. A method according to claim 77, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HIV GAG protein, Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, human parechovirus 2 polyprotein, Hepatitis E Virus ORF-3 protein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

84. A method according to claim 77, wherein said peptide includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein or HIV GAG protein, said contiguous amino acid sequence encompassing the late domain motif of said Matrix protein or GAG protein.

85. A method according to claim 77, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, said contiguous amino acid sequence encompassing the late domain motif of said first protein.

86. A method for treating an infection caused by a virus, wherein the virus is a member of the group consisting of hepatitis B virus, human herpesvirus 1, and human herpesvirus 2, said method comprising: administering to a patient in need of such treatment a composition comprising a peptide associated with a transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, and wherein said peptide includes an amino acid sequence motif PX1X2P and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R.

87. A method according to claim 86, wherein said transporter is capable of increasing the uptake of said peptide by a mammalian cell by at least 300%.

88. A method according to claim 86, wherein X1 is threonine (T) or serine (S), and X2 is alanine (A).

89. A method according to claim 86, wherein said peptide is covalently linked to said transporter.

90. A method according to claim 89, wherein said transporter is selected from the group consisting of penetratins, l-Tat49-57, d-Tat49-57, retro-inverso isomers of l- or d-Tat49-57, L-arginine oligomers, D-arginine oligomers, L-lysine oligomers, D-lysine oligomers, L-histidine oligomers, D-histidine oligomers, L-ornithine oligomers, D-ornithine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, and HSV-1 structural protein VP22 and fragments thereof, and peptoid analogs thereof.

91. A method according to claim 89, wherein said transporter is a peptide having at least six contiguous amino acid residues that are L-arginine, D-arginine, L-lysine, D-lysine, L-histidine, D-histidine, L-ornithine, D-ornithine, or a combination thereof.

92. A method according to claim 86, wherein said transporter is selected from the group consisting of liposomes, dendrimers, and siderophores.

93. A method according to claim 86, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HIV GAG protein, Ebola virus Matrix (EbVp40) protein, HBV PreS1/PreS2/S envelope protein, HSV1 RL2 protein, HSV2 virion glycoprotein K, HSV2 Strain 333 glycoprotein I, EBV nuclear protein EBNA2, Influenza A virus hemagglutinin, HPV L1 proteins, HPV L2 proteins, HPV late proteins, HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, Rubella virus non-structural protein, Colorado tick fever virus VP12, foot-and-mouth disease virus VP1 capsid protein, human foamy virus GAG protein, hepatitis E virus ORF-3 protein, hepatitis G virus polyprotein precursor, HSV5 UL32 protein, HSV5 UL32 protein, human parechovirus 2 polyprotein, Hepatitis E Virus ORF-3 protein, and Semliki forest virus polyprotein, and wherein said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

94. A method according to claim 86, wherein said peptide includes a contiguous amino acid sequence of Ebola virus Matrix (EbVp40) protein or HIV GAG protein, said contiguous amino acid sequence encompassing the late domain motif of said Matrix protein or GAG protein.

95. A method according to claim 86, wherein said peptide includes a contiguous amino acid sequence of a first protein selected from the group consisting of HTLV-2 GAG protein, West Nile virus polyprotein precursor, Measles virus matrix protein, human foamy virus GAG protein, hepatitis G virus polyprotein precursor, human parechovirus 2 polyprotein, and Semliki forest virus polyprotein, said contiguous amino acid sequence encompassing the P(T/S)AP motif of said first protein.

96. A method according to claim 86, wherein said peptide consists of from 8 to about 50 amino acids.

97. A method according to claim 86, wherein said peptide consists of from 10 to about 20 amino acids.

98. A method for treating an infection caused by a virus, wherein the virus is a member of the group consisting of hepatitis B virus, human herpesvirus 1, and human herpesvirus 2, said method comprising: administering to a patient in need of such treatment a composition comprising a hybrid polypeptide, said hybrid polypeptide consists of a peptide covalently linked to a peptidic transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 100%, and wherein said peptide consists of from about 8 to about 100 amino acid residues, comprises an amino acid sequence motif PX1X2P, and is capable of binding the UEV domain of Tsg101, wherein X1 and X2 are amino acids, and X2 is not R.

99. A method according to claim 98, wherein said peptide consists of from about 9 to about 20 amino acid residues.

100. A method according to claim 99, wherein said transporter that is capable of increasing the uptake of said peptide by a mammalian cell by at least 300%.

101. A method according to claim 98, wherein said transporter is selected from the group consisting of penetratins, l-Tat49-57, retro-inverso isomers of l-Tat49-57, L-arginine oligomers, L-lysine oligomers, L-histidine oligomers, fibroblast growth factor and fragments thereof, Galparan and fragments thereof, HSV-1 structural protein VP22 and fragments thereof, and peptides consisting of at least six contiguous amino acid residues that are L-arginine oligomers, L-lysine oligomers, L-histidine oligomers or a combination thereof.