Trophic factor combinations for nervous system treatment

Abstract

The present invention relates to a composition including an effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect and an effective amount of a neurotrophin. The composition can also include an effective amount of at least one of a growth factor and a neuropeptide. The present invention also relates a method of treating an injury to a nervous system of an animal that includes the steps of identifying the injury to the nervous system and applying to the injury an effective amount of at least one of antimicrobial peptide and a substance having an antimicrobial peptide effect. The method can also include applying an effective amount of one or more trophic factors selected from the group consisting of a growth factor, a neurotrophin, and a neuropeptide to the injury.

Description

FIELD OF THE INVENTION

The invention relates to combinations of neurochemically active agents for treating a nervous system and the methods of treating a nervous system with the combinatorial treatments.

BACKGROUND OF THE INVENTION

The nervous system is comprised of two divisions: the central nervous system (CNS) and the peripheral nervous system (PNS). The CNS includes the brain and the spinal cord and controls most functions of the body and mind. The remainder of the nervous system is the PNS. Nerves of the PNS connect the CNS to sensory organs (such as the eyes and ears), other organs of the body, muscles, blood vessels, and glands. The peripheral nerves include the cranial nerves, the spinal nerves, and roots.

The CNS controls all voluntary movement, such as movement of the legs during walking, and all involuntary movement, such as beating of the heart. The spinal cord connects the body and the brain by transmitting information to and from the body and the brain.

The nervous system can be injured in numerous ways, and injuries can be traumatic. For instance, sudden physical assault on a portion of the nervous system results in a traumatic injury. In the case of a traumatic brain injury, the injury can be focal, i.e., confined to a specific area of the brain, or diffuse, i.e., involving more than one area of the brain.

Injuries to the nervous system include contusions, which are bruises of the nervous system, and blood clots. Blood clots can form in or around the nervous system. For example, when bleeding occurs between the skull and the brain, the blood forms a clot. This puts pressure on the brain, which can lead to changes in brain function.

Spinal cord injuries (SCI) are a particular type of injury to the nervous system. As of the year 2000, approximately 450,000 people in the United States have sustained SCI, with more than 10,000 new cases reported in the United States every year. Motor vehicle accidents are the leading cause of SCI (44 percent), followed by acts of violence (24 percent), falls (22 percent), sports injuries (8 percent), and other causes (2 percent). Of the 10,000 new cases of SCI in the United States each year, 51.7% have tetraplegia, i.e., injuries to one of the eight cervical segments of the spinal cord, and 56.7% have paraplegia, i.e., lesions in the thoracic, lumbar, or sacral regions of the spinal cord. Since 1990, the most frequent neurologic category is incomplete tetraplegia (29.5%), followed by complete paraplegia (27.9%), incomplete paraplegia (21.3%), and complete tetraplegia (18.5%).

With spinal cord injuries in the neck, significant impairment of breathing may result. The most frequent site of spinal injury is the neck or cervical region and, of these, the major cause of death arises from respiratory complications. For patients that survive a major spinal cord injury in the neck, they may spend the rest of their lives depending on an artificial ventilator or phrenic nerve pacemaker to sustain their lives. For others with less severe respiratory impairment, they may be able to breathe normally, but are unable to sigh or breathe deeply and maintain the integrity of the lung. As a consequence, regions of the lung will collapse in these patients, causing pneumonia and allowing other respiratory infections to become established. Clearly, restoration of normal breathing ability, including deep breaths and sighs, is a major goal in the treatment of spinal cord injury patients.

Injury to the spinal cord and other parts of the nervous system may be particularly devastating to life and the quality of life. In addition, injury to the nervous system can engender serious economic losses to the individual and to society. Currently, there are few effective treatment options available for patients with spinal cord injuries, although there are a few promising indications that physical therapy or chronic intermittent hypoxia (CIH), may have beneficial effects. Exposure to intermittent hypoxic episodes has been shown to initiate spinal protein synthesis. However, studies have also shown that chronic intermittent hypoxia has other drawbacks as a treatment for spinal cord injuries. For example, certain CIH treatment methods can cause systemic hypertension, altered sympathetic chemoreflexes, and hippocampal cell death by the process of apoptosis.

Physical training and preconditioning have been used to treat SCI. Almost all patients with spinal cord injuries can now achieve a partial return of function with proper physical therapy that maintains flexibility and function of the muscles and joints, and strengthens the neural pathways that underlie movement. Physical therapy can also help reduce the risk of blood clots and boost the patient's morale. Physical training currently being investigated includes body weight-supported treadmill training, in which patients with partial spinal cord injury “walk” on a treadmill while they are partially supported through the use of a specially designed harness attached to an overhead lift. Unfortunately, this type of therapy is very expensive, and efficacy is far from complete.

SUMMARY OF THE INVENTION

The invention, which is defined by the claims set out at the end of this disclosure, is intended to solve at least some of the problems noted above. A composition is provided that includes an effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect. The composition also includes an effective amount of a neurotrophin.

In another embodiment, the composition also includes an effective amount of at least one of a growth factor and a neuropeptide.

Also provided is a method of treating an injury to a nervous system of an animal. In one embodiment, the method includes the steps of identifying the injury to the nervous system and applying to the injury an effective amount of at least one of antimicrobial peptide and a substance having an antimicrobial peptide effect.

In another embodiment, an injury to the nervous system is identified. An effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect is combined with an effective amount of one or more trophic factors selected from the group consisting of a growth factor, a neurotrophin, and a neuropeptide. The combination is applied to the injury.

A kit is also provided. In an embodiment, the kit includes at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect. The kit also includes a neurotrophin. In another embodiment, the kit also includes a viscous substance. In some embodiments, the kit also includes at least one of a growth factor and a neuropeptide.

BRIEF DESCRIPTION OF THE DRAWINGS

Preferred exemplary embodiments of the invention are illustrated in the accompanying drawings in which:

FIG. 1 is a graph showing change in body weight at 2 weeks after spinal cord injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, the body weight is shown for spinal injury alone (black bar) and for spinal injury and a trophic factor combination made in accordance with the invention (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 2 is a graph showing peak neurogram voltages from the phrenic nerve during inspiration on the side of injury (Y-axis) at 2 weeks post-injury in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, neurogram voltages are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 3 is a graph showing evoked potential voltage (in volts) from the phrenic neurogram on the side of injury at 2 weeks post-injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). The stimulating current was 1000 uA. For each strain of rats, evoked potential voltages are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 4 is a graph showing the stimulating current (in uAmps) required to evoke potentials in the phrenic nerve on the side of injury at 2 weeks post-injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, stimulating currents are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 5 is a graph showing the change in body mass in grams at 2 weeks post-injury (Y-axis) in different Lewis rats (X-axis). The body weight is shown for spinal injury alone (SCI) and for spinal injury and a trophic factor combination made in accordance with the invention (SCI+NTs). FIG. 5 also shows change in phrenic amplitude at 2 weeks post-injury (Y-axis) in the rats (X-axis) for spinal injury alone (SCI) and for spinal injury and a trophic factor combination made in accordance with the invention (SCI+NTs).

Before explaining embodiments of the invention in detail, it is to be understood that the invention is not limited in its application to the details of construction and the arrangement of the components set forth in the following description or illustrated in the drawings. The invention is capable of other embodiments or being practiced or carried out in various ways. Also, it is to be understood that the phraseology and terminology employed herein is for the purpose of description and should not be regarded as limiting.

DETAILED DESCRIPTION

Definitions

To facilitate understanding of the invention, a number of terms are defined below.

As used herein, the term “antimicrobial polypeptide” refers to polypeptides that inhibit the growth of microbes (e.g., bacteria). Examples of antimicrobial polypeptides include, but are not limited to, the polypeptides described in Tables 1 and 2 below. Antimicrobial polypeptides include peptides synthesized from both L-amino and D-amino acids.

As used herein, the term “pore forming agent” refers to any agent (e.g., peptide or other organic compound) that forms pores in a biological membrane. When the pore forming agent is a peptide, the peptide can be synthesized from both L-amino and D-amino acids.

As used herein, the term “growth factor” refers to any compound that is involved in cell differentiation and growth. Growth factors can be proteins (e.g., IGF-1 (insulin-like growth factor 1), IGF-2 (insulin-like growth factor 2), NGF-β (nerve growth factor-β), EGF (epidermal growth factor), CSGF (colony-stimulating growth factor), FGF (fibroblast growth factor), PDGF (platelet-derived growth factor), VEGF (vascular endothelial growth factor), TGF-β (transforming growth factor β, and bone morphogenetic proteins)), either purified from natural sources or genetically engineered, as well as fragments, mimetics, and derivatives or modifications thereof. Further examples of growth factors are provided in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and 5,410,019; all of which are incorporated herein by reference.

The term “trophic factor” as used herein refers to a substance that stimulates growth and development or stimulates increased activity.

The term “hyaluronic acid” includes hyaluronic acid and its derivatives, for instance, esters, salts such as the sodium, potassium, magnesium, calcium, alkaline, alkaline earth metals, and the like, and derivatives such as sulphated or polysulphated hyaluronates, or hyaluronates that have been otherwise modified in a manner way such that the function of hyaluronic acid is retained.

The term “recombinant protein” or “recombinant polypeptide” as used herein refers to a protein molecule expressed from a recombinant DNA molecule. In contrast, the term “native protein” or “native polypeptide” is used herein to indicate a protein isolated from a naturally occurring (i.e., a nonrecombinant) source. Molecular biological techniques may be used to produce a recombinant form of a protein or polypeptide with similar or identical properties as compared to the native form of the protein.

Where an amino acid sequence is recited herein to refer to an amino acid sequence of a naturally occurring protein molecule, amino acid sequence and like terms, such as polypeptide or protein are not meant to limit the amino acid sequence to the complete, native amino acid sequence associated with the recited protein molecule.

As used herein in reference to an amino acid sequence or a protein, the term “portion” (as in “a portion of an amino acid sequence”) refers to fragments of that protein. The fragments may range in size from four amino acid residues to the entire amino acid sequence minus one amino acid (e.g., 5, 6, 7, 8, . . . x−1).

As used herein, the term “variant,” when used in reference to a protein, refers to a protein encoded by partially homologous nucleic acids so that the amino acid sequence of the protein varies. As used herein, the term “variant” encompasses proteins encoded by homologous genes having both conservative and nonconservative amino acid substitutions that do not result in a change in protein function, as well as proteins encoded by homologous genes having amino acid substitutions that cause decreased protein function or increased protein function.

As used herein, the term “fusion protein” refers to a chimeric protein containing the protein of interest (e.g., defensins and fragments thereof) joined to a heterologous protein fragment (e.g., the fusion partner which consists of a non-defensin protein). The fusion partner may enhance the solubility of a defensin as expressed in a host cell, may provide an affinity tag to allow purification of the recombinant fusion protein from the host cell or culture supernatant, or both. If desired, the fusion protein may be removed from the protein of interest (e.g., defensin or fragments thereof) by a variety of enzymatic or chemical processes known to the art.

As used herein, the term “purified” refers to molecules, either nucleic or amino acid sequences, that are removed from their natural environment, isolated, or separated. The percent of a purified component is thereby increased in the sample. For example, an isolated defensin is therefore a purified defensin. Substantially purified molecules are at least 60% free, preferably at least 75% free, and more preferably at least 90% free from other components with which they are naturally associated.

The term “gene” as used herein, refers to a DNA sequence that comprises control and coding sequences necessary for the production of a polypeptide or protein precursor. The polypeptide can be encoded by a full length coding sequence or by any portion of the coding sequence, as long as the desired protein activity is retained.

The term “homology” refers to a degree of complementarity. There may be partial homology or complete homology (i.e., identity). A “partially complementary sequence” is one that at least partially inhibits a completely complementary sequence from hybridizing to a target nucleic acid. This situation is referred to using the functional term “substantially homologous.” The inhibition of hybridization of the completely complementary sequence to the target sequence may be examined using a hybridization assay (e.g., Southern or Northern blot, solution hybridization, and the like) under conditions of low stringency. A substantially homologous sequence or probe will compete for and inhibit the binding (i.e., the hybridization) of a completely homologous sequence or probe to a target under conditions of low stringency. This is not to say that conditions of low stringency are such that non-specific binding is permitted; low stringency conditions require that the binding of two sequences to one another be a specific (i.e., selective) interaction. The absence of non-specific binding may be tested by the use of a second target that lacks even a partial degree of complementarity (e.g., less than about 30% identity). In this case, in the absence of non-specific binding, the probe will not hybridize to the second non-complementary target.

When used in reference to a double-stranded nucleic acid sequence such as a cDNA or a genomic clone, the term “substantially homologous” refers to any probe which can hybridize to either or both strands of the double-stranded nucleic acid sequence under conditions of low stringency as described herein.

As used herein, the term “hybridization” is used in reference to the pairing of complementary nucleic acid strands. Hybridization and the strength of hybridization (i.e., the strength of the association between nucleic acid strands) is impacted by many factors well known in the art including the degree of complementarity between the nucleic acids, stringency of the conditions involved affected by such conditions as the concentration of salts, the T_m (melting temperature) of the formed hybrid, the presence of other components (e.g., the presence or absence of polyethylene glycol), the molarity of the hybridizing strands, and the G:C content of the nucleic acid strands.

As used herein, the term “stringency” is used in reference to the conditions of temperature, ionic strength, and the presence of other compounds, under which nucleic acid hybridizations are conducted. With high stringency conditions, nucleic acid base pairing will occur only between nucleic acid fragments that have a high frequency of complementary base sequences. Thus, conditions of medium or low stringency are often required when it is desired that nucleic acids that are not completely complementary to one another be hybridized or annealed together. It is well known in the art that numerous equivalent conditions can be employed to comprise medium or low stringency conditions. The choice of hybridization conditions is generally evident to one skilled in the art and is normally guided by the purpose of the hybridization, the type of hybridization (DNA-DNA or DNA-RNA), and the level of desired relatedness between the sequences (e.g., Sambrook et al., 1989, Nucleic Acid Hybridization, A Practical Approach, IRL Press, Washington D.C., 1985, for a general discussion of the state of the art).

The stability of nucleic acid duplexes is known to decrease with an increased number of mismatched bases, and further to be decreased to a greater or lesser degree depending on the relative positions of mismatches in the hybrid duplexes. Thus, the stringency of hybridization can be used to maximize or minimize stability of such duplexes. Hybridization stringency can be altered, for example, by adjusting the temperature of hybridization; adjusting the percentage of helix destabilizing agents, such as formamide, in the hybridization mix; and adjusting the temperature and/or salt concentration of the wash solutions. For filter hybridizations, the final stringency of hybridizations can be determined by the salt concentration and/or temperature used for the post-hybridization washes.

“High stringency conditions” when used in reference to nucleic acid hybridization comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH₂PO₄.H₂O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS, 5× Denhardt's reagent and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 0.1×SSPE, 1.0% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.

“Medium stringency conditions” when used in reference to nucleic acid hybridization comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH₂PO₄.H₂O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS, 5× Denhardt's reagent and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 1.0×SSPE, 1.0% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.

“Low stringency conditions” comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH₂PO₄.H₂O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.1% SDS, 5× Denhardt's reagent [50× Denhardt's contains per 500 ml: 5 g Ficoll (Type 400, Pharamcia), 5 g BSA (Fraction V; Sigma)] and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 5×SSPE, 0.1% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.

As used herein, the term “T_m” is used in reference to the melting temperature, which is the temperature at which 50% of a population of double-stranded nucleic acid molecules becomes dissociated into single strands. The equation for calculating the Tm of nucleic acids is well known in the art. The T_m of a hybrid nucleic acid can be estimated using a formula adopted from hybridization assays in 1 M salt, and commonly used for calculating T_m for PCR primers: [(number of A+T)×2° C.+(number of G+C)×4° C.]. (C. R. Newton et al., PCR, 2nd Ed., Springer-Verlag (New York, 1997), p. 24). This formula was found to be inaccurate for primers longer than 20 nucleotides. (Id.) Another simple estimate of the T_m value can be calculated by the equation: T_m=81.5+0.41(% G+C), when a nucleic acid is in aqueous solution at 1 M NaCl. (e.g., Anderson and Young, Quantitative Filter Hybridization, in Nucleic Acid Hybridization (1985). Other more sophisticated computations exist in the art which take structural as well as sequence characteristics into account for the calculation of T_m. A calculated T_m is merely an estimate; the optimum temperature is commonly determined empirically.

As used herein, the term “vector” is used in reference to nucleic acid molecules that transfer DNA segment(s) from one cell to another and capable of replication in a cell. Vectors may include plasmids, bacteriophages, viruses, cosmids, and the like.

The terms “recombinant vector” and “expression vector” as used herein refer to DNA or RNA sequences containing a desired coding sequence and appropriate DNA or RNA sequences necessary for the expression of the operably linked coding sequence in a particular host organism. Prokaryotic expression vectors include a promoter, a ribosome binding site, an origin of replication for autonomous replication in host cells and can also include other sequences, e.g., an optional operator sequence. A “promoter” is defined as a DNA sequence that directs RNA polymerase to bind to DNA and to initiate RNA synthesis. Eukaryotic expression vectors include a promoter, polyadenylation signal and optionally an enhancer sequence.

As used herein the term “coding region” when used in reference to structural gene refers to the nucleotide sequences which encode the amino acids found in the nascent polypeptide as a result of translation of a mRNA molecule. Typically, the coding region is bounded on the 5′ side by the nucleotide triplet ATG, which encodes the initiator methionine, and on the 3′ side by a stop codon (e.g., TAA, TAG, TGA). In some cases, the coding region is also known to initiate by a nucleotide triplet TTG.

The terms “buffer” or “buffering agents” refer to materials that when added to a solution, cause the solution to resist changes in pH.

The term “monovalent salt” refers to any salt in which the metal (e.g., Na, K, or Li) has a net 1+ charge in solution (i.e., one more proton than electron).

The term “divalent salt” refers to any salt in which a metal (e.g., Mg, Ca, or Sr) has a net 2+ charge in solution.

The term “solution” refers to an aqueous mixture.

The term “buffering solution” refers to a solution containing a buffering reagent.

The present invention relates to neurochemically active agents and combinations thereof. Neurochemically active agents include one or more antimicrobial peptide and/or a substance having an antimicrobial peptide effect. Antimicrobial peptides themselves are known to have trophic effects. As such, an antimicrobial peptide and/or a substance having an antimicrobial peptide effect can be used by itself in the methods of the invention. Neurochemically active agents also include one or more growth factor, neurotrophin, and neuropeptide. Combinations of neurochemically active agents are referred to herein as “trophic factor combinations.”

According to the invention, neurochemically active agents can be used alone or in combination to treat injuries to the nervous system, i.e., the central nervous system and the peripheral nervous system. The one or more neurochemically active agents can be used to treat nervous system injuries, including trauma induced injuries, degenerative induced injuries, age induced injuries, and infection induced injuries. Injuries that can be treated include, but are not limited to, spinal cord injury, including severed spinal cords; peripheral nerve damage, brain injuries, e.g., blood clots, tumors, strokes, and ischemis and perfusion; and Parkinson's disease, Alzheimer disease, muscular dystrophy, amyotrophic lateral sclerosis, multiple sclerosis, Pick's disease, prion diseases, Huntington disease, and related disorders.

When applied to a the nervous system, trophic factor combinations of the invention result in at least one of the following: lower loss in body weight after the injury when compared to controls not receiving the trophic factor combinations, strengthened motor recovery in injured animals treated with the trophic factor combination when compared to animals not treated with the trophic factor combination, larger evoked potentials in nerves when compared to controls not receiving the trophic factor combination, and a lower current required to evoke a response (threshold current) when compared to controls not receiving the trophic factor combination.

It is contemplated that the trophic factor combinations of the present invention used to treat injuries of the nervous system result in reduced inflammation, growth of new cells, increased plasticity, among other beneficial effects.

I. Trophic Factor Combinations

The present invention contemplates the use of trophic factor combinations and their individual components for treatment of injuries to the nervous system. Trophic factor combinations according to the invention can include one or more of the following elements: antimicrobial polypeptides (e.g., defensins), a substance having an effect of an antimicrobial peptide, a growth factor, a neurotrophin, and a neuropeptide. Additional components can also be included and are discussed below.

A. Antimicrobial Peptides

In some embodiments, one or more antimicrobial polypeptides and/or one or more substances having an antimicrobial peptide effect are used as a trophic factor to treat an injury to a nervous system. For additional information on antimicrobial peptides, see, for example, Antimicrobial Peptide Protocols, ed. W. M. Shafer, Humana Press, Totowa, N.J., 1997; and databases including http://aps.unmc.edu/AP/main.php (discussed in Wang Z, Wang G., APD: the Antimicrobial Peptide Database, Nucleic Acids Res. 2004 Jan. 1; 32(Database issue):D590-2), http://sdmc.lit.org.sg/Templar/DB/Antimic/, and http://www.bbcm.units.it/˜zelezetsky/hdpdb.html (database of defense peptides) and Table 1 below.

In some embodiments, the antimicrobial peptide is a compound or peptide selected from the following: bovine defensin peptide (BNP-1, Romeo et al., J. Biol. Chem. 263(15):9573-9575 [1988]), magainin (e.g., magainin I, magainin II, xenopsin, xenopsin precursor fragment, caerulein precursor fragment), magainin I and II analogs (PGLa, magainin A, magainin G, pexiganin, Z-12, pexigainin acetate, D35, MSI-78A, MG0 [K10E, K11E, F12W-magainin 2], MG2+ [K10E, F12W-magainin-2], MG4+ [F12W-magainin 2], MG6+ [f12W, E19Q-magainin 2 amide], MSI-238, reversed magainin II analogs [e.g., 53D, 87-ISM, and A87-ISM], Ala-magainin II amide, magainin II amide), cecropin P1, cecropin A, cecropin B, indolicidin, nisin, ranalexin, lactoferricin B, poly-L-lysine, cecropin A (1-8)-magainin II (1-12), cecropin A (1-8)-melittin (1-12), CA(1-13)-MA(1-13), CA(1-13)-ME(1-13), gramicidin, gramicidin A, gramicidin D, gramicidin S, alamethicin, protegrin, histatin, dermaseptin, lentivirus amphipathic peptide or analog, parasin I, lycotoxin I or II, globomycin, gramicidin S, surfactin, ralinomycin, valinomycin, polymyxin B, PM2 [(+/−) 1-(4-aminobutyl)-6-benzylindane], PM2c [(+/−)-6-benzyl-1-(3-carboxypropyl)indane], PM3 [(+/−) 1-benzyl-6-(4-aminobutyl)indane], tachyplesin, buforin I or II, misgurin, melittin, PR-39, PR-26, 9-phenylnonylamine, (KLAKKLA)n, (KLAKLAK)n, where n=1, 2, or 3, (KALKALK)3, KLGKKLG)n, and KAAKKAA)n, wherein N=1, 2, or 3, paradaxin, Bac 5, Bac 7, ceratoxin, mdelin 1 and 5, bombin-like peptides, PGQ, cathelicidin, HD-5, Oabac5alpha, ChBac5, SMAP-29, Bac7.5, lactoferrin, granulysin, thionin, hevein and knottin-like peptides, MPG1, 1bAMP, snakin, lipid transfer proteins, and plant defensins. Exemplary sequences for the above listed compounds are provided in Table 1. In some embodiments, the antimicrobial peptides or substances having an antimicrobial peptide effect (where they are peptides) are synthesized from L-amino acids, while in other embodiments, the peptides are synthesized from or comprise D-amino acids.

The compounds listed above can be isolated and purified from natural sources as appropriate. The compounds can also be produced recombinantly or synthetically, as described below.

In preferred embodiments, the trophic factor combinations of the present invention comprise one or more antimicrobial polypeptides and/or one or more substance having an antimicrobial peptide effect at a concentration of about 0.01 to about 1000 mg/L. In preferred embodiments, the trophic factor combinations comprise a solution comprising one or more antimicrobial polypeptides at a concentration of about 0.1 to about 5 mg/L.

In some embodiments of the present invention, the antimicrobial polypeptide is a defensin. In preferred embodiments, the trophic factor combinations of the present invention comprise one or more defensins. In further preferred embodiments, the trophic factor combination comprises a solution comprising purified defensins at a concentration of about 0.01 to 1000 mg/L. In particularly preferred embodiments, the trophic factor combinations comprise a solution comprising defensins at a concentration of about 0.1 to 5 mg/L. In still further preferred embodiments, the antimicrobial polypeptide is BNP1 (also known as bactanecin and bovine dodecapeptide). In certain embodiments, the defensin comprises the following consensus sequence:

X₁CN₁CRN₂CN₃ERN₄CN₅GN₆CCX₂, wherein N and X represent conservatively or nonconservatively substituted amino acids and N₁=1, N₂=3 or 4, N₃=3 or 4, N₄=1, 2, or 3, N₆=5-9, X₁ and X₂ may be present, absent, or equal from 1-2.

The present invention is not limited to any particular defensin. Indeed, trophic factor combinations comprising a variety of defensins are contemplated. Representative defensins are provided in Tables 1 and 2 below. In general, defensins are a family of highly cross-linked, structurally homologous antimicrobial peptides that can be found in the azurophil granules of polymorphonuclear leukocytes (PMNs) with homologous peptides being present in macrophages (e.g., Selsted et al., Infect. Immun. 45:150-154 [1984]). Originally described as “Lysosomal Cationic Peptides” in rabbit and guinea pig PMN (Zeya et al., Science 154:1049-1051 [1966]; Zeya et al., J. Exp. Med. 127:927-941 [1968]; Zeya et al., Lab. Invest. 24:229-236 [1971]; Selsted et al., [1984], supra.), this mixture was found to account for most of the microbicidal activity of the crude rabbit PMN extract against various microorganisms (Zeya et al., [1966], supra; Lehrer et al., J. Infect. Dis. 136:96-99 [1977]; Lehrer et al., Infect. Immun. 11:1226-1234 [1975]). Six rabbit neutrophil defensins have been individually purified and are designated NP-1, NP-2, NP-3A, NP-3B, NP-4, and NP-5. Their amino acid sequences were determined, and their broad spectra of activity were demonstrated against a number of bacteria (Selsted et al., Infect. Immun. 45:150-154 [1984]), viruses (Lehrer et al., J. Virol. 54:467 [1985]), and fungi (Selsted et al., Infect. Immun. 49:202-206 [1985]; Segal et al., 151:890-894 [1985]). Defensins have also been shown to possess mitogenic activity (e.g., Murphy et al., J. Cell. Physiol. 155:408-13 [1993]).

Four peptides of the defensin family have been isolated from human PMN's and are designated HNP-1, HNP-2, HNP-3, and HNP-4 (Ganz et al., J. Clin. Invest. 76:1427-1435 [1985]; Wilde et al., J. Biol. Chem. 264:11200-11203 [1989]). The amino acid sequences of HNP-1, HNP-2, and HNP-3 differ from each other only in their amino terminal residues, while each of the human defensins are identical to the six rabbit peptides in 10 or 11 of their 29 to 30 residues. These are the same 10 or 11 residues that are shared by all six rabbit peptides. Human defensin peptides have been shown to share with the rabbit defensins a broad spectrum of antimicrobial activity against bacteria, fungi, and enveloped viruses (Ganz et al., [1985], supra).

Three defensins designated RatNP-1, RatNP-2, and RatNP-4, have been isolated from rat (Eisenhauer et al., Infection and Immunity 57:2021-2027 [1989]). A guinea pig defensin (GPNP) has also been isolated, purified, sequenced and its broad spectrum antimicrobial properties verified (Selsted et al., Infect. Immun. 55:2281-2286 [1987]). Eight of its 31 residues were among those invariant in six rabbit and three human defensin peptides. The sequence of GPNP also included three nonconservative substitutions in positions otherwise invariant in the human and rabbit peptides. Of the defensins tested in a quantitative assay HNP-1, RatNP-1, and rabbit NP-1 possess the most potent antimicrobial properties, while NP-5 possesses the least amount of antimicrobial activity when tested against a panel of organisms in stationary growth phase (Selsted et al., Infect. Immun. 45:150-154 [1984]; Ganz et al., J. Clin. Invest. 76:1427-1435 [1985]). Defensin peptides are further described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777 (each of which is incorporated herein by reference).

Defensin peptides suitable for use alone in the methods and/or in trophic factor combinations of the present invention include natural defensin peptides isolated from known cellular sources, synthetic peptides produced by solid phase or recombinant DNA techniques, and defensin analogs which may be smaller peptides or other molecules having similar binding and biological activity as the natural defensin peptides (e.g., peptide mimetics). Methods for the purification of defensin peptides are described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777, the disclosures of which are incorporated herein by reference.

In preferred embodiments, suitable synthetic peptides will comprise all or part of the amino acid sequence of a known peptide, more preferably incorporating at least some of the conserved regions identified in Table 2. In particularly preferred embodiments, the synthetic peptides incorporate at least one of the conserved regions, more typically incorporating two of the conserved regions, preferably conserving at least three of the conserved regions, and more preferably conserving four or more of the conserved regions. In preferred embodiments, the synthetic peptides comprise fifty amino acids or fewer, although there may be advantages in increasing the size of the peptide above that of the natural peptides in certain instances. In certain embodiments, the peptides have a length in the range from about 10 to 50 amino acids, preferably being in the range from about 10 to 40 amino acids, and most preferably being in the range from about 30 to 35 amino acids which corresponds generally to the length of the natural defensin peptides.

In some cases, it may be desirable to incorporate one or more non-natural amino acids in the synthetic defensin peptides of the present invention. In preferred embodiments, non-natural amino acids comprise at least an N-terminus and a C-terminus of the peptide and have side chains that are either identical to or chemically modified or substituted from a natural amino acid counterpart. An example of a non-natural amino acid is an optical isomer of a naturally-occurring L-amino acid, such as a peptide containing all D-amino acids. Examples of the synthesis of peptides containing all D-amino acids include Merrifield et al., Ciba Found Symp. 186:5-26 (1994); Wade et al., Proc. Natl. Acad. Sci. USA 87(12):4761-5 (1990); and U.S. Pat. No. 5,792,831, which is herein incorporated by reference. Examples of chemical modifications or substitutions include hydroxylation or fluorination of C—H bonds within natural amino acids. Such techniques are used in the manufacture of drug analogs of biological compounds and are known to one of ordinary skill in the art.

Synthetic peptides having biological and binding activity the same or similar to that of natural defensin peptides can be produced by either of two exemplary approaches. First, the polypeptides can be produced by the well-known Merrifield solid-phase chemical synthesis method wherein amino acids are sequentially added to a growing chain (Merrifield, J. Am. Chem. Soc. 85:2149-2156 [1963]). Automatic peptide synthesis equipment is available from several commercial suppliers, including PE Biosystems, Inc., Foster City, Calif.; Beckman Instruments, Inc., Waldwick, N.J.; and Biosearch, Inc., San Raphael, Calif. Using such automatic synthesizers according to manufacturer's instructions, peptides can be produced in gram quantities for use in the present invention.

Second, the synthetic defensin peptides of the present invention can be synthesized by recombinant techniques involving the expression in cultured cells of recombinant DNA molecules encoding a gene for a desired portion of a natural or analog defensin molecule. The gene encoding the defensin peptide can itself be natural or synthetic. Conveniently, polynucleotides can be synthesized by well-known techniques based on the desired amino acid sequence. For example, short single-stranded DNA fragments can be prepared by the phosphoramidite method (Beaucage et al., Tetra. Lett. 22:1859-1862 [1981]). A double-stranded fragment can then be obtained either by synthesizing the complementary strand and annealing the strands together under appropriate conditions, or by adding the complementary strand using DNA polymerase under appropriate conditions, or by adding the complementary strand using DNA polymerase with an appropriate primer sequence. The natural or synthetic DNA fragments coding for the desired defensin peptide can then be incorporated in a suitable DNA construct capable of introduction to and expression in an in vitro cell culture. The DNA fragments can be portions or variants of wild-type nucleic acids encoding defensins. Suitable variants include those both with conservative and nonconservative amino acid substitutions.

The methods, compositions, and trophic factor combinations of the present invention can also employ synthetic non-peptide compositions that have biological activity functionally comparable to that of known defensin peptides. By functionally comparable, it is meant that the shape, size, flexibility, and electronic configuration of the non-peptide molecule is such that the biological activity of the molecule is similar to defensin peptides. In particular, the non-peptide molecules should display comparable mitogenic activity and/or antimicrobial activity or pore forming ability, preferably possessing both activities. Such non-peptide molecules will typically be small molecules having a molecular weight in the range from about 100 to about 1000 daltons. The use of such small molecules is frequently advantageous in the preparation of trophic factor combinations. Candidate mimetics can be screened in large numbers to identify those having the desired activity.

The identification of such nonpeptide analog molecules can be performed using techniques known in the art of drug design. Such techniques include, but are not limited to, self-consistent field (SCF) analysis, configuration interaction (CI) analysis, and normal mode dynamics computer analysis, all of which are well described in the scientific literature (e.g., Rein et al., Computer-Assisted Modeling of Receptor-Ligand Interactions, Alan Liss, N.Y., [1989]). Preparation of the identified compounds will depend on the desired characteristics of the compounds and will involve standard chemical synthetic techniques (e.g., Cary et al., Advanced Organic Chemistry, part B, Plenum Press, New York [1983]).

In some embodiments of the present invention, one or more substances having an effect that an antimicrobial peptide has can be used. Effects that antimicrobial peptides have include, but are not limited to, the following: form pores on the cell membrane; enter cells without membrane lysis and, once in the cytoplasm, bind to, and inhibit the activity of specific molecular targets essential to bacterial growth, thereby causing cell death; induce expression of syndecan, an integral membrane proteoglycan associated largely with epithelial cells, in mesenchymal cells and inhibit the NADPH oxidase activity of neutrophils, suggesting a role of this peptide in wound repair and inflammation; exert a protective effect in various animal models of ischemia-reperfusion injury, preventing the post-ischemic oxidant production; induce angiogenesis both in vitro and in vivo; inhibit membrane protein synthesis; inhibit DNA synthesis; antitumor effect; stimulate cell proliferation; interfere with signal pathways; chemoattractant for immune cells; stimulate cytokine expression; stimulate adhesion molecule expression; angiogenesis; and chloride secretion.

TABLE 1
Human Antimicrobial Peptides
	Organism
Protein Name	Name	Length	Sequence
Antibacterial		170	MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQV
peptide LL-37			LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR
precursor			PTMDGDPDTPKPVSFTVKETVCPRTTQQSP
			EDCDFKKDGLVKRCMGTVNLNQARGSFDIS
			CDKDNKRFALLGDFFRKSKEKIGKEFKRIVQR
			IKDFLRNLVPRTES
Antibacterial	Homo	170	MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQV
protein FALL-	sapiens		LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR
39 precursor			PTMDGDPDTPKPVSFTVKETVCPRTTQQSP
			EDCDFKKDGLVKRCMGTVTLNQARGSFDISC
			DKDNKRFALLGDFFRKSKEKIGKEFKRIVQRI
			KDFLRNLVPRTES
Antimicrobial	Homo	476	MQPVMLALWSLLLLWGLATPCQELLETVGTL
peptide RYA3	sapiens		ARIDKDELGKAIQNSLVGEPILQNVLGSVTAV
			NRGLLGSGGLLGGGGLLGHGGVFGVVEELS
			GLKIEELTLPKVLLKLLPGFGVQLSLHTKVGM
			HCSGPLGGLLQLAAEVNVTSRVALAVSSRGT
			PILILKRCSTLLGHISLFSGLLPTPLFGVVEQM
			LFKVLPGLLCPVVDSVLGVVNELLGAVLGLVS
			LGALGSVEFSLATLPLISNQYIELDINPIVKSVA
			GDIIDFPKSRAPAKVPPKKDHTSQVMVPLYLF
			NTTFGLLQTNGALDMDITPELVPSDVPLTTTD
			LAALLPEALGKLPLHQQLLLFLRVREAPTVTL
			HNKKALVSLPANIHVLFYVPKGTPESLFELNS
			VMTVRAQLAPSATKLHISLSLERLSVKVASSF
			THAFDGSRLEEWLSHVVGAVYAPKLNVALDV
			GIPLPKVLNINFSNSVLEIVENAVVLTVAS
Azurocidin	Homo	251	MTRLTVLALLAGLLASSRAGSSPLLDIVGGRK
precursor	sapiens		ARPRQFPFLASIQNQGRHFCGGALIHARFVM
			TAASCFQSQNPGVSTVVLGAYDLRRRERQS
			RQTFSISSMSENGYDPQQNLNDLMLLQLDRE
			ANLTSSVTILPLPLQNATVEAGTRCQVAGWG
			SQRSGGRLSRFPRFVNVTVTPEDQCRPNNV
			CTGVLTRRGGICNGDGGTPLVCEGLAHGVA
			SFSLGPCGRGPDFFTRVALFRDWIDGVLNNP
			GPGPA
Bactericidal	Homo	483	MARGPCNAPRWVSLMVLVAIGTAVTAAVNP
permeability-	sapiens		GVVVRISQKGLDYASQQGTAALQKELKRIKIP
increasing			DYSDSFKIKHLGKGHYSFYSMDIREFQLPSS
protein			QISMVPNVGLKFSISNANIKISGKWKAQKRFL
precursor (BPI)			KMSGNFDLSIEGMSISADLKLGSNPTSGKPTI
(CAP 57)			TCSSCSSHINSVHVHISKSKVGWLIQLFHKKIE
			SALRNKMNSQVCEKVTNSVSSKLQPYFQTLP
			VMTKIDSVAGINYGLVAPPATTAETLDVQMK
			GEFYSENHHNPPPFAPPVMEFPAAHDRMVY
			LGLSDYFFNTAGLVYQEAGVLKMTLRDDMIP
			KESKFRLTTKFFGTFLPEVAKKFPNMKIQIHV
			SASTPPHLSVQPTGLTFYPAVDVQAFAVLPN
			SSLASLFLIGMHTTGSMEVSAESNRLVGELKL
			DRLLLELKHSNIGPFPVELLQDIMNYIVPILVLP
			RVNEKLQKGFPLPTPARVQLYNVVLQPHQNF
			LLFGADVVYK
bactericidal/per-	Homo	487	MRENMARGPCNAPRWVSLMVLVAIGTAVTA
meability-	sapiens		AVNPGVVVRISQKGLDYASQQGTAALQKELK
increasing			RIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQL
protein			PSSQISMVPNVGLKFSISNANIKISGKWKAQK
precursor			RFLKMSGNFDLSIEGMSISADLKLGSNPTSGK
			PTITCSSCSSHINSVHVHISKSKVGWLIQLFHK
			KIESALRNKMNSQVCEKVTNSVSSKLQPYFQ
			TLPVMTKIDSVAGINYGLVAPPATTAETLDVQ
			MKGEFYSENHHNPPPFAPPVMEFPAAHDRM
			VYLGLSDYFFNTAGLVYQEAGVLKMTLRDDM
			IPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIH
			VSASTPPHLSVQPTGLTFYPAVDVQAFAVLP
			NSSLASLFLIGMHTTGSMEVSAESNRLVGEL
			KLDRLLLELKHSNIGPFPVELLQDIMNYIVPILV
			LPRVNEKLQKGFPLPTPARVQLYNVVLQPHQ
			NFLLFGADVVYK
beta defensin	Homo	111	MKSLLFTLAVFMLLAQLVSGNWYVKKCLNDV
126	sapiens		GICKKKCKPEEMHVKNGWAMCGKQRDCCV
preproprotein;			PADRRANYPVFCVQTKTTRISTVTATTATTTL
epididymal			MMTTASMSSMAPTPVSPTG
secretory
protein
ESP13.2; beta
defensin 26;
chromosome
20 open
reading frame
8
beta-defensin	Homo	65	MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT
	sapiens		CKNNCGKNEELIALCQKFLKCCRTIQPCGSII
			D
Beta-defensin	Homo	67	MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC
103 precursor	sapiens		RVRGGRCAVLSCLPKEEQIGKCSTRGRKCC
(Beta-defensin			RRKK
3) (DEFB-3)
(BD-3) (hBD-3)
(HBD3)
(Defensin like
protein)
Beta-defensin	Homo	72	MQRLVLLLAVSLLLYQDLPVRSEFELDRICGY
104 precursor	sapiens		GTARCRKKCRSQEYRIGRCPNTYACCLRKW
(Beta-defensin			DESLLNRTKP
4) (DEFB-4)
(BD-4) (hBD-4)
beta-defensin	Homo	77	MALIRKTFYFLFAMFFILVQLPSGCQAGLDFS
105	sapiens		QPFPSGEFAVCESCKLGRGKCRKECLENEK
			PDGNCRLNFLCCRQR
Beta-defensin	Homo	78	MALIRKTFYFLFAMFFILVQLPSGCQAGLDFS
105 precursor	sapiens		QPFPSGEFAVCESCKLGRGKCRKECLENEK
(Beta-defensin			PDGNCRLNFLCCRQRI
5) (DEFB-5)
(BD-5)
beta-defensin	Homo	57	MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT
106	sapiens		CKNNCGKNEELIALCQKSLKCCRTI
Beta-defensin	Homo	65	MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT
106 precursor	sapiens		CKNNCGKNEELIALCQKSLKCCRTIQPCGSII
(Beta-defensin			D
6) (DEFB-6)
(BD-6)
Beta-defensin	Homo	63	MKIFVFILAALILLAQIFQARTAIHRALISKRME
107 precursor	sapiens		GHCEAECLTFEVKIGGCRAELAPFCCKNR
(Beta-defensin
7) (DEFB-7)
(Fragment)
beta-defensin	Homo	59	MRIAVLFFTIFFFMSQVLPAKGKFKEICERPN
108	sapiens		GSCRDFCLETEIHVGRCLNSRPCCLPL
Beta-defensin	Homo	73	MRIAVLLFAIFFFMSQVLPARGKFKEICERPN
108 precursor	sapiens		GSCRDFCLETEIHVGRCLNSQPCCLPLGHQP
(Beta-defensin			RIESTTPKKD
8) (DEFB-8)
Beta-defensin	Homo	123	MKLLLLALPMLVLLPQVIPAYSGEKKCWNRS
118 precursor	sapiens		GHCRKQCKDGEAVKDTCKNLRACCIPSNED
(Beta-defensin			HRRVPATSPTPLSDSTPGIIDDILTVRFTTDYF
18) (DEFB-18)			EVSSKKDMVEESEAGRGTETSLPNVHHSS
(Epididymal
secretory
protein 13.6)
(ESP13.6)
Beta-defensin	Homo	84	MKLLYLFLAILLAIEEPXISGKRHILRCMGNSGI
119 precursor	sapiens		CRASCKKNEQPYLYCRNCQSCCLQSYMRISI
(Beta-defensin			SGKEENTDWSYEKQWPRLP
19) (DEFB-19)
Beta-defensin	Homo	88	MKLLYLFLAILLAIEEPVISVECWMDGHCRLLC
120 precursor	sapiens		KDGEDSIIRCRNRKRCCVPSRYLTIQPVTIHGI
(Beta-defensin			LGWTTPQMSTTAPKMKTNITNR
20) (DEFB-20)
Beta-defensin	Homo	67	MKLLLLTLTVLLLLSQLTPGGTQRCWNLYGK
123 precursor	sapiens		CRYRCSKKERVYVYCINNKMCCVKPKYQPK
(Beta-defensin			ERWWPF
23) (DEFB-23)
Beta-defensin	Homo	43	EFKRCWKGQGACQTYCTRQETYMHLCPDA
124 (Beta-	sapiens		SLCCLSYALKPPPV
defensin 24)
(DEFB-24)
(Fragment)
Beta-defensin	Homo	152	MLTFIICGLLTRVTKGSFEPQKCWKNNVGHC
125 precursor	sapiens		RRRCLDTERYILLCRNKLSCCISIISHEYTRRP
(Beta-defensin			AFPVIHLEDITLDYSDVDSFTGSPVSMLNDLIT
25) (DEFB-25)			FDTTKFGETMTPETNTPETTMPPSEATTPET
			TMPPSETATSETMPPPSQTALTHN
Beta-defensin	Homo	111	MKFLLFTLAVFMLLAQLVSGNWYVKKCLNDV
126 precursor	sapiens		GICKKKCKPEEMHVKNGWAMCGKQRDCCV
(Beta-defensin			PADRRANYPVFCVQTKTTRISTVTATTATTTL
26) (DEFB-26)			MMTTASMSSMAPTPVSPTG
(Epididymal
secretory
protein 13.2)
(ESP13.2)
Beta-defensin	Homo	99	MGLFMIIAILLFQKPTVTEQLKKCWNNYVQGH
127 precursor	sapiens		CRKICRVNEVPEALCENGRYCCLNIKELEACK
(Beta-defensin			KITKPPRPKPATLALTLQDYVTIIENFPSLKTQ
27) (DEFB-27)			ST
Beta-defensin	Homo	183	MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLG
129 precursor	sapiens		RCRDHCNVDEKEIQKCKMKKCCVGPKVVKLI
(Beta-defensin			KNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQ
29) (DEFB-29)			RKHILSVLPQIKSTSFFANTNFVIIPNATPMNS
			ATISTMTPGQITYTATSTKSNTKESRDSATAS
			PPPAPPPPNILPTPSLELEEAEEQ
Beta-defensin	Homo	70	MRVLFFVFGVLSLMFTVPPGRSFISNDECPS
131 precursor	sapiens		EYYHCRLKCNADEHAIRYCADFSICCKLKIIEI
(Beta-defensin			DGQKKW
31) (DEFB-31)
Beta-Defensin	Homo	37	PVTCLKSGAICHPVFCPRRYKQIGTCGLPGT
2	sapiens		KCCKKP
Beta-defensin	Homo	64	MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCL
2 precursor	sapiens		KSGAICHPVFCPRRYKQIGTCGLPGTKCCKK
(BD-2) (hBD-2)			P
(Skin-
antimicrobial
peptide 1)
(SAP1)
beta-defensin	Homo	156	MNILMLTFIICGLLTRVTKGSFEPQKCWKNNV
25 precursor	sapiens		GHCRRRCLDTERYILLCRNKLSCCISIISHEYT
			RRPAFPVIHLEDITLDYSDVDSFTGSPVSMLN
			DLITFDTTKFGETMTPETNTPETTMPPSEATT
			PETTMPPSETATSETMPPPSQTALTHN
beta-defensin	Homo	93	MKLFLVLIILLFEVLTDGARLKKCFNKVTGYCR
28 precursor	sapiens		KKCKVGERYEIGCLSGKLCCANDEEEKKHVS
			FKKPHQHSGEKLSVLQDYIILPTITIFTV
Beta-Defensin	Homo	45	GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGK
3	sapiens		CSTRGRKCCRRKK
beta-defensin	Homo	95	MKFLLLVLAALGFLTQVIPASAGGSKCVSNTP
32 precursor	sapiens		GYCRTCCHWGETALFMCNASRKCCISYSFL
			PKPDLPQLIGNHWQSRRRNTQRKDKKQQTT
			VTS
Beta-defensin-	Homo	47	GNFLTGLGHRSDHYNCISSGGQCLYSACPIF
1 (Fragment)	sapiens		TKIQGTCYRGKAKCCK
Beta-Defensin-	Homo	41	GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGL
2	sapiens		PGTKCCKKP
Beta-defensin-	Homo	67	MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC
3	sapiens		RVRGGRCAVLSRLPKEEQIGKCSTRGRKCC
			RRKK
Calgranulin A	Homo	93	MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDD
(Migration	sapiens		LKKLLETECPQYIRKKGADVWFKELDINTDGA
inhibitory			VNFQEFLILVIKMGVAAHKKSHEESHKE
factor-related
protein 8)
(MRP-8)
(Cystic fibrosis
antigen)
(CFAG) (P8)
(Leukocyte L1
complex light
chain) (S100
calcium-binding
protein A8)
(Calprotectin
L1L subun
Calgranulin B	Homo	114	MTCKMSQLERNIETIINTFHQYSVKLGHPDTL
(Migration	sapiens		NQGEFKELVRKDLQNFLKKENKNEKVIEHIME
inhibitory			DLDTNADKQLSFEEFIMLMARLTWASHEKMH
factor-related			EGDEGPGHHHKPGLGEGTP
protein 14)
(MRP-14)
(P14)
(Leukocyte L1
complex heavy
chain) (S100
calcium-
binding protein
A9)
(Calprotectin
L1H subunit)
Calgranulin C	Homo	92	MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGE
(CAGC)	sapiens		LKQLLTKELANTIKNIKDKAVIDEIFQGLDANQ
(CGRP)			DEQVDFQEFISLVAIALKAAHYHTHKE
(Neutrophil
S100 protein)
(Calcium-
binding protein
in amniotic fluid
1) (CAAF1)
(p6) [Contains:
Calcitermin]
cathelicidin	Homo	170	MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQV
antimicrobial	sapiens		LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR
peptide			PTMDGDPDTPKPVSFTVKETVCPRTTQQSP
			EDCDFKKDGLVKRCMGTVTLNQARGSFDISC
			DKDNKRFALLGDFFRKSKEKIGKEFKRIVQRI
			KDFLRNLVPRTES
Cathepsin G	Homo	255	MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSR
precursor (EC	sapiens		PYMAYLQIQSPAGQSRCGGFLVREDFVLTAA
3.4.21.20) (CG)			HCWGSNINVTLGAHNIQRRENTQQHITARRAI
			RHPQYNQRTIQNDIMLLQLSRRVRRNRNVNP
			VALPRAQEGLRPGTLCTVAGWGRVSMRRGT
			DTLREVQLRVQRDRQCLRIFGSYDPRRQICV
			GDRRERKAAFKGDSGGPLLCNNVAHGIVSY
			GKSSGVPPEVFTRVSSFLPWIRTTMRSFKLL
			DQMETPL
chromogranin	Homo	457	MRSAAVLALLLCAGQVTALPVNSPMNKGDTE
A; parathyroid	sapiens		VMKCIVEVISDTLSKPSPMPVSQECFETLRGD
secretory			ERILSILRHQNLLKELQDLALQGAKERAHQQK
protein 1			KHSGFEDELSEVLENQSSQAELKEAVEEPSS
			KDVMEKREDSKEAEKSGEATDGARPQALPE
			PMQESKAEGNNQAPGEEEEEEEEATNTHPP
			ASLPSQKYPGPQAEGDSEGLSQGLVDREKG
			LSAEPGWQAKREEEEEEEEEAEAGEEAVPE
			EEGPTVVLNPHPSLGYKEIRKGESRSEALAV
			DGAGKPGAEEAQDPEGKGEQEHSQQKEEE
			EEMAVVPQGLFRGGKSGELEQEEERLSKEW
			EDSKRWSKMDQLAKELTAEKRLEGQEEEED
			NRDSSMKLSFRARAYGFRGPGPQLRRGWR
			PSSREDSLEAGLPLQVRGYPEEKKEEEGSAN
			RRPEDQELESLSAIEAELEKVAHQLQALRRG
Defensin 5	Homo	94	MRTIAILAAILLVALQAQAESLQERADEATTQK
precursor	sapiens		QSGEDNQDLAISFAGNGLSALRTSGSQARAT
(Defensin,			CYCRTGRCATRESLSGVCEISGRLYRLCCR
alpha 5)
Defensin 6	Homo	101	MRTLTILTAVLLVALQAKAEPLQAEDDPLQAK
	sapiens		AYEADAQEQRGANDQDFAVSFAEDASSSLR
			ALGGSTRAFTCHCRRSCYSTEYSYGTCTVM
			GINHRFCCL
Defensin 6	Homo	100	MRTLTILTAVLLVALQAKAEPLQAEDDPLQAK
precursor	sapiens		AYEADAQEQRGANDQDFAVSFAEDASSSLR
(Defensin,			ALGSTRAFTCHCRRSCYSTEYSYGTCTVMGI
alpha 6)			NHRFCCL
defensin alpha-	Homo	65	CCSPGADCSGHPRSGCFPCMGRKLGSKAS
3 precursor	sapiens		RLKEKHGLLLQNTSVHCRRTSLWNLHLPGKT
(mistranslated)			LGILL
defensin beta	Homo	60	MKIFFFILAALILLAQIFQARTAIHRALISKRME
107	sapiens		GHCEAECLTFEVKIGGCRAELAPFCC
defensin beta	Homo	52	GKFKEICERPNGSCRDFCLETEIHVGRCLNS
108	sapiens		QPCCLPLGHQPRIESTTPKKD
Defensin beta	Homo	21	SCTAIGGRCKNQCDDSEFRIS
112 (Fragment)	sapiens
Defensin beta	Homo	39	KRYGRCKRDCLESEKQIDICSLPGKICCTEKL
114 (Fragment)	sapiens		YEEDDMF
defensin beta	Homo	101	GEKKCWNRSGXCRKQCKDGEAVKDTCKNX
118	sapiens		RACCIPSNEDHRRVPATSPTPLSDSTPGIIDDI
			LTVRFTTDYFEVSSKKDMVEESEAGRGTETS
			LPNVHHSS
defensin beta	Homo	94	SLLFTLAVFMLLAQLVSGNWYVKKCLNDVGI
126	sapiens		CKKKCKPEEMHVKNGWAMCGKQRDCCVPA
			DRRANYPVFCVQTKTTRISTVTATTATTTLMM
			TT
defensin beta	Homo	59	EQLKKCWNNYVQRHCRKICRVNEVPEALCE
127	sapiens		NGRYCCLNIKELEACKKITKPPSPKQHLH
defensin beta	Homo	155	MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLG
129	sapiens		RCRDHCNVDEKEIQKCKMKKCCVGPKVVKLI
			KNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQ
			RKHILSVLPQIKSTSFFANTNFVIIPNATPMNS
			ATISTMTPGQITYTATSTKSNTKESRDS
defensin beta-1	Homo	36	DHYNCVSSGGQCLYSACPIFTKIQGTCYRGK
	sapiens		AKCCK
Defensin HNP-	Homo	30	DCYCRIPACIAGERRYGTCIYQGRLWAFCC
3 - Chain B	sapiens
EP2E	Homo	80	MKVFFLFAVLFCLVQTNSGDVPPGIRNTICRM
	sapiens		QQGICRLFFCHSGEKKRDICSDPWNRCCVS
			NTDEEGKEKPEMDGRSGI
gene TAP1	Homo	33	GYDTEVGEAGSQLSGGQRQAVALARALIRKP
protein	sapiens		CV
Hepcidin	Homo	84	MALSSQIWAACLLLLLLLASLTSGSVFPQQTG
precursor	sapiens		QLAELQPQDRAGARASWMPMFQRRRRRDT
(Liver-			HFPICIFCCGCCHRSKCGMCCKT
expressed
antimicrobial
peptide)
(LEAP-1)
(Putative liver
tumor
regressor)
(PLTR)
[Contains:
Hepcidin 25
(Hepc25);
Hepcidin 20
(Hepc20)]
High mobility	Homo	215	MGKGDPKKPRGKMSSYAFFVQTCREEHKKK
group protein 1	sapiens		HPDASVNFSEFSKKCSERWKTMSAKEKGKF
(HMG-1)			EDMAKADKARYEREMKTYIPPKGETKKKFKD
			PNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIG
			DVAKKLGEMWNNTAADDKQPYEKKAAKLKE
			KYEKDIAAYRAKGKPDAAKKGVVKAEKSKKK
			KEEEEDEEDEEDEEEEEDEEDEDEEEDDDD
			E
liver-expressed	Homo	81	MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAK
antimicrobial	sapiens		RRPRRMTPFWRGVSLRPIGASCRDDSECITR
peptide 2			LCRKGQQSPPTMLRSMEY
isoform
Liver-	Homo	77	MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAK
expressed	sapiens		RRPRRMTPFWRGVSLRPIGASCRDDSECITR
antimicrobial			LCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Lysozyme C	Homo	148	MKALIVLGLVLLSVTVQGKVFERCELARTLKR
precursor (EC	sapiens		LGMDGYRGISLANWMCLAKWESGYNTRATN
3.2.1.17) (1,4-			YNAGDRSTDYGIFQINSRYWCNDGKTPGAV
beta-N-			NACHLSCSALLQDNIADAVACAKRVVRDPQG
acetylmurami-			IRAWVAWRNRCQNRDVRQYVQGCGV
dase C)
Neutrophil	Homo	94	MRTLAILAAILLVALQAQAEPLQARADEVAAA
defensin 1	sapiens		PEQIAADIPEVVVSLAWDESLAPKHPGSRKN
precursor			MACYCRIPACIAGERRYGTCIYQGRLWAFCC
(HNP-1) (HP-1)
(HP1)
(Defensin,
alpha 1)
[Contains: HP
1-56;
Neutrophil
defensin 2
(HNP-2) (HP-2)
(HP2)]
Neutrophil	Homo	94	MRTLAILAAILLVALQAQAEPLQARADEVAAA
defensin 3	sapiens		PEQIAADIPEVVVSLAWDESLAPKHPGSRKN
precursor			MDCYCRIPACIAGERRYGTCIYQGRLWAFCC
(HNP-3) (HP-3)
(HP3)
(Defensin,
alpha 3)
[Contains: HP
3-56;
Neutrophil
defensin 2
(HNP-2) (HP-2)
(HP2)]
Neutrophil	Homo	97	MRIIALLAAILLVALQVRAGPLQARGDEAPGQ
defensin 4	sapiens		EQRGPEDQDISISFAWDKSSALQVSGSTRG
precursor			MVCSCRLVFCRRTELRVGNCLIGGVSFTYCC
(HNP-4) (HP-4)			TRVD
(Defensin,
alpha 4)
Retrocyclin	Homo	56	MPCFSWWPCRLRRSHFRQELMKLQPRSSLE
	sapiens		QMIRKWLMPLHGMKVPLFRFQTQREA
Ribonuclease 7	Homo	156	MAPARAGFCPLLLLLLLGLWVAEIPVSAKPKG
precursor (EC	sapiens		MTSSQWFKIQHMQPSPQACNSAMKNINKHT
3.1.27.-)			KRCKDLNTFLHEPFSSVAATCQTPKIACKNG
(RNase 7)			DKNCHQSHGPVSLTMCKLTSGKYPNCRYKE
(Skin-derived			KRQNKSYVVACKPPQKKDSQQFHLVPVHLD
antimicrobial			RVL
protein 2)
(SAP-2)
Salivary gland	Homo	46	MHDFWVLWVLLEYIYNSACSVLSATSSVSSR
antimicrobial	sapiens		VLNRSLQVKVVKITN
salvic
Secretogranin I	Homo	677	MQPTLLLSLLGAVGLAAVNSMPVDNRNHNE
precursor (SgI)	sapiens		GMVTRCIIEVLSNALSKSSAPPITPECRQVLKT
(Chromogranin			SRKDVKDKETTENENTKFEVRLLRDPADASE
B) (CgB)			AHESSSRGEAGAPGEEDIQGPTKADTEKWA
[Contains:			EGGGHSRERADEPQWSLYPSDSQVSEEVKT
GAWK peptide;			RHSEKSQREDEEEEEGENYQKGERGEDSSE
CCB peptide]			EKHLEEPGETQNAFLNERKQASAIKKEELVA
			RSETHAAGHSQEKTHSREKSSQESGEEAGS
			QENHPQESKGQPRSQEESEEGEEDATSEVD
			KRRTRPRHHHGRSRPDRSSQGGSLPSEEKG
			HPQEESEESNVSMASLGEKRDHHSTHYRAS
			EEEPEYGEEIKGYPGVQAPEDLEWERYRGR
			GSEEYRAPRPQSEESWDEEDKRNYPSLELD
			KMAHGYGEESEEERGLEPGKGRHHRGRGG
			EPRAYFMSDTREEKRFLGEGHHRVQENQMD
			KARRHPQGAWKELDRNYLNYGEEGAPGKW
			QQQGDLQDTKENREEARFQDKQYSSHHTAE
			KRKRLGELFNPYYDPLQWKSSHFERRDNMN
			DNFLEGEEENELTLNEKNFFPEYNYDWWEK
			KPFSEDVNWGYEKRNLARVPKLDLKRQYDR
			VAQLDQLLHYRKKSAEFPDFYDSEEPVSTHQ
			EAENEKDRADQTVLTEDEKKELENLAAMDLE
			LQKIAEKFSQRG
Similar to	Homo	226	AEGKWGLAHGRAEAHVWPGQGGWRLGPP
azurocidin 1	sapiens		QGRWTGSSPLLDIVGGRKARPRQFPFLASIQ
(Cationic			NQGRHFCGGALIHARFVMTAASCFQSQNPG
antimicrobial			VSTVVLGAYDLRRRERQSRQTFSISSMSENG
protein 37)			YDPQQNLNDLMLLQLDREANLTSSVTILPLPL
(Fragment)			QNATVEAGTRCQVAGWGSQRSGGRLSRFP
			RFVNVTVTPEDQCRPNNVCTGVLTRRGGICN
			VSAPCGGRRGPERY

Nonhuman Animal
Antimicrobial Peptides
	Organism
Protein Name	Name	Length	Sequence
11.5 kDa	Carcinus	84	NKDCKYWCKDNLGLNYCCGQPGVTYPPFTK
antibacterial	maenas		KHLGRCPAVRDTCTGVRTQLPTYCPHDGAC
protein			QFRSKCCYDTCLKHHVCKTAEYPY
27 kDa	Cyprinus	19	GIGGKPVQTAFVDNDGIYD
antibacterial	carpio
protein
(Fragment)
4 kDa defensin	Androctonus	37	GFGCPFNQGACHRHCRSIRRRGGYCAGLFK
	australis		QTCTCYR
4 kDa defensin	Leiurus	38	GFGCPLNQGACHRHCRSIRRRGGYCAGFFK
(Antibacterial 4	quinquestriatus		QTCTCYRN
kDa peptide)
7.5 kDa	Ovis aries	164	METQMASPSLGRCSLWLLLLGLLLPSASAQA
bactinecin			LSYREAVLRAVGQLNEKSSEVNLYRLLELDP
(Fragment)			PPKDAEDQGARKPVSFRVKETVCPRTSQQP
			PEQCDFKENGLVKQCVGTVSLDTSNDEFDL
			NCNELQSVRRLRPRRPRLPRPRPRPRPRPR
			SLPLPRPQPRRI
Abaecin	Bombus	39	FVPYNPPRPGQSKPFPSFPGHGPFNPKIQW
	pascuorum		PYPLPNPGH
Abaecin	Apis mellifera	53	MKVVIFIFALLATICAAFAYVPLPNVPQPGRRP
precursor			FPTFPGQGPFNPKIKWPQGY
Acaloleptin A1	Acalolepta	71	SLQPGAPNVNNKDQPWQVSPHISRDDSGNT
	luxuriosa		RTDINVQRHGENNDFEAGWSKVVRGPNKAK
			PTWHIGGTHRW
Achacin	Achatina	531	MLLLNSALFILCLVCWLPGTSSSRVLTRREGP
precursor	fulica		QCSRSVDVAVVGAGPSGTYSAYKLRNKGQT
			VELFEYSNRIGGRLFTTHLPNVPDLNLESGG
			MRYFKNHHKIFGVLVKELNLSNKEFTEGFGK
			PGRTRFFARGKSLTLEEMTSGDVPYNLSTEE
			KANQANLAGYYLKKLTGFDGEVLTIPQANKLE
			VDDGRKLYQLTVDEALDKVGTPEGKEFLKAF
			STGNTEFIEGVSAVNYFLVELGEREEEILTLTD
			GMSALPQALADAFLKSSTSHALTLNRKLQSL
			SKTDNGLYLLEFLETNTHEGYTEESNITDLVC
			ARKVILAIPQSALIHLDWKPLRSETVNEAFNAV
			KFIPTSKVFLTFPTAWWLSDAVKNPAFVVKST
			SPFNQMYDWKSSNVTGDAAMIASYADTSDT
			KFQENLNSKGELIPGSAPGANRVTVALKEELL
			SQLSQAYGIERSDIPEPKSGTSQFWSSYPFE
			GDWTVWKAGYHCEYTQYIIERPSLIDDVFVV
			GSDHVNCIENAWTESAFLSVENVFEKYF
Acyl-CoA-	Sus scrofa	87	MSQAEFEKAAEEVKNLKTKPADDEMLFIYSH
binding protein			YKQATVGDINTERPGILDLKGKAKWDAWNGL
(ACBP)			KGTSKEDAMKAYINKVEELKKKYGI
(Diazepam
binding
inhibitor) (DBI)
(Endozepine)
(EP) [Contains:
DBI(32-86)]
Adenoregulin	Phyllomedusa	81	MAFLKKSLFLVLFLGLVSLSICEEEKRENEDE
precursor	bicolor		EEQEDDEQSEMKRGLWSKIKEVGKEAAKAA
(Dermaseptin			AKAAGKAALGAVSEAVGEQ
BII)
(Dermaseptin
B2)
Alpha-defensin	Macaca	96	MRTLAILAAILLVALQAQAEPLQARTDEATAA
1	mulatta		QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
			KNMACYCRIPACLAGERRYGTCFYMGRVWA
			FCC
Alpha-defensin	Macaca	96	MRTLAILAAILLVALQAQAEPLQARTDEATAA
1A	mulatta		QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
			KNMACYCRIPACLAGERRYGTCFYLGRVWA
			FCC
Alpha-defensin	Macaca	94	MRTLAILAAILLFALLAQAKSLQETADDAATQE
2	mulatta		QPGEDDQDLAVSFEENGLSTLRASGSQARR
			TCRCRFGRCFRRESYSGSCNINGRIFSLCCR
Alpha-S2	Bos taurus	222	MKFFIFTCLLAVALAKNTMEHVSSSEESIISQE
casein			TYKQEKNMAINPSKENLCSTFCKEVVRNANE
precursor			EEYSIGSSSEESAEVATEEVKITVDDKHYQKA
[Contains:			LNEINQFYQKFPQYLQYLYQGPIVLNPWDQV
Casocidin-I]			KRNAVPITPTLNREQLSTSEENSKKTVDMES
			TEVFTKKTKLTEEEKNRLNFLKKISQRYQKFA
			LPQYLKTVYQHQKAMKPWIQPKTKVIPYVRY
			L
Androctonin	Androctonus	25	RSVCRQIKICRRRGGCYYKCTNRPY
	australis
Andropin	Drosophila	57	MKYFVVLVVLALILAITVGPSDAVFIDILDKME
precursor	mauritiana		NAIHKAAQAGIGIAKPIEKMILPK
Andropin	Drosophila	57	MKYFVVLVVLALILAISVGPSDAVFIDILDKVEN
precursor	melanogaster		AIHNAAQVGIGFAKPFEKLINPK
Andropin	Drosophila	67	MKYFLVLVVLTLILAISVGQSDALFVDIIDNVEN
precursor	orena		AIHKAAKTGIGMVKPIENIFIPNQQKKSTEASN
Andropin	Drosophila	57	MKYFVVLVVLALILAITVDPSDAVFIDILDKMEN
precursor	sechellia		AIHKAAQAGIGLAKPIENMILPK
Andropin	Drosophila	60	MKYFVVLVVALILAIAVGPSDAVFIDILDKME
precursor	simulans		NAIHKAAQAGIGIAKPIENMILPKLTK
Andropin	Drosophila	62	MKYFSVLVVLTLILAIVDQSDAFINLLDKVEDA
precursor	teissieri		LHTGAQAGFKLIRPVERGATPKKSEKPEK
Andropin	Drosophila	60	MKYFSVLVVLTLILAISVGQSNAIFVDVLDNVE
precursor	yakuba		TALHNAAKAGFKLIKPIEKMIMPSKEK
Anionic	Bombina	144	MNFKYIFAVSFLIASAYARSVQNDEQSLSQRD
antimicrobial	maxima		VLEEESLREIRGIGGKILSGLKTALKGAAKELA
peptide			STYLHRKRTAEEHEEMKRLEAVMRDLDSLDY
			PEEASERETRGFNQDEIANLFTKKEKRILGPV
			LGLVSDTLDDVLGILG
Antibacterial	Carcinus	30	XXVPYPRPFPRPPIGPRPLPFPGGGRPFQS
6.5 kDa protein	maenas
(Fragment)
Antibacterial	Bos taurus	158	METQRASLSLGRWSLWLLLLGLALPSASAQA
peptide BMAP-			LSYREAVLRAVDQFNERSSEANLYRLLELDP
27 precursor			PPKEDDENPNIPKPVSFRVKETVCPRTSQQP
(Myeloid			AEQCDFKENGLVKQCVGTVTLDAVKGKINVT
antibacterial			CEELQSVGRFKRFRKKFKKLFKKLSPVIPLLH
peptide 27)			LG
Antibacterial	Bos taurus	159	METQRASLSLGRWSLWLLLLGLALPSASAQA
peptide BMAP-			LSYREAVLRAVDQLNEKSSEANLYRLLELDP
28 precursor			PPKEDDENPNIPKPVSFRVKETVCPRTSQQS
(Myeloid			PEQCDFKENGLLKECVGTVTLDQVGSNFDIT
antibacterial			CAVPQSVGGLRSLGRKILRAWKKYGPIIVPIIR
peptide 28)			IG
Antibacterial	Bos taurus	165	METQRASFSLGRSSLWLLLLGLVVPSASAQD
peptide BMAP-			LSYREAVLRAVDQFNERSSEANLYRLLELDP
34 precursor			PPEQDVEHPGARKPVSFTVKETVCPRTTPQP
			PEQCDFKENGLVKQCVGTVTRYWIRGDFDIT
			CNNIQSAGLFRRLRDSIRRGQQKILEKARRIG
			ERIKDIFRG
Antibacterial	Bombyx mori	59	MNFTRIIFFLFVVVFATASGKPWNIFKEIERAV
peptide			ARTRDAVISAGPAVRTVAAATSVASG
enbocin
precursor
(Moricin)
Antibacterial	Sus scrofa	153	METQRASLCLGRWSLWLLLLGLVVPSASAQ
peptide PMAP-			ALSYREAVLRAVDRLNEQSSEANLYRLLELD
23 precursor			QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
(Myeloid			PELCDFKENGRVKQCVGTVTLKEIRGNFDITC
antibacterial			NQLQSVRIIDLLWRVRRPQKPKFVTVWVR
peptide 23)
Antibacterial	Sus scrofa	166	METQRASLCLGRWSLWLLLLGLVVPSASAQ
peptide PMAP-			ALSYREAVLRAVDRLNEQSSEANLYRLLELD
36 precursor			QPPKADEDPGTPKPVSFTVKETVCPRPTWR
(Myeloid			PPELCDFKENGRVKQCVGTVTLNPSNDPLDI
antibacterial			NCDEIQSVGRFRRLRKKTRKRLKKIGKVLKWI
peptide 36)			PPIVGSIPLGCG
Antibacterial	Sus scrofa	167	METQRASLCLGRWSLWLLLLALVVPSASAQA
peptide PMAP-			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
37 precursor			PPKADEDPGTPKPVSFTVKETVCPRPTWRP
(Myeloid			PELCDFKENGRVKQCVGTVTLDQIKDPLDITC
antibacterial			NEIQSVGLLSRLRDFLSDRGRRLGEKIERIGQ
peptide 37)			KIKDLSEFFQS
Antibacterial	Carcinus	88	GLFPNKDCKYWCKDNLGLNYCCGQPGVTYP
protein 11.5	maenas		PFTKKHLGRCPAVRDTCTGVRTQLPTYCPHD
kDa			GACQFRSKCCYDTCLKHHVCKTAEYPY
(Fragment)
Antibacterial	Sus scrofa	172	METQRASLCLGRWSLWLLLLGLVVPSASAQ
protein PR-39			ALSYREAVLRAVDRLNEQSSEANLYRLLELD
precursor			QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
			PELCDFKENGRVKQCVGTVTLNPSIHSLDISC
			NEIQSVRRRPRPPYLPRPRPPPFFPPRLPPRI
			PPGFPPRFPPRFPGKR
antibacterial	Sus scrofa	172	METQRASLCLGRWSLWLLLLALVVPSASAQA
protein			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
precursor			PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
			ELCDFKENGRVKQCVGTVTLNPSIHSLDISCN
			EIQSVRRRPRPPYLPRPRPPPFFPPRLPPRIP
			PGFPPRFPPRFPGKR
antibacterial	Cavia	42	GLRKKFRKTRKRIQKLGRKIGKTGRKVXKAW
protein, 11 K	porcellus		REYGQIPYPCR
Antifungal	Galleria	76	MKIAFIVAISLAFLAVTSCIEFEKSTESHDIQKR
peptide	mellonella		GVTITVKPPFPGCVFYECIANCRSRGYKNGG
gallerimycin			YCTINGCQCLR
Antifungal	Sarcophaga	85	MVKLFVIVILALIAVAFGQHGHGGQDQHGYG
protein	peregrina		HGQQAVYGKGHEGHGVNNLGQDGHGQHG
precursor			YAHGHSDQHGHGGQHGQHDGYKNRGY
(AFP)
Antimicrobial	Xenopus	66	LKCVNLQANGIKMTQECAKEDTKCLTLRSLK
amphipathic	laevis		KTLKFCASGRTCTTMKIMSLPGEQITCCEGN
helix-forming			MCNA
peptide
Antimicrobial	Acrocinus	34	CIKNGNGCQPDGSQGNCCSRYCHKEPGWV
peptide ALO1	longimanus		AGYCR
Antimicrobial	Acrocinus	34	CIANRNGCQPDGSQGNCCSGYCHKEPGWV
peptide ALO2	longimanus		AGYCR
Antimicrobial	Acrocinus	36	CIKNGNGCQPNGSQGNCCSGYCHKQPGWV
peptide ALO3	longimanus		AGYCRRK
Antimicrobial	Glossina	208	MQSFKICFFISCLSVVLVKGQFGGTVSSNPN
peptide attacin	morsitans		GGLDVNARLSKTIGDPNANVVGGVFAAGNTD
AttA			GGPATRGAFLAANKDGHGLSLQHSKTDNFG
			SSLTSSAHAHLFNDKTHKLDANAFHSRTHLD
			NGFKFDRVGGGLRYDHVTGHGASLTASRIP
			QLDMNTLGLTGKANLWSSPNRATTLDLTGG
			VSKHFGGPFDGQTNKQIGLGLNSRF
Antimicrobial	Manduca	67	MKFSRVLFFVFACFAAFTVTAAKPWDFLKEL
peptide	sexta		EGAGQRIRDAIISAQPAVETIAQATAIFKGQSK
cecropin 6			EED
Antimicrobial	Gallus gallus	39	GRKSDCFRKSGFCAFLKCPSLTLISGKCSRF
peptide CHP1			YLCCKRIR
(Chicken
heterophil
peptide 1)
Antimicrobial	Gallus gallus	34	GRKSDCFRKNGFCAFLKCPYLTLISGLCSXF
peptide CHP2			HLC
(Chicken
heterophil
peptide 2)
(Fragment)
Antimicrobial	Glossina	87	MKFYLVLAFLTLCAVAVTALPAGDETRIDLETL
peptide	morsitans		EEDLRLVDGAQVTGELKRDKRVTCNIGEWV
defensin DefA			CVAHCNSKSKKSGYCSRGVCYCTN
Antimicrobial	Glossina	76	PQSPPAQIKDPKIYASGGGSPKDGYNVNVDV
peptide	morsitans		RKNVWVSQNGRHSIDATGGYSQHLGGPYG
diptericin DipA			NSRPDFRGGASYTYRF
(Fragment)
Antimicrobial	Equus	46	DVQCGEGHFCHDXQTCCRASQGGXACCPY
peptide eNAP-	caballus		SQGVCCADQRHCCPVGF
1 (Fragment)
Antimicrobial	Equus	46	EVERKHPLGGSRPGRCPTVPPGTFGHCACL
peptide eNAP-	caballus		CTGDASEPKGQKCCSN
2 (Fragment)
Antimicrobial	Manduca	171	AILFAAIVACACAQVSMPPQYAQIYPEYYKYS
peptide	sexta		KQVRHPRDVTWDKQVGNNGKVFGTLGQND
gloverin			QGLFGKGGYQHQFFDDHRGKLTGQGYGSR
(Fragment)			VLGPYGDSTNFGGRLDWANKNANAALDVTK
			SIGGRTGLTASGSGVWQLGKNTDLSAGGTL
			SQTLGHGKPDVGFQGLFQHRW
Antimicrobial	Sus scrofa	82	MALSVQIRAACLLLLLLVSLTAGSVLPSQTRQ
peptide			LTDLRTQDTAGATAGLTPVAQRLRRDTHFPI
hepcidin			CIFCCGCCRKAICGMCCKT
Antimicrobial	Lumbricus	76	MSLCISDYLYLTLTFSKYERQKDKRPYSERKN
peptide	rubellus		QYTGPQFLYPPERIPPQKVIKWNEEGLPIYEI
lumbricin1			PGEGGHAEPAAA
Antimicrobial	Mytilus	82	MKAVFVLLVVGLCIMMMDVATAGFGCPNNY
peptide	galloprovincialis		ACHQHCKSIRGYCGGYCASWFRLRCTCYRC
MGD2b			GGRRDDVEDIFDIYDNVAVERF
Antimicrobial	Manduca	67	MKLTSLFIFVIVALSLLFSSTDAAPGKIPVKAIK
peptide moricin	sexta		QAGKVIGKGLRAINIAGTTHDWSFFRPKKKK
			H
Antimicrobial	Equus	160	MKKMGCGGRLSSCPTMTSRALLLLASALLGT
peptide NK-	caballus		PGLTFSGLNPESYDLATAHLSDGEQFCQGLT
lysin			QEDLQGDLLTERERQGIACWSCRKILQKLED
			LVGEQPNEATINEAASRVCRNLGLLRGACKKI
			MRTCLRLISRDILAGKKPQEVCVDIKLCKHKA
			GLI
Antimicrobial	Xenopus	24	GVLSNVIGYLKKLGTGALNAVLKQ
peptide PGQ	laevis
Antimicrobial	Meleagris	65	MRIVYLLFPFILLLAQGAAGSSLALGKREKCL
peptide THP1	gallopavo		RRNGFCAFLKCPTLSVISGTCSRFQVCCKTLL
precursor			G
(Turkey
heterophil
peptide 1)
Antimicrobial	Meleagris	64	MRILYLLFSLLFLALQVSPGLSSPKRDMLFCK
peptide THP2	gallopavo		RGTCHFGRCPSHLIKVGSCFGFRSCCKWPW
precursor			DA
(Turkey
heterophil
peptide 2)
Antimicrobial	Meleagris	25	LSCKRGTCHFGRCPSHLIKGSCSGG
peptide THP3	gallopavo
(Turkey
heterophil
peptide 3)
(Fragment)
Antimicrobial	Manduca	207	KMFTKFVVLVCLLVGAKARPQLGALTFNSDG
protein attacin	sexta		TSGAAVKVPFGGNKNNIFSAIGGADFNANHK
2 (Fragment)			LSSATAGVALDNIRGHGLSLTDTHIPGFGDKL
			TAAGKLNLFHNNNHDLTANAFATRNMPNIPQ
			VPNFNTVGGGLDYMFKNKVGASLGAAHTDFI
			NRNDYSVGGKLNLFRNPSTSLDFNAGFKKFD
			TPFMRSGWEPNMGFSLSKFF
Antimicrobial	Oryctolagus	171	METHKHGPSLAWWSLLLLLLGLLMPPAIAQD
protein CAP18	cuniculus		LTYREAVLRAVDAFNQQSSEANLYRLLSMDP
precursor (18			QQLEDAKPYTPQPVSFTVKETECPRTTWKLP
kDa			EQCDFKEDGLVKRCVGTVTRYQAWOSFDIR
lipopolysacchar-			CNRAQESPEPTGLRKRLRKFRNKIKEKLKKIG
ide- binding			QKIQGFVPKLAPRTDY
protein) (18
kDa cationic
protein)
(CAP18-A)
Antimicrobial-	Pheretima	67	MYSKYERQKDKRPYSERKDQYTGPQFLYPP
like peptide	tschiliensis		DRIPPSKAIKWNEEGLPMYEVLPDGAGAKTA
PP-1			VEAAAE
Apidaecin	Bombus	17	GNRPVYIPPPRPPHPRL
	pascuorum
apidaecin Ib	Apis mellifera	26	EAKPEAKPGNNRPVYIPQPRPPHPRL
precursor
Apidaecin	Apis mellifera	168	MKNFALAILVVTFVVAVFGNTNLDPPTRPARL
precursor, type			RREAKPEAEPGNNRPIYIPQPRPPHPRLRRE
14			AEPKAEPGNNRPIYIPQPRPPHPRLRREAES
			EAEPGNNRPVYIPQPRPPHPRLRREPEAEPG
			NNRPVYIPQPRPPHPRLRREPEAEPGNNRPV
			YIPQPRPPHPRI
Apidaecin	Apis mellifera	144	MKNFALAILVVTFVVAVFGNTNLDPPTRPTRL
precursor, type			RREAEPEAEPGNNRPVYIPQPRPPHPRLRRE
22			AEPEAEPGNNRPVYIPQPRPPHPRLRREAEP
			EAEPGNNRPVYIPQPRPPHPRLRREAEPEAE
			PGNNRPVYIPQPRPPHPRI
Apidaecin	Apis mellifera	283	KNFALAILVVTFVVAVFGNTNLDPPTRPTRLR
precursor, type			REAKPEAEPGNNRPVYIPQPRPPHPRLRREA
73 (Fragment)			EPEAEPGNNRPVYIPQPRPPHPRLRREAELE
			AEPGNNRPVYISQPRPPHPRLRREAEPEAEP
			GNNRPVYIPQPRPPHPRLRREAELEAEPGNN
			RPVYISQPRPPHPRLRREAEPEAEPGNNRPV
			YIPQPRPPHPRLRREAEPEAEPGNNRPVYIP
			QPRPPHPRLRREAEPEAEPGNNRPVYIPQPR
			PPHPRLRREAKPEAKPGNNRPVYIPQPRPPH
			PRI
Apolipoprotein	Bos taurus	76	QAEESNLQSLVSQYFQTVADYGKDLVEKAK
A-II (Apo-AII)			GSELQTQAKAYFEKTQEELTPFFKKAGTDLL
(Antimicrobial			NFLSSFIDPKKQPAT
peptide BAMP-
1)
ASABF	Ascaris suum	93	MKTAIIVVLLVIFASTNAAVDFSSCARMDVPGL
precursor			SKVAQGLCISSCKFQNCGTGHCEKRGGRPT
(ASABF-alpha)			CVCDRCGRGGGEWPSVPMPKGRSSRGRR
			HS
ASABF-epsilon	Ascaris suum	65	MVTKGIVLFMLVILFASTDAATCGYDDAKLNR
(ASABF-			PTIGCILSCKVQGCETGACYLRDSRPICVCKR
epsilon2)			C
ASABF-zeta	Ascaris suum	94	MKAILIALLLTTFTVVNGGVVLTSCARMDTPVL
			SKAAQGLCITSCKYQNCGTGFCQKVGGRPT
			CMCRRCANGGGSWPVIPLDTLVKLALKRGK
			R
ASABF-zeta2	Ascaris suum	35	TSCKYQNCGTGFCQKVGGRPTCMCRRCAN
(Fragment)			GGGSWP
Attacin A	Drosophila	224	MQKTSILIVALVALFAITEALPSLPTTGPIRVRR
precursor	melanogaster		QVLGGSLTSNPAGGADARLDLTKGIGNPNHN
			VVGQVFAAGNTQSGPVTTGGTLAYNNAGHG
			ASLTKTHTPGVKDVFQQEAHANLFNNGRHNL
			DAKVFASQNKLANGFEFQRNGAGLDYSHING
			HGASLTHSNFPGIGQQLGLDGRANLWSSPN
			RATTLDLTGSASKWTSGPFANQKPNFGAGL
			GLSHHFG
Attacin A	Trichoplusia	254	MFTYKLILGLVLVVSASARYLVFEDLEGESYL
precursor	ni		VPNQAEDEQVLEGEPFYENAVQLASPRVRR
			QAQGSVTLNSDGSMGLGAKVPIVGNEKNVL
			SALGSVDLNDQLKPASRGMGLALDNVNGHG
			LSVMKETVPGFGDRLTGAGRVNVFHNDNHDI
			SAKAFVTKNMPDFPNVPNFNTVGGGVDYMY
			KNKVGASLGMANTPFLDRKDYSAMGNLNVF
			RSPTTSVDFNAGFKKFDTPVFKSNWEPNFGL
			TFSRSFGNKW
Attacin B	Drosophila	218	MQKTSILILALFAIAEAVPTTGPIRVRRQVLGG
precursor	melanogaster		SLASNPAGGADARLNLSKGIGNPNHNVVGQ
			VFAAGNTQSGPVTTGGTLAYNNAGHGASLT
			KTHTPGVKDVFQQEAHANLFNNGRHNLDAK
			VFASQNKLANGFEFQRNGAGLDYSHINGHG
			ASLTHSNFPGIGQQLGLDGRANLWSSPNRAT
			TLDLTGSASKWTSGPFANQKPNFGAGLGLS
			HHFG
Attacin B	Hyalophora	233	MFAKLFLVSVLLVGVNSRYVLVEEPGYYDKQ
precursor	cecropia		YEEQPQQWVNSRVRRQAGALTINSDGTSGA
(Immune			VVKVPITGNENHKFSALGSVDLTNQMKLGAA
protein P5)			TAGLAYDNVNGHGATLTKTHIPGFGDKMTAA
			GKVNLFHNDNHDFSAKAFATKNMPNIPQVPN
			FNTVGAGVDYMFKDKIGASANAAHTDFINRN
			DYSLGGKLNLFKTPTTSLDFNAGWKKFDTPF
			FKSSWEPSTSFSFSKYF
Aftacin E and F	Hyalophora	235	MFGKIVFLLLVALCAGVQSRYLIVSEPVYYIEH
precursor	cecropia		YEEPELLASSRVRRDAHGALTLNSDGTSGAV
(Immune			VKVPFAGNDKNIVSAIGSVDLTDRQKLGAATA
protein P5)			GVALDNINGHGLSLTDTHIPGFGDKMTAAGK
			VNVFHNDNHDITAKAFATRNMPDIANVPNFN
			TVGGGIDYMFKDKIGASASAAHTDFINRNDYS
			LDGKLNLFKTPDTSIDFNAGFKKFDTPFMKSS
			WEPNFGFSLSKYF
Attacin	Bombyx mori	214	MSKSVALLLLCACLASGRHVPTRARRQAGSF
precursor			TVNSDGTSGAALKVPLTGNDKNVLSAIGSAD
(Nuecin)			FNDRHKLSAASAGLALDNVNGHGLSLTGTRI
			PGFGEQLGVAGKVNLFHNNNHDLSAKAFAIR
			NSPSAIPNAPNFNTLGGGVDYMFKQKVGASL
			SAAHSDVINRNDYSAGGKLNLFRSPSSSLDF
			NAGFKKFDTPFYRSSWEPNVGFSFSKFF
Attacin-A	Drosophila	221	MQNTSILIVALVALFAITEALPTTGPIRVRRQVL
CG10146-PA	melanogaster		GGSLTSNPAGGADARLDLTKGIGNPNHNVV
			GQVFAAGNTQSGPVTTGGTLAYNNAGHGAS
			LTKTHTPGVKDVFQQEAHANLFNNGRHNLD
			AKVFASQNKLANGFEFQRNGAGLDYSHINGH
			GASLTHSNFPGIGQQLGLDGRANLWSSPNR
			ATTLDLTGSASKWTSGPFANQKPNFGAGLGL
			SHHFG
Attacin-B	Drosophila	218	MQKTSILILALFAIAEAVPTTGPIRVRRQVLGG
CG18372-PA	melanogaster		SLASNPAGGADARLNLSKGIGNPNHNVVGQ
			VFAAGNTQSGPVTTGGTLAYNNAGHGASLT
			KTHTPGVKDVFQQEAHANLFNNGRHNLDAK
			VFASQNKLANGFEFQRNGAGLDYSHINGHG
			GSLTHSNFPGIGQQLGLDGRANLWSSPNRA
			TTLDLTGSASKWTSGPFANQKPNFGAGLGLS
			HHFG
Azurocidin	Sus scrofa	219	IVGGRRAQPQEFPFLASIQKQGRPFCAGALV
(Cationic			HPRFVLTAASCFRGKNSGSASVVLGAYDLRQ
antimicrobial			QEQSRQTFSIRSISQNGYDPRQNLNDVLLLQ
protein CAP37)			LDREARLTPSVALVPLPPQNATVEAGTNCQV
(Heparin-			AGWGTQRLRRLFSRFPRVLNVTVTSNPCLP
binding protein)			RDMCIGVFSRRGRISQGDRGTPLVCNGLAQ
(HBP)			GVASFLRRRFRRSSGFFTRVALFRNWIDSVL
			NNPP
bactenecin 5	Bos taurus	42	RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPP
			FRPPLRFP
Bactenecin 5	Ovis aries	176	METQGASLSLGRWSLWLLLLGLVLPSASAQA
precursor			LSYREAVLRAVGQLNERSSEANLYRLLELDP
(BAC5)			APNDEVDPGTRKPVSFTVKETVCPRTTQQPP
			EECDFKENGLVKQCVGTVTLDPSNDQFDINC
			NELQSVRFRPPIRRPPIRPPFRPPFRPPVRPP
			IRPPFRPPFRPPIGPFPGRR
Bactenecin 5	Bos taurus	176	METQRASLSLGRCSLWLLLLGLVLPSASAQA
precursor			LSYREAVLRAVDQFNERSSEANLYRLLELDP
(BAC5) (PR-			TPNDDLDPGTRKPVSFRVKETDCPRTSQQPL
42)			EQCDFKENGLVKQCVGTVTLDPSNDQFDINC
			NELQSVRFRPPIRRPPIRPPFYPPFRPPIRPPI
			FPPIRPPFRPPLGPFPGRR
Bactenecin 5	Capra hircus	176	METQGASLSLGRWSLWLLLLGLVVPLASAQA
precursor			LSYREAVLRAVGQLNERSSEANLYRLLELDP
(CHBAC5)			APNDEVDPGTRKPVSFTVKETVCPRTTQQPP
			EECDFKENGLVKQCVGTVTLDPSNDQFDINC
			NELQSVRFRPPIRRPPIRPPFNPPFRPPVRPP
			FRPPFRPPFRPPIGPFPGRR
bactenecin 7	Bos taurus	59	RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPL
			PFPRPGPRPIPRPLPFPRPGPRPIPRP
Bactenecin 7	Ovis aries	190	METQMASPSLGRCSLWLLLLGLLLPSASAQA
precursor			LSYREAVLRAVGQLNEKSSEVNLYRLLELDP
(BAC7)			PPKDAEDQGARKPVSFRVKETVCPRMSQQP
			PEQCDFKENGLVKQCVGTVSLDTSNDEFDL
			NCNELQSVRRLRPRRPRLPRPRPRPRPRPR
			SLPLPRPQPRRIPRPILLPWRPPRPIPRPQPQ
			PIPRWL
Bactenecin 7	Bos taurus	190	METQRASLSLGRWSLWLLLLGLVLPSASAQA
precursor			LSYREAVLRAVDRINERSSEANLYRLLELDPP
(BAC7) (PR-			PKDVEDRGARKPTSFTVKETVCPRTSPQPPE
59)			QCDFKENGLVKQCVGTITLDQSDDLFDLNCN
			ELQSVRRIRPRPPRLPRPRPRPLPFPRPGPR
			PIPRPLPFPRPGPRPIPRPLPFPRPGPRPIPR
			PL
beta defensin	Mus	74	MKISYFLLLILSLGSSQINPVSGDDSIQCFQKN
39	musculus		NTCHTNQCPYFQDEIGTCYDRRGKCCQKRL
			LHIRVPRKKKV
Beta defensin 9	Mus	78	MPVTKSYFMTVVVVLILVDETTGGLFGFRSSK
precursor	musculus		RQEPWIACELYQGLCRNACQKYEIQYLSCPK
(Hypothetical			TRKCCLKYPRKITSF
defensin-like
structure
containing
protein)
Beta defensin-	Capra hircus	64	MRLHHLLLALFFLVLSAGSGFTQGIINHRSCY
2 precursor			RNKGVCAPARCPRNMRQIGTCHGPPVKCCR
			KK
Beta-defensin	Bos taurus	38	DFASCHTNGGICLPNRCPGHMIQIGICFRPRV
1 (BNDB-1)			KCCRSW
(BNBD-1)
Beta-defensin	Capra hircus	64	MRLHHLLLVLFFLVLSAGSGFTQGIRSRRSCH
1 precursor			RNKGVCALTRCPRNMRQIGTCFGPPVKCCR
(BD-1)			KK
Beta-defensin	Sus scrofa	64	MRLHRLLLVFLLMVLLPVPGLLKNIGNSVSCL
1 precursor			RNKGVCMPGKCAPKMKQIGTCGMPQVKCC
(BD-1)			KRK
(Defensin, beta
1)
Beta-defensin	Pan	68	MRTSYLLLFTLCLLLSEMASGGNFLTGLGHR
1 precursor	troglodytes		SDHYNCVSSGGQCLYSACPIFTKIQGTCYRG
(BD-1) (hBD-1)			KAKCCK
(Defensin, beta
1)
Beta-defensin	Mus	69	MKTHYFLLVMICFLFSQMEPGVGILTSLGRRT
1 precursor	musculus		DQYKCLQHGGFCLRSSCPSNTKLQGTCKPD
(BD-1) (mBD-			KPNCCKS
1)
Beta-defensin	Rattus	69	MKTHYFLLVMLFFLFSQMELGAGILTSLGRRT
1 precursor	norvegicus		DQYRCLQNGGFCLRSSCPSHTKLQGTCKPD
(BD-1) (RBD-1)			KPNCCRS
Beta-defensin	Macaca	68	MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
1 precursor	mulatta		SDHYNCVRSGGQCLYSACPIYTRIQGTCYHG
(BD-1) (RhBD-			KAKCCK
1) (Defensin,
beta 1)
Beta-defensin	Ovis aries	64	MRLHHLLLVLFFVVLSAGSGFTQGVRNRLSC
1 precursor			HRNKGVCVPSRCPRHMRQIGTCRGPPVKCC
(BD-1) (sBD1)			RKK
Beta-defensin	Bos taurus	40	QGVRSYLSCWGNRGICLLNRCPGRMRQIGT
10 (BNDB-10)			CLAPRVKCCR
(BNBD-10)
Beta-defensin	Bos taurus	38	GPLSCRRNGGVCIPIRCPGPMRQIGTCFGRP
11 (BNDB-11)			VKCCRSW
(BNBD-11)
Beta-defensin	Macaca	123	MKLLLLALPILVLLPQVIPAYGGEKKCWNRSG
118 precursor	mulatta		HCRKQCKDGEAVKETCKNHRACCVPSNEDH
(Epididymal			RRLPTTSPTPLSDSTPGIIDNILTIRFTTDYFEI
secretory			SSKKDMVEESEAGQGTQTSPPNVHHTS
protein 13.6)
(ESP13.6)
Beta-defensin	Bos taurus	38	GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRP
12 (BNDB-12)			VKCCRSW
(BNBD-12)
Beta-defensin	Macaca	123	MKSLLFTLAVFMLLAQLVSGNLYVKRCLNDIG
126 precursor	fascicularis		ICKKTCKPEEVRSEHGWVMCGKRKACCVPA
(Epididymal			DKRSAYPSFCVHSKTTKTSTVTARATATTATT
secretory			ATAATPLMISNGLISLMTTMAATPVSPTT
protein 13.2)
(ESP13.2)
Beta-defensin	Bos taurus	42	SGISGPLSCGRNGGVCIPIRCPVPMRQIGTCF
13 (BNDB-13)			GRPVKCCRSW
(BNBD-13)
Beta-defensin	Macaca	64	MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCL
2	mulatta		KNGAICHPVFCPRRYKQIGTCGLPGTKCCKK
			P
Beta-defensin	Bos taurus	40	VRNHVTCRINRGFCVPIRCPGRTRQIGTCFG
2 (BNDB-2)			PRIKCCRSW
(BNBD-2)
Beta-defensin	Mus	71	MRTLCSLLLICCLLFSYTTPAVGSLKSIGYEAE
2 precursor	musculus		LDHCHTNGGYCVRAICPPSARRPGSCFPEK
(BD-2) (mBD-			NPCCKYMK
2)
Beta-defensin	Rattus	63	MRIHYLLFSFLLVLLSPLSAFTQSINNPITCLTK
2 precursor	norvegicus		GGVCWGPCTGGFRQIGTCGLPRVRCCKKK
(BD-2) (RBD-2)
Beta-defensin	Ovis aries	64	MRLHHLLLVLFFVVLSAGSGFTHGVTDSLSC
2 precursor			RWKKGICVLTRCPGTMRQIGTCFGPPVKCC
(BD-2) (sBD2)			RLK
Beta-defensin	Mus	63	MRIHYLLFAFLLVLLSPPAAFSKKINNPVSCLR
3 precursor	musculus		KGGRCWNRCIGNTRQIGSCGVPFLKCCKRK
(BD-3) (mBD-
3)
Beta-defensin	Bos taurus	57	LALLFLVLSAGSGFTQGVRNHVTCRINRGFC
3 precursor			VPIRCPGRTRQIGTCFGPRIKCCRSW
(BNDB-3)
(BNBD-3)
(Fragment)
Beta-defensin	Mus	63	MRIHYLLFTFLLVLLSPLAAFTQIINNPITCMTN
4 precursor	musculus		GAICWGPCPTAFRQIGNCGHFKVRCCKIR
(BD-4) (mBD-
4)
Beta-defensin	Bos taurus	63	MRLHHLLLAVLFLVLSAGSGFTQRVRNPQSC
4 precursor			RWNMGVCIPFLCRVGMRQIGTCFGPRVPCC
(BNDB-4)			RR
(BNBD-4)
beta-defensin 4	Mus	63	MRIHYLLFTFLPVLLSPLAAFTQIINNPITCMTN
variant	musculus		GAICWGPCPTAFRQIGNCGHFKVRCCKIR
Beta-defensin	Bos taurus	64	MRLHHLLLVLLFLVLSAGSGFTQVVRNPQSC
5 precursor			RWNMGVCIPISCPGNMRQIGTCFGPRVPCC
(BNDB-5)			RRW
(BNBD-5)
Beta-defensin	Mus	63	MKIHYLLFAFILVMLSPLAAFSQLINSPVTCMS
6	musculus		YGGSCQRSCNGGFRLGGHCGHPKIRCCRR
			K
Beta-defensin	Bos taurus	42	QGVRNHVTCRIYGGFCVPIRCPGRTRQIGTC
6 (BNDB-6)			FGRPVKCCRRW
(BNBD-6)
Beta-Defensin	Mus	37	NSKRACYREGGECLQRCIGLFHKIGTCNFRF
7	musculus		KCCKFQ
Beta-defensin	Bos taurus	40	QGVRNFVTCRINRGFCVPIRCPGHRRQIGTC
7 (BNDB-7)			LGPRIKCCR
(BNBD-7)
Beta-defensin	Mus	71	MRIHYVLFAFLLVLLSPFAAFSQDINSKRACY
7 precursor	musculus		REGGECLQRCIGLFHKIGTCNFRFKCCKFQIP
			EKKTKIL
Beta-Defensin	Mus	35	NEPVSCIRNGGICQYRCIGLRHKIGTCGSPFK
8	musculus		CCK
Beta-defensin	Mus	60	MRIHYLLFTFLLVLLSPLAAFSQKINEPVSCIR
8 (Beta-	musculus		NGGICQYRCIGLRHKIGTCGSPFKCCK
defensin 6)
Beta-defensin	Bos taurus	38	VRNFVTCRINRGFCVPIRCPGHRRQIGTCLG
8 (BNDB-8)			PQIKCCR
(BNBD-8)
Beta-defensin	Bos taurus	55	LALLFLVLSAGSGFTQGVRNFVTCRINRGFCV
9 precursor			PIRCPGHRRQIGTCLAPQIKCCR
(BNDB-9)
(BNBD-9)
(Fragment)
Beta-defensin	Bos taurus	53	LALLFLVLSAGSGISGPLSCRRKGGICILIRCP
C7 precursor			GPMRQIGTCFGRPVKCCRSW
(BBD(C7))
(Fragment)
Beta-defensin	Gallus gallus	80	MRIVYLLIPFFLLFLQGAAGTATQCRIRGGFC
prepropeptide			RVGSCRFPHIAIGKCATFISCCGRAYEVDALN
			SVRTSPWLLAPGNNPH
Beta-defensin	Meleagris	59	MRIVYLLFPFFLLFLQSAAGTPIQCRIRGGFCR
prepropeptide	gallopavo		FGSCRFPHIAIAKCATFIPCCGSIWG
Beta-defensin-	Equus	64	MRILHFLLAFLIVFLLPVPGFTAGIETSFSCSQ
1	caballus		NGGFCISPKCLPGSKQIGTCILPGSKCCRKK
Beta-defensin-	Mus	85	MKNLPSNMALSREVFYFGFALFFIVVELPSGS
12	musculus		WAGLEYSQSFPGGEIAVCETCRLGRGKCRR
(Hypothetical			TCIESEKIAGWCKLNFFCCRERI
defensin-like
structure
containing
protein)
Beta-defensin-	Pan	64	MRVLYLLFSFLFIELMPLPGVFGGISDPVTCLK
2	troglodytes		SGAICHPVFCPRRYKQIGTCGLPGTKCCKKP
beta-defensin-3	Bos taurus	42	QGVRNHVTCRINRGFCVPIRCPGRTRQIGTC
			FGPRIKCCRSW
Beta-defensin-	Pan	64	MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC
3 (Fragment)	troglodytes		RVRGGRCAVLTCLPKEEQIGKCSTRGRKCC
			R
beta-defensin-4	Bos taurus	41	QRVRNPQSCRWNMGVCIPFLCRVGMRQIGT
			CFGPRVPCCRR
beta-defensin-5	Bos taurus	40	QVVRNPQSCRWNMGVCIPISCPGNMRQIGT
			CFGPRVPCCR
beta-defensin-9	Bos taurus	40	QGVRNFVTCRINRGFCVPIRCPGHRRQIGTC
			LGPQIKCCR
Beta-defensin-	Canis	65	MKAFLLTLAALVLLSQVTSGSAEKCWNLRGS
like peptide 1	familiaris		CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML
			QR
Beta-defensin-	Canis	69	MKAFLLTLAALVLLSQVTSGSAEECWNLRGS
like peptide 2	familiaris		CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML
			QRSVQF
Beta-defensin-	Canis	99	MKAFLLTLAALVLLSQVTSGSAEKCWNLRGS
like peptide 3	familiaris		CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML
			QRNRKDNPKICLELQKILNIQSNLDKEEQSWK
			HCTS
Big defensin	Tachypleus	79	NPLIPAIYIGATVGPSVWAYLVALVGAAAVTA
	tridentatus		ANIRRASSDNHSCAGNRGWCRSKCFRHEYV
			DTYYSAVCGRYFCCRSR
bombinin H	Bombina	20	IIGPVLGMVGSALGGLLKKI
Met-8	variegata
Bombinin	Bombina	21	IIGPVLGMVGSALGGLLKKIG
H1/H3	variegata
Bombinin H4	Bombina	21	LIGPVLGLVGSALGGLLKKIG
	variegata
Bombinin H5	Bombina	21	IIGPVLGLVGSALGGLLKKIG
	variegata
Bombinin-like	Bombina	27	GIGSAILSAGKSALKGLAKGLAEHFAN
peptide 2 (BLP-	orientalis
2)
Bombinin-like	Bombina	25	GIGAAILSAGKSIIKGLANGLAEHF
peptide 4 (BLP-	orientalis
4)
Bombinin-like	Bombina	144	MNFKYIVAVSFLIASTYARSVKNDEQSLSQRD
peptide 7, BPL-	orientalis		VLEEESLREIRGIGGALLSAGKSALKGLAKGL
7 precursor			AEHFANGKRTAEEHEVMKRLEAVMRDLDSL
			DYPEEASEMETRSFNQEEIANLFTKKEKRILG
			PVLDLVGRALRGLLKKIG
Bombinin-like	Bombina	204	MNFKYIVAVSILIASAYARSEENDIQSLSQRDV
peptides 1	orientalis		LEEESLREIRGIGASILSAGKSALKGLAKGLAE
precursor			HFANGKRTAEDHEVMKRLEAAIQSLSQRDVL
[Contains:			EEESLREIRGIGASILSAGKSALKGLAKGLAEH
Acidic peptide			FANGKRTAEEHEVMKRLEAVMRDLDSLDYP
1; Bombinin-			EEASEMETRSFNQEEIANLYTKKEKRILGPIL
like peptide 1			GLVSNALGGLLG
(BLP-1);
Octapeptide 1;
Acidic peptide
2; Octapeptide
2; Acidic
peptide 3; GH-
1 peptide]
Bombinin-like	Bombina	137	MNFKYIVAVSILIASAYARSEENDIQSLSQRDV
peptides 1	variegata		LEEESLREIRGIGGALLSAAKVGLKGLAKGLA
precursor			EHFANGKRTAEEREVMKRLEAAMRDLDSFE
[Contains:			HPEEASEKETRGFNQEEKEKRIIGPVLGLVGS
Acidic peptide			ALGGLLKKIG
1-1; Bombinin-
like peptide 1
(BLP-1);
Octapeptide 1;
Acidic peptide
1-2; Bombinin
H]
Bombinin-like	Bombina	137	MNFKYIVAVSILIASAYARREENNIQSLSQRDV
peptides 2	variegata		LEEESLREIRGIGASILSAGKSALKGFAKGLAE
precursor			HFANGKRTAEDHEMMKRLEAAVRDLDSLEH
[Contains:			PEEASEKETRGFNQEEKEKRIIGPVLGLVGSA
Acidic peptide			LGGLLKKIG
2-1; Bombinin-
like peptide 2
(BLP-2);
Octapeptide 2;
Acidic peptide
2-2; Bombinin
H2]
Bombinin-like	Bombina	200	MNFKYIVAVSILIASAYARSEENDIQSLSQRDV
peptides 3	orientalis		LEEESLREIRGIGAAILSAGKSALKGLAKGLAE
precursor			HFGKRTAEDHEVMKRLEAAIHSLSQRDVLEE
[Contains:			ESLREIRGIGAAILSAGKSALKGLAKGLAEHF
Acidic peptide			GKRTAEEHEMMKRLEAVMRDLDSLDYPEEA
1; Bombinin-			SEMETRSFNQEEIANLYTKKEKRILGPILGLVS
like peptide 3			NALGGLLG
(BLP-3);
Octapeptide 1;
Acidic peptide
2; Octapeptide
2; Acidic
peptide 3; GH-
1 peptide]
Bovine	Bos taurus	38	APLSCGRNGGVCIPIRCPVPMRQIGTCFGRP
Neutrophil			VKCCRSW
Beta-Defensin
12
Brevinin-1	Rana	24	FLPVLAGIAAKVVPALFCKITKKC
	brevipoda
Brevinin-1BA	Rana	24	FLPFIAGMAAKFLPKIFCAISKKC
	berlandieri
Brevinin-1BB	Rana	24	FLPAIAGMAAKFLPKIFCAISKKC
	berlandieri
Brevinin-1BC	Rana	24	FLPFIAGVAAKFLPKIFCAISKKC
	berlandieri
Brevinin-1BD	Rana	24	FLPAIAGVAAKFLPKIFCAISKKC
	berlandieri
Brevinin-1BE	Rana	24	FLPAIVGAAAKFLPKIFCVISKKC
	berlandieri
Brevinin-1BF	Rana	24	FLPFIAGMAANFLPKIFCAISKKC
	berlandieri
Brevinin-1E	Rana	71	MFTLKKSMLLLFFLGTINLSLCEEERDADEEE
precursor	esculenta		RRDNPDESEVEVEKRFLPLLAGLAANFLPKIF
			CKITRKC
Brevinin-1Ea	Rana	24	FLPAIFRMAAKVVPTIICSITKKC
	esculenta
brevinin-1Eb	Rana	24	VIPFVASVAAEMMQHVYCAASRKC
	esculenta
Brevinin-1Eb	Rana	23	VIPFVASVAAEMQHVYCAASRKC
	esculenta
Brevinin-1LA	Rana	24	FLPMLAGLAASMVPKLVCLITKKC
	luteiventris
Brevinin-1LB	Rana	24	FLPMLAGLAASMVPKFVCLITKKC
	luteiventris
Brevinin-1PA	Rana pipiens	24	ELPIIAGVAAKVFPKIFCAISKKC
Brevinin-1PB	Rana pipiens	24	FLPIIAGIAAKVFPKIFCAISKKC
Brevinin-1PC	Rana pipiens	24	FLPIIASVAAKVFSKIFCAISKKC
Brevinin-1PD	Rana pipiens	24	FLPIIASVAANVFSKIFCAISKKC
Brevinin-1PE	Rana pipiens	24	FLPIIASVAAKVFPKIFCAISKKC
Brevinin-1Sa	Rana	24	FLPAIVGAAGQFLPKIFCAISKKC
	sphenocephala
Brevinin-1Sb	Rana	24	FLPAIVGAAGKFLPKIFCAISKKC
	sphenocephala
Brevinin-1Sc	Rana	24	FFPIVAGVAGQVLKKIYCTISKKC
	sphenocephala
Brevinin-1SY	Rana	24	FLPVVAGLAAKVLPSIICAVTKKC
	sylvatica
Brevinin-1T	Rana	20	VNPIILGVLPKFVCLITKKC
	temporaria
Brevinin-1TA	Rana	17	FITLLLRKFICSITKKC
	temporaria
Brevinin-2	Rana	33	GLLDSLKGFAATAGKGVLQSLLSTASCKLAKT
	brevipoda		C
Brevinin-2E	Rana	33	GIMDTLKNLAKTAGKGALQSLLNKASCKLSG
	esculenta		QC
Brevinin-2Ea	Rana	33	GILDTLKNLAISAAKGAAQGLVNKASCKLSGQ
	esculenta		C
Brevinin-2Eb	Rana	33	GILDTLKNLAKTAGKGALQGLVKMASCKLSG
	esculenta		QC
Brevinin-2Ec	Rana	34	GILLDKLKNFAKTAGKGVLQSLLNTASCKLSG
	esculenta		QC
Brevinin-2Ed	Rana	29	GILDSLKNLAKNAGQILLNKASCKLSGQC
	esculenta
Brevinin-2Ee	Rana	29	GIFDKLKNFAKGVAQSLLNKASCKLSGQC
	esculenta
Brevinin-2Ef	Rana	74	MFTMKKSLLLIFFLGTISLSLCQEERNADDDD
precursor	esculenta		GEMTEEEKRGIMDTLKNLAKTAGKGALQSLV
			KMASCKLSGQC
Brevinin-2T	Rana	33	GLLSGLKKVGKHVAKNVAVSLMDSLKCKISG
	temporaria		DC
Brevinin-2Tb	Rana	74	MFTMKKSLLLFFFLGTISLSLCQEERNADEDD
precursor	temporaria		GEMTEEEKRGILDTLKHLAKTAGKGALQSLL
			NHASCKLSGQC
Brevinin-2TC	Rana	29	GLWETIKNFGKKFTLNILHKLKCKIGGGC
	temporaria
Brevinin-2TD	Rana	29	GLWETIKNFGKKFTLNILHNLKCKIGGGC
	temporaria
buforin I	Bufo	129	MSGRGKQGGKVRAKAKTRSSRAGLQFPVG
	gargarizans		RVHRLLRKGNYAQRVGAGAPVYLAAVLEYLT
			AEILELAGNAARDNKKTRIIPRHLQLAVRNDE
			ELNKLLGGVTIAQGGVLPNIQAVLLPKTESSK
			PAKSK
Buthinin	Androctonus	34	SIVPIRCRSNRDCRRFCGFRGGRCTYARQCL
	australis		CGY
Caeridin	Litoria chloris	13	MGLLDGLLGTLGL
1.1/1.2/1.3
Caeridin	Litoria	12	GLLDGLLGTLGL
1.1/1.2/1.3	xanthomera
Caeridin 1.4	Litoria chloris	13	MGLLDGLLGGLGL
Caeridin 1.4	Litoria	12	GLLDGLLGGLGL
	xanthomera
Caerin 1.1	Litoria	26	MGLLSVLGSVAKHVLPHVVPVIAEHL
	caerulea
Caerin 1.1	Litoria	25	GLLSVLGSVAKHVLPHVVPVIAEHL
	splendida
Caerin 1.6	Litoria chloris	25	MGLFSVLGAVAKHVLPHVVPVIAEK
Caerin 1.6	Litoria	24	GLFSVLGAVAKHVLPHVVPVIAEK
	xanthomera
Caerin 1.7	Litoria chloris	25	MGLFKVLGSVAKHLLPHVAPVIAEK
Caerin 1.7	Litoria	24	GLFKVLGSVAKHLLPHVAPVIAEK
	xanthomera
Caerulein	Litoria	10	QQDYTGWMDF
	xanthomera
cathelin related	Mus	172	MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPS
antimicrobial	musculus		YRDAVLRAVDDFNQQSLDTNLYRLLDLDPEP
peptide			QGDEDPDTPKSVRFRVKETVCGKAERQLPE
			QCAFKEQGWKQCMGAVTLNPAADSFDISC
			NEPGAQPFRFKKISRLAGLLRKGGEKIGEKLK
			KIGQKIKNFFQKLVPQPE
Cathelin-	Mus	173	MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPS
related	musculus		YRDAVLRAVDDFNQQSLDTNLYRLLDLDPEP
antimicrobial			QGDEDPDTPKSVRFRVKETVCGKAERQLPE
peptide			QCAFKEQGWKQCMGAVTLNPAADSFDISC
precursor			NEPGAQPFRFKKISRLAGLLRKGGEKIGEKLK
(Cramp)			KIGQKIKNFFQKLVPQPEQ
(Cathelin-like
protein) (CLP)
Cathelin-	Ovis aries	160	METQRASLSLGRCSLWLLLLGLALPSASAQV
related peptide			LSYREAVLRAADQLNEKSSEANLYRLLELDP
SC5 precursor			PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
1 (Antibacterial			AEQCDFKENGLLKECVGTVTLDQVRNNFDIT
peptide SMAP-			CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
29) (Myeloid			RIAG
antibacterial
peptide SMAP-
29)
Cathelin-	Ovis aries	160	METQRASLSLGRRSLWLLLLGLVLASASAQA
related peptide			LSYREAVLRAVDQLNEKSSEANLYRLLELDP
SC5 precursor			PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
2 (Antibacterial			AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
peptide SMAP-			CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
29) (Myeloid			RIAG
antibacterial
peptide SMAP
29)
cathelin-related	Ovis aries	160	METQRAGLSLGRRSLWLLLLGLVLASASAQA
protein 1			LSYREAVLRAVDQLNEKSSEANLYRLLELDP
precursor			PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
			AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
			CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
			RIAG
cathelin-related	Ovis aries	152	SLGRCSLWLLLLGLALPSASAQVLSYREAVL
protein 2			RAADQLNEKSSEANLYRLLELDPPPKQDDEN
precursor			SNIPKPVSFRVKETVCPRTSQQPAEQCDFKE
			NGLLKECVGTVTLDQVRNNFDITCAEPQSVR
			GLRRLGRKIAHGVKKYGPTVLRIIRIAG
Cecropin	Bombyx mori	35	RWKIFKKIEKVGQNIRDGIVKAGPAVAVVGQA
(Antibacterial			ATI
peptide CM-IV)
Cecropin 1	Ceratitis	63	MNFNKVFILVAIVIAIFAGQTEAGWLKKIGKKIE
precursor	capitata		RVGQHTRDATIQTIAVAQQAANVAATARG
Cecropin 1	Drosophila	63	MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI
precursor	virilis		ERIGQHTRDATIQGLGIAQQAANVAATARG
Cecropin 2	Ceratitis	63	MNFNKVLVLLAVIFAVFAGQTEAGWLKKIGKK
precursor	capitata		IERVGQHTRDATIQTIGVAQQAANVAATLKG
Cecropin 2	Drosophila	63	MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI
precursor	virilis		ERVGQHTRDATIQGLGIAQQAANVAATARG
Cecropin 3	Drosophila	63	MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI
precursor	virilis		ERIGQHTRDATIQGVGIAQQAANVAATARG
Cecropin A	Aedes	59	MNFTKLFLLIAVAVLLLTGQSEAGGLKKLGKK
precursor	aegypti		LEGAGKRVFNAAEKALPVVAGAKALRK
Cecropin A	Bombyx mori	63	MNFVRILSFVFALVLALGAVSAAPEPRWKLFK
precursor			KIEKVGRNVRDGLIKAGPAIAVIGQAKSLGK
Cecropin A	Trichoplusia	62	MNLVKILFCVFACLVFTVTAVPEPRWKFFKKI
precursor	ni		EKVGQNIRDGIIKAGPAVAWGQAASITGK
Cecropin A	Hyalophora	64	MNFSRIFFFVFACLTALAMVNAAPEPKWKLF
precursor	cecropia		KKIEKVGQNIRDGIIKAGPAVAWGQATQIAK
(Cecropin C)			G
Cecropin A	Spodoptera	57	IFFFVFACLLALSAVSAAPEPRWKVFKKIEKV
precursor	litura		GRNVRDGIIKAGPAIGVLGQAKALG
(Fragment)
Cecropin	Drosophila	63	MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIE
A1/A2	melanogaster		RVGQHTRDATIQGLGIAQQAANVAATARG
precursor
Cecropin B	Antheraea	35	KWKIFKKIEKVGRNIRNGIIKAGPAVAVLGEAK
	pernyi		AL
Cecropin B	Drosophila	63	MNFNKIFVFVALILAISLGNSEAGWLRKLGKKI
precursor	melanogaster		ERIGQHTRDASIQVLGIAQQAANVAATARG
Cecropin B	Spodoptera	58	ILSFVFACLLALSAVSAAPEPRWKVFKKIEKM
precursor	litura		GRNIRDGIVKAGPAIEVLGSAKALGK
(Fragment)
Cecropin B	Hyalophora	62	MNFSRIFFFVFALVLALSTVSAAPEPKWKVFK
precursor	cecropia		KIEKMGRNIRNGIVKAGPAIAVLGEAKALG
(Immune
protein P9)
Cecropin B	Bombyx mori	63	MNFAKILSFVFALVLALSMTSAAPEPRWKIFK
precursor			KIEKMGRNIRDGIVKAGPAIEVLGSAKAIGK
(Lepidopteran
A and B)
Cecropin C	Drosophila	63	MNENKIFVFVALILAISLGQSEAGWLKKLGKRI
precursor	erecta		ERIGQHTRDATIQGLGIAQQAANVAATARG
Cecropin C	Drosophila	63	MNFYKIFVFVALILAISIGQSEAGWLKKLGKRI
precursor	mauritiana		ERIGQHTRDATIQGLGIAQQAANVAATARG
Cecropin D	Bombyx mori	61	MKFSKIFVFVFAIVFATASVSAAPGNFFKDLE
precursor			KMGQRVRDAVISAAPAVDTLAKAKALGQG
Cecropin D	Hyalophora	62	MNFTKILFFWACVFAMRTVSAAPWNPFKEL
precursor	cecropia		EKVGQRVRDAVISAGPAVATVAQATALAKGK
Cecropin P1	Sus scrofa	31	SWLSKTAKKLENSAKKRISEGIAIAIQGGPR
ceratotoxin A	Ceratitis	29	SIGSALKKALPVAKKIGKIALPIAKAALP
	capitata
Ceratotoxin A	Ceratitis	71	MANLKAVFLICIVAFIALQCVVAEPAAEDSVVV
precursor 1	capitata		KRSIGSALKKALPVAKKIGKIALPIAKAALPVAA
			GLVG
Ceratotoxin A	Ceratitis	71	MANLKAVFLICIVAFIAFQCVVAEPAAEDSIVV
precursor 2	capitata		KRSIGSALKKALPVAKKIGKIALPIAKAALPVAA
			GLVG
Ceratotoxin B	Ceratitis	29	SIGSAFKKALPVAKKIGKAALPIAKAALP
	capitata
Ceratotoxin C	Ceratitis	67	MANIKAVFLICIVAFIAFHCVVAEPTAEDSVVV
precursor	capitata		KRSLGGVISGAKKVAKVAIPIGKAVLPVVAKLV
			G
Ceratotoxin D	Ceratitis	71	MANLKAVFLICILAFIAFHCWGAPTAEDSIVV
precursor	capitata		KRSIGTAVKKAVPIAKKVGKVAIPIAKAVLSVV
			GQLVG
Chlamysin	Chlamys	137	MMYFVLFCLLAAGTTYGSHNFATGIVPHSCL
precursor	islandica		ECICKTESGCRAIGCKFDVYSDSCGYFQLKQ
			AYWEDCGRPGGSLTSCADDIHCSSQCVQHY
			MSRYIGHTSCSRTCESYARLHNGGPHGCEH
			GSTLGYWGHVQGHGC
Chromogranin	Bos taurus	449	MRSAAVLALLLCAGQVIALPVNSPMNKGDTE
A precursor			VMKCIVEVISDTLSKPSPMPVSKECFETLRGD
(CgA) (Pituitary			ERILSILRHQNLLKELQDLALQGAKERTHQQK
secretory			KHSSYEDELSEVLEKPNDQAEPKEVTEEVSS
protein I) (SP-I)			KDAAEKRDDFKEVEKSDEDSDGDRPQASPG
[Contains:			LGPGPKVEEDNQAPGEEEEAPSNAHPLASLP
Vasostatin-1			SPKYPGPQAKEDSEGPSQGPASREKGLSAE
Chromostatin;			QGRQTEREEEEEKWEEAEAREKAVPEEESP
Chromacin;			PTAAFKPPPSLGNKETQRAAPGWPEDGAGK
Pancreastatin;			MGAEEAKPPEGKGEWAHSRQEEEEMARAP
WE-14;			QVLFRGGKSGEPEQEEQLSKEWEDAKRWS
Catestatin]			KMDQLAKELTAEKRLEGEEEEEEDPDRSMR
			LSFRARGYGFRGPGLQLRRGWRPNSREDSV
			EAGLPLQVRGYPEEKKEEEGSANRRPEDQE
			LESLSAIEAELEKVAHQLEELRRG
chromogranin	Bos taurus	170	MPVDIRNHNEEVVTHLRDPADTSEAPGLSAG
B			EPPGSQVAKEAKTRYSKSEGQNREEEMVKY
			QKRERGEVGSEERLSEGPQRNQTPAKKSSQ
			EGNPPLEEESHVGTGALEEGAERLPGELRNY
			LDYGEEKGEESAEFPDFYDSEEQMSPQHTA
			EDLELQKIAEKFSGTRRG
Chrysophsin-1	Pagrus major	25	FFGWLIKGAIHAGKAIHGLIHRRRH
Chrysophsin-2	Pagrus major	25	FFGWLIRGAIHAGKAIHGLIHRRRH
Chrysophsin-3	Pagrus major	20	FIGLLISAGKAIHDLIRRRH
Cicadin	Cicada	55	NEYHGFVDKANNENKRKKQQGRDDFWKPN
(Fragment)	flammata		NFANRRRKDDYNENYYDDVDAADVV
Citropin 1.1	Litoria citropa	16	GLFDVIKKVASVIGGL
[Contains:
Citropin 1.1.1;
Citropin 1.1.2]
Citropin 1.1.3	Litoria citropa	18	GLFDVIKKVASVIGLASP
Citropin 1.1.4	Litoria citropa	18	GLFDVIKKVASVIGLASQ
Citropin 1.2	Litoria citropa	16	GLFDIIKKVASVVGGL
[Contains:
Citropin 1.2.1;
Citropin 1.2.2;
Citropin 1.2.3]
Citropin 1.2.4	Litoria citropa	18	GLFDIIKKVASVVGLASP
Citropin 1.2.5	Litoria citropa	18	GLFDIIKKVASVVGLASQ
Citropin 1.3	Litoria citropa	16	GLFDIIKKVASVIGGL
Citropin 2.1.3	Litoria citropa	26	GLIGSIGKALGGLLVDVLKPKLQAAS
[Contains:
Citropin 2.1.2;
Citropin 2.1.1;
Citropin 2.1]
Citropin 3.1.2	Litoria citropa	24	DLFQVIKEKLKELTGGVIEGIQGV
[Contains:
Citropin 3.1.1;
Citropin 3.1]
Clavanin A	Styela clava	80	MKTTILILLILGLGINAKSLEERKSEEEKVFQFL
precursor			GKIIHHVGNFVHGFSHVFGDDQQDNGKFYG
			HYAEDNGKHWYDTGDQ
Clavanin B	Styela clava	23	VFQFLGRIIHHVGNFVHGFSHVF
Clavanin C	Styela clava	80	MKTTILILLILGLGINAKSLEERKSEEEKVFHLL
precursor			GKIIHHVGNFVYGFSHVFGDDQQDNGKFYG
			HYAEDNGKHWYDTGDQ
Clavanin D	Styela clava	80	MKTTILILLILGLGINAKSLEERKSEEEKAFKLL
precursor			GRIIHHVGNFVYGFSHVFGDDQQDNGKFYG
			HYAEDNGKHWYDTGDQ
Clavanin E	Styela clava	80	MKTTILILLILGLGINAKSLEERKSEEEKLFKLL
precursor			GKIIHHVGNFVHGFSHVFGDDQQDNGKFYG
			YYAEDNGKHWYDTGDQ
Coleoptericin	Zophobas	74	SLQGGAPNFPQPSQQNGGWQVSPDLGRDD
	atratus		KGNTRGQIEIQNKGKDHDFNAGWGKVIRGP
			NKAKPTWHVGGTYRR
Corticostatin I	Oryctolagus	93	MRTLILLAAILLAALQAQAELFSVNVDEVLDQ
precursor (CS-	cuniculus		QQPGSDQDLVIHLTGEESSALQVPDTKGICA
I) (Neutrophil			CRRRFCPNSERFSGYCRVNGARYVRCCSRR
antibiotic
peptide NP-3A)
(Microbicidal
peptide NP-3A)
(Antiadrenocort-
icotropin
peptide I)
Corticostatin II	Oryctolagus	34	GRCVCRKQLLCSYRERRIGDCKIRGVRFPFC
(CS-II)	cuniculus		CPR
(Neutrophil
antibiotic
peptide NP-3B)
(Microbicidal
peptide NP-3B)
(Antiadrenocort-
icotropin
peptide II)
Corticostatin III	Oryctolagus	95	MRTLALLAAILLVALQAQAEHVSVSIDEVVDQ
precursor (CS-	cuniculus		QPPQAEDQDVAIYVKEHESSALEALGVKAGV
III)			VCACRRALCLPRERRAGFCRIRGRIHPLCCR
(Macrophage			R
antibiotic
peptide MCP-
1) (NP-1)
(Antiadrenocort-
icotropin
peptide III)
Corticostatin IV	Oryctolagus	95	MRTLALLAAILLVALQAQAEHISVSIDEVVDQQ
precursor (CS-	cuniculus		PPQAEDQDVAIYVKEHESSALEALGVKAGVV
IV)			CACRRALCLPLERRAGFCRIRGRIHPLCCRR
(Macrophage
antibiotic
peptide MCP-
2) (NP-2)
(Antiadrenocort-
icotropin
peptide IV)
Corticostatin VI	Oryctolagus	34	GICACRRRFCLNFEQFSGYCRVNGARYVRC
(CS-VI)	cuniculus		CSRR
(Neutrophil
antibiotic
peptide NP-6)
Corticostatin-	Oryctolagus	32	MPCSCKKYCDPWEVIDGSCGLFNSKYICCRE
related peptide	cuniculus		K
RK-1
Crabrolin	Vespa crabro	13	FLPLILRKIVTAL
cryptdin	Mus	23	CKRRERMNGTCRKGHLLYTLCCR
	musculus
cryptdin 12	Mus	35	LRDLVCYCRARGCKGRERMNGTCRKGHLLY
	musculus		MLCCR
Cryptdin-1	Mus	35	LRDLVCYCRTRGCKRRERMNXTCRKGHLMY
(CR1)	musculus		TLCCX
Cryptdin-1	Mus	93	MKKLVLLFALVLLGFQVQADSIQNTDEETKTE
precursor	musculus		EQPGEEDQAVSVSFGDPEGTSLQEESLRDL
(DEFCR)			VCYCRSRGCKGRERMNGTCRKGHLLYTLCC
			R
cryptdin-10	Mus	35	LRDLVCYCRKRGCKGRERMNGTCRKGHLLY
	musculus		TLCCR
Cryptdin-10	Mus	92	KTLVLLSALVLLAFQVQADPIQNTDEETKTEE
precursor	musculus		QPGEDDQAVSVSFGDPEGSSLQEESLRDLV
(Fragment)			CYCRKRGCKGRERMNGTCRKGHLLYTMCC
			R
cryptdin-11	Mus	35	LRDLVCYCRSRGCKGRERMNGTCRKGHLLY
	musculus		MLCCR
Cryptdin-11	Mus	85	ALVLLAFQVQADPIQNTDEETKTEEQPGEED
precursor	musculus		QAVSVSFGDPEGTSLQEESLRDLVCYCRSR
(Fragment)			GCKGRERMNGTCRKGHLLYMLCCR
cryptdin-13	Mus	35	LRDLVCYCRKRGCKRREHMNGTCRRGHLM
	musculus		YTLCCR
Cryptdin-13	Mus	93	MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor	musculus		EQPGEEDQAVSVSFGDPEGTSLQEESLRDL
			VCYCRKRGCKRREHMNGTCRRGHLMYTLC
			CR
Cryptdin-14	Mus	85	ALVLLAFQVQADPIQNTDEETKTEEQPGEDD
precursor	musculus		QAVSVSFGDPEGSSLQEESLRDLVCYCRTR
(Fragment)			GCKRRERMNGTCRKGHLMHTLCCR
cryptdin-15	Mus	35	LRDLVCYCRKRGCKRREHINGTCRKGHLLY
	musculus		MLCCR
Cryptdin-15	Mus	93	MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor	musculus		EQPGEDDQAVSVSFGDPEGSSLQEESLRDL
			VCYCRKRGCKRREHINGTCRKGHLLYMLCC
			R
cryptdin-16	Mus	35	LRDLVCYCRSRGCKGRERMNGTCRKGHLM
	musculus		YTLCCR
Cryptdin-16	Mus	93	MKTLILLSALVLLAFQVQADPIQNTDEETKTEE
precursor	musculus		QPGEEDQAVSVSFGDPEGTSLQEESLRDLV
			CYCRSRGCKGRERMNGTCRKGHLMYTLCC
			R
Cryptdin-17	Mus	82	LLAFQVQADPIQNTDEETKTEEQPGEEDQAV
precursor	musculus		SVSFGDPEGTSLQEESLRDLVCYCRKRGCK
(CRYP17)			RREHMNGTCRKGHLLYTLCCR
(Fragment)
Cryptdin-2	Mus	35	LRDLVCYCRARGXKGRERMNGTXRKGHLLY
(CR2)	musculus		MXXXX
Cryptdin-2	Mus	93	MKPLVLLSALVLLSFQVQADPIQNTDEETKTE
precursor	musculus		EQSGEEDQAVSVSFGDREGASLQEESLRDL
			VCYCRTRGCKRRERMNGTCRKGHLMYTLC
			CR
Cryptdin-3	Mus	93	MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor	musculus		EQPGEDDQAVSVSFGDPEGSSLQEESLRDL
			VCYCRKRGCKRRERMNGTCRKGHLMYTLC
			CR
cryptdin-4	Mus	34	LRGLLCYCRKGHCKRGERVRGTCGIRFLYCC
	musculus		PRR
Cryptdin-4	Mus	92	MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor	musculus		EQPGEEDQAVSISFGGQEGSALHEKSLRGLL
			CYCRKGHCKRGERVRGTCGIRFLYCCPRR
Cryptdin-5	Mus	93	MKTFVLLSALVLLAFQVQADPIHKTDEETNTE
precursor	musculus		EQPGEEDQAVSISFGGQEGSALHEELSKKLI
			CYCRIRGCKRRERVFGTCRNLFLTFVFCCS
Cryptdin-6/12	Mus	93	MKTLILLSALVLLAFQVQADPIQNTDEETKTEE
precursor	musculus		QPGEEDQAVSVSFGDPEGTSLQEESLRDLV
			CYCRARGCKGRERMNGTCRKGHLLYMLCC
			R
cryptdin-7	Mus	35	LRDLVCYCRTRGCKRREHMNGTCRKGHLMY
	musculus		TLCCR
Cryptdin-7	Mus	93	MKTLILLSALVLLAFQVQADPIQNTDEETKTEE
precursor	musculus		QPGEDDQAVSVSFGDPEGSSLQEESLRDLV
			CYCRTRGCKRREHMNGTCRKGHLMYTLCC
			R
cryptdin-8	Mus	35	LRDLVCYCRKRGCKRREHMNGTCRKGHLM
	musculus		YTLCCR
Cryptdin-8	Mus	81	LAFQVQADPIQNTDEETKTEEQPGEDDQAVS
precursor	musculus		VSFGDPEGSSLQEESLRDLVCYCRKRGCKR
(Fragment)			REHMNGTCRKGHLMYTLCCR
cryptdin-9	Mus	35	LRDLVCYCRKRGCKRREHMNGTCRKGHLLY
	musculus		MLCCR
Cryptdin-9	Mus	93	MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor	musculus		EQPGEEDQAVSVSFGDPEGSSLQEESLRDL
			VCYCRKRGCKRREHMNGTCRKGHLLYMLC
			CR
Cryptdin-	Mus	116	MKTLVLLSALVLPCFQVQADPIQNTDEETKTE
related protein	musculus		EQPEEEDQAVSVSFGGTEGSALQDVAQRRF
1C precursor			PWCRKCRVCQKCQVCQKCPVCPTCPQCPK
(CRS1C)			QPLCEERQNKTAITTQAPNTQHKGC
Cryptdin-	Mus	91	MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related protein	musculus		EQPGEKDQAVSVSFGDPQGSALQDAALGW
4C-1 precursor			GRRCPQCPRCPSCPSCPRCPRCPRCKCNP
(CRS4C)			K
Cryptdin-	Mus	91	MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related protein	musculus		EQQGEEDQAVSVSFGDPQGSGLQDAALGW
4C-2 precursor			GRRCPRCPPCPRCSWCPRCPTCPRCNCNP
(CRS4C)			K
Cryptdin-	Mus	91	MKKLVLLSAFVLLAFQVQADSIQNTDEETKTE
related protein	musculus		EQPGEENQAMSVSFGDPEGSALQDAAVGM
4C-4 precursor			ARPCPPCPSCPSCPWCPMCPRCPSCKCNP
(CRS4C)			K
Cryptdin-	Mus	91	MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTE
related protein	musculus		EQPGEENQAVSISFGDPEGYALQDAAIRRAR
4C-5 precursor			RCPPCPSCLSCPWCPRCLRCPMCKCNPK
(CRS4C)
Cyclic	Bos taurus	155	METPRASLSLGRWSLWLLLLGLALPSASAQA
dodecapeptide			LSYREAVLRAVDQLNEQSSEPNIYRLLELDQP
precursor			PQDDEDPDSPKRVSFRVKETVCSRTTQQPP
(Bactenecin 1)			EQCDFKENGLLKRCEGTVTLDQVRGNFDITC
			NNHQSIRITKQPWAPPQAARLCRIVVIRVCR
Cyclic	Ovis aries	155	METQRASLSLGRCSLWLLLLGLALPSASAQV
dodecapeptide			LSYREAVLRAVDQLNEQSSEPNIYRLLELDQP
precursor			PQDDEDPDSPKRVSFRVKETVCPRTTQQPP
(Bactenecin 1)			EQCDFKENGLLKRCEGTVTLDQVRGNFDITC
			NNHQSIRITKQPWAPPQAARICRIIFLRVCR
DEFB1-like	Cercopithecus	68	MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
protein	aethiops		SDHYNCVRSGGQCLYSACPIYTKIQGTCYHG
			KAKCCK
DEFB1-like	Cercopithecus	68	MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
protein	erythrogaster		SDHYICVRSGGQCLYSACPIYTKIQGTCYHG
			KAKCCK
DEFB1-like	Gorilla gorilla	68	MRTSYLLLFTLCLLLSEIASGGNFLTGLGHRS
protein			DHYNCVSSGGQCLYSACPIFTKIQGTCYGGK
			AKCCK
DEFB1-like	Hylobates	68	MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
protein	concolor		SDHYNCVRSGGQCLYSACPIYTKIQGTCYQG
			KAKCCK
DEEBI-like	Pan	68	MRTSYLLLFTLCLLLSEMASGGNFLTGLGHR
protein	troglodytes		SDHYNCVSSGGQCLYSACPIFTKIQGTCYGG
			KAKCCK
DEFB1-like	Presbytis	68	MRTSYLLLFTLCLLMSEMASGDNFLTGLGHR
protein	obscura		SDHYNCVRSGGQCLYSACPIYTKIQGTCYHG
			KAKCCK
DEFB1-like	Saguinus	68	MRTSYLLLFILCLVLCDMDSGDTFLTGLGHRS
protein	oedipus		DHYNCVKGGGQCLYSACPIYTKVQGTCYGG
			KAKCCK
DEFB36	Mus	43	MKLLLLTLAALLLVSQLTPGDAQKCWNLHGK
(Fragment)	musculus		CRHRCSRKESVY
Defensin	Aeshna	38	GFGCPLDQMQCHRHCQTITGRSGGYCSGPL
	cyanea		KLTCTCYR
Defensin	Allomyrina	43	VTCDLLSFEAKGFAANHSLCAAHCLAIGRRG
	dichotoma		GSCERGVCICRR
Defensin	Anopheles	102	MKCATIVCTIAVVLAATLLNGSVQAAPQEEAA
	gambiae		LSGGANLNTLLDELPEETHHAALENYRAKRA
			TCDLASGFGVGNNLCAAHCIARRYRGGYCN
			SKAVCVCRN
defensin	Anopheles	131	NSRVNGATPAKLKLVLLCLPRASSSPQLIMKC
	gambiae		ATIVCTIAWLAATLLNGSVQAAPQEEAALSG
			GANLNTLLDELPEETHHAALENYRAKRATCD
			LASGFGVGSSLCAAHCIARRYRGGYCNSKAV
			CVCRN
Defensin	Bombus	51	VTCDLLSIKGVAEHSACAANCLSMGKAGGRC
	pascuorum		ENGICLCRKTTFKELWDKRF
Defensin	Branchiostoma	117	MEKKTAYCLLFLVLLVPYTALGAVLKRAPAKK
	beicheri		EKRAVPLAVPLVYWGASVSPAVWNWLLVTF
			GAAAVAAAAVTVSDNDSHSCANNRGWCRS
			RCFSHEYIDSWHSDVCGSYDCCRPRY
Defensin	Drosophila	92	MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
	melanogaster		HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
			WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin	Drosophila	92	MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
	melanogaster		HVLVHEDANQEVLQHSRQKRATCDLLSKWN
			WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin	Drosophila	92	MKFFVLVAIAFALLTCMAQAQPVSDVDPIPED
	melanogaster		HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
			WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin	Drosophila	92	MKFFVPVAIAFALLACVAQAQPVSDVDPIPED
	melanogaster		HVLVHDDAHQEVLQHSRQKRATCDLLSKWN
			WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin	Drosophila	92	MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
	simulans		HALVHEDAHQEWQHSRQKRATCDLLSKWN
			WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin	Mamestra	98	MLCLADIRIVASCSAAIKSGYGQQPWLAHVA
	brassicae		GPYANSLFDDVPADSYHAAVEYLRLIPASCYL
			LDGYAAGRDDGRAHCIAPRNRRLYCASYQV
			CVCRY
Defensin	Musca	92	MKYFTMFAFFFVAVCYISQSSASPAPKEEAN
	domestica		FVHGADALKQLEPELHGRYKRATCDLLSGTG
			VGHSACAAHCLLRGNRGGYCNGKGVCVCR
			N
Defensin	Ornithodoros	73	MNKLFIVALVLALAVATMAHEVHDDIEEPSVP
	moubata		RVRRGFGCPFNQYECHAHCSGVPGYKGGY
			CKGLFKQTCNCY
Defensin	Ornithodoros	73	MNKLFIVALVLALAVATMAHEVYDDVEEPSVP
	moubata		RVRRGYGCPFNQYQCHSHCSGIRGYKGGY
			CKGLFKQTCNCY
Defensin	Palomena	43	ATCDALSFSSKWLTVNHSACAIHCLTKGYKG
	prasina		GRCVNTICNCRN
Defensin	Phlebotomus	40	ATCDLLSAFGVGHAACAAHCIGHGYRGGYC
	duboscqi		NSKAVCTCRR
Defensin	Pyrocoelia	55	MKLSVFVLVAVMLVLLCCAMQTEARRRCRS
	rufa		CVPFCGSNERMISTCFSGGVVCCPR
Defensin	Pyrrhocoris	43	ATCDILSFQSQWVTPNHAGCALHCVIKGYKG
	apterus		GQCKITVCHCRR
Defensin	Aedes	57	DELPEETYQAAVENYRRKRATCDLLSGFGVG
(Fragment)	albopictus		DSACAAHCIARRNRGGYCNAKTVCVC
Defensin	Apis mellifera	57	FEPLEHFENEERADRHRRVTCDLLSFKGQVN
(Fragment)			DSACAANCHSLGKAGGHCEKGVCICR
Defensin 1	Stomoxys	39	ATCDLLSGMGVNHSACAAHCVLRGNRGGYC
(Fragment)	calcitrans		NSKAVCVCR
Defensin 1	Acalolepta	83	MKFFITFTFVLSLWLTVYSAPREFAEPEEQD
precursor	luxuriosa		EGHFRVKRFTCDVLSVEAKGVKLNHAACGIH
			CLFRRRTGGYCNKKRVCICR
Defensin 1	Stomoxys	79	MKFLNVVAIALLVVACLAVYSNAAPHEGVKEV
precursor	calcitrans		AAAKPMGITCDLLSLWKVGHAACAAHCLVLG
			DVGGYCTKEGLCVCKE
Defensin 1A	Stomoxys	79	MKFLNVVAIALLVVACLSVYSNAAPHEGVKEV
precursor	calcitrans		AAAKPMGITCDLLSLWKVGHAACAAHCLVLG
			NVGGYCTKEGLCVCKE
Defensin 2	Stomoxys	97	MKFFSLFPVIVVVVACLTMRANAAPSAGNEV
precursor	calcitrans		DHHPDYVDGVEALRQLEPELHGRYKRATCD
			LLSMWNVNHSACAAHCLLLGKSGGRCNDDA
			VCVCRK
Defensin 2A	Stomoxys	97	MKFFSLFPVILVVVACLTMRANAAPSAGDEV
precursor	calcitrans		DHHPDYVDGVEALRQLEPELHGRYKRATCD
			LLSMWNVNHSACAAHCLLLGKSGGRCNDDA
			VCVCRK
Defensin 5	Rattus	93	MKKLVLLSALVLLALQVEAEPTPKTDEGTKTD
precursor (RD-	norvegicus		EQPGKEDQWSVSIEGQGDPAFQDAVLRDL
5) (Enteric			KCFCRRKSCNWGEGIMGICKKRYGSPILCCR
defensin
Defensin A	Aedes	98	MQSLTVICFLALCTGAITSAYPQEPVLADEAR
	aegypti		PFANSLFDELPEETYQAAVENFRLKRATCDLL
			SGFGVGDSACAAHCIARGNRGGYCNSKKVC
			VCRN
Defensin A	Mytilus edulis	37	GFGCPNDYPCHRHCKSIPGRXGGYCGGXHR
			LRCTCYR
Defensin A	Ornithodoros	73	MNKLFIVALVVALAVATMAQEVHNDVEEQSV
	moubata		PRVRRGYGCPFNQYQCHSHCSGIRGYKGGY
			CKGTFKQTCKCY
Defensin A	Rhodnius	94	MKCILSLVTLFLVAVLVHSHPAEWNTHQQLD
	prolixus		DALWEPAGEVTEEHVARLKRATCDLFSFRSK
			WVTPNHAACAAHCLLRGNRGGRCKGTICHC
			RK
defensin A	Aedes	37	MKSLTVICFLALCTGAITSAYPQEPVLADEAR
isoform 2;	aegypti		PFANS
AaDefA2
defensin A	Aedes	37	MQSLTVICFLALCTGAITSAYPQEPVLADEAR
isoform 3;	aegypti		PFANS
AaDefA3
defensin A	Aedes	37	MQPLTVICFLALCTGAITSAYPQEPVLADEAR
isoform 4;	aegypti		PFANS
AaDefA4
Defensin A	Aedes	98	MKSITVICFLALCTVAITSAYPQEPVLADEARP
precursor	aegypti		FANSLFDELPEETYQAAVENFRLKRATCDLLS
(AADEF)			GFGVGDSACAAHCIARGNRGGYCNSKKVCV
			CRN
defensin A	Aedes	98	MQSITVICFLALCTGAITSAYPQEPVLADEARP
protein isoform	aegypti		FANSLFDELPEETYQAAVENFRLKRATCDLLS
5			GFGVGDSACAAHCIARGNRGGYCNSKKVCV
			CRN
defensin alpha-	Macaca	30	ACYCRIPACLAGERRYGTCFYLGRVWAFCC
1	mulatta
defensin alpha-	Macaca	30	ACYCRIPACLAGERRYGTCFYRRRVWAFCC
3	mulatta
defensin alpha-	Macaca	33	RRTCRCRFGRCFRRESYSGSCNINGRIFSLC
4	mulatta		CR
defensin alpha-	Macaca	32	RTCRCRFGRCFRRESYSGSCNINGRIFSLCC
5	mulatta		R
defensin alpha-	Macaca	33	RRTCRCRFGRCFRRESYSGSCNINGRISSLC
6	mulatta		CR
defensin alpha-	Macaca	32	RTCRCRFGRCFRRESYSGSCNINGRISSLCC
7	mulatta		R
Defensin B	Aedes	40	ATCDLLSGFGVGDSACAAHCIARGNRGGYC
	aegypti		NSQKVCVCRN
Defensin B	Ornithodoros	73	MNKLFIVALVVALAVATMAQEVHDDVEEQSV
	moubata		PRVRRGYGCPFNQYQCHSHCRGIRGYKGG
			YCTGRFKQTCKCY
Defensin B	Rhodnius	94	MKCILSLVTLFLVAVLVHSHPAEWNTQQELD
	prolixus		DALWEPAGEVTEEHVARLKRATCDLLSFSSK
			WVTPNHAGCAAHCLLRGNRGGHCKGTICHC
			RK
Defensin B	Mytilus edulis	35	GFGCPNDYPCHRHCKSIPGRYGGYCGGXHR
(Fragment)			LRCTC
defensin beta	Mus	67	MRLHYLLFVFLILFLVPAPGDAFLPKTLRKFFC
14; beta	musculus		RIRGGRCAVLNCLGKEEQIGRCSNSGRKCC
defensin 14			RKKK
defensin beta	Mus	81	MKTFLFLFAVLFFWSQPRMHFFFFDEKCSRI
34; beta	musculus		NGRCTASCLKNEELVALCWKNLKCCVTVQS
defensin 34			CGRSKGNQSDEGSGHMGTRG
defensin beta	Mus	62	MKFSYFLLLLLSLSNFQNNPVAMLDTIACIENK
37; beta	musculus		DTCRLKNCPRLHNVVGTCYEGKGKCCHKN
defensin 37
defensin beta	Mus	63	MKISCFLLLILSLYFFQINQAIGPDTKKCVQRK
38; beta	musculus		NACHYFECPWLYYSVGTCYKGKGKCCQKRY
defensin 38
defensin beta	Mus	73	MKISCFLLMIFFLSCFQINPVAVLDTIKCLQGN
40; beta	musculus		NNCHIQKCPWFLLQVSTCYKGKGRCCQKRR
defensin 40			WFARNHVYHV
Defensin beta	Mus	64	MRIHYLLFAFLLVLLCPLASDFSKTINNPVSCC
5	musculus		MIGGICRYLCKGNILQNGNCGVTSLNCCKRK
Defensin C	Rhodnius	94	MKCILSLFTLFLVATLVYSYPAEWNSQHQLDD
	prolixus		AQWEPAGELTEEHLSRMKRATCDLLSLTSK
			WFTPNHAGCAAHCIFLGNRGGRCVGTVCHC
			RK
defensin C	Zophobas	43	FTCDVLGFEIAGTKLNSAACGAHCLALGRTG
	atratus		GYCNSKSVCVCR
Defensin C	Aedes	99	MRTLIWCFVALCLSAIFTTGSALPGELADDV
precursor	aegypti		RPYANSLFDELPEESYQAAVENFRLKRATCD
			LLSGFGVGDSACAAHCIARRNRGGYCNAKK
			VCVCRN
Defensin D	Aedes	96	VPTVICFLAMCLVAITGAYPQEPVLADEAQSV
precursor	albopictus		ANSLFDELPEESYQAAVENLRLKRATCDLLS
(AALDEFD)			GFGVGDSACAAHCIARGNRGGYCNSKKVCV
(Fragment)			CPI
Defensin	Heliothis	44	DKLIGSCVWGAVNYTSDCNGECKRRGYKGG
heliomicin	virescens		HCGSFANVNCWCET
Defensin	Heliothis	44	DKLIGSCVWGAVNYTSDCNGECLLRGYKGG
Heliomicin	virescens		HCGSFANVNCWCET
defensin	Aedes	98	MKSITVICFLALCTGSITSAYPQDPVLADEARP
isoform A1	aegypti		FANSLFDELPEETYQAAVENFRLKRATCDLLS
			GFGVGDSACAAHCIARGNRGGYCNSKKVCV
			CRN
defensin	Aedes	98	MKSITVICFLALCTVAITSAYPQEPVLADEARP
isoform B1	aegypti		FANSLFDELPEETYQAAVENFRLKRATCDLLS
			GFGVGDSACAAHCIARGNRGGYCNSQKVCV
			CRN
defensin	Aedes	98	MKSITVICFLALCTGSITSAYPQEPVLADEARP
isoform B2	aegypti		FANSLFDELPEETYQAAVENFRLKRATCDLLS
			GFGVGDSACAAHCIARGNRGGYCNSQKVCV
			CRN
defensin	Aedes	99	MRTLIVVCFVALCLSAIFTTGSALPEELADDVR
isoform C1	aegypti		SYANSLFDELPEESYQAAVENFRLKRATCDL
			LSGFGVGDSACAAHCIARRNRGGYCNAKKV
			CVCRN
Defensin Mgd-	Mytilus	39	GFGCPNNYQCHRHCKSIPGRCGGYCGGWH
1	galloprovincialis		RLRCTCYRCG
Defensin MGD-	Mytilus	38	GFGCPNNYQCHRHCKSIPGRCGGYCGGXH
1	galloprovincialis		RLRCTCYRC
Defensin MGD-	Mytilus	81	MKAAFVLLWGLCIMTDVATAGFGCPNNYAC
2 precursor	galloprovincialis		HQHCKSIRGYCGGYCAGWFRLRCTCYRCG
			GRRDDVEDIFDIYDNVAVERF
defensin NP-1	Rattus	32	VTCYCRRTRCGFRERLSGACGYRGRIYRLC
	norvegicus		CR
defensin NP-4	Rattus	31	ACYCRIGACVSGERLTGACGLNGRIYRLCCR
	norvegicus
Defensin	Anopheles	102	MKCATIVCTIAVVLAATLLNGSVQAAPQEEAA
precursor	gambiae		LSGGANLNTLLDELPEETHHAALENYRAKRA
			TCDLASGFGVGSSLCAAHCIARRYRGGYCN
			SKAVCVCRN
Defensin	Drosophila	92	MKFFVLVAIAFALLACVAQAQPVSDVDPIPED
precursor	melanogaster		HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
			WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin	Oryctes	79	MSRFIVFAFIVAMCIAHSLAAPAPEALEASVIR
precursor	rhinoceros		QKRLTCDLLSFEAKGFAANHSLCAAHCLAIG
			RKGGACQNGVCVCRR
defensin	Spodoptera	102	MGVKVINVFLLIAVSACLIHAVAGKPNPRDSS
precursor	frugiperda		VVEEQSLGPIHNEDLEVKVKPETTTTPEPRIP
			GRVSCDFEEANEDAVCQEHCLPKGYTYGICV
			SHTCSCI
Defensin	Culex pipiens	40	ATCDLLSGFGVNDSACAAHCILRGNRGGYC
precursor			NGKKVCVCRN
(Fragment)
defensin R-2	Rattus	31	VTCSCRTSSCRFGERLSGACRLNGRIYRLCC
	norvegicus
defensin R-5	Rattus	32	VTCYCRSTRCGFRERLSGACGYRGRIYRLC
	norvegicus		CR
defensin	Mus	92	MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTE
related	musculus		EQPGEENQAVSISFGDPEGYALQDAAAIRRA
cryptdin,			RRCPPCPSCLSCPWCPRCLRCPMCKCNPK
related
sequence 12
defensin	Mus	92	MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related	musculus		EQQGEEDQAVSVSFGDPQGSGLQDAAALG
cryptdin,			WGRRCPRCPPCPRCSWCPRCPTCPRCNCN
related			PK
sequence 7
Defensin	Mus	60	MRIHYLLFTFLLVLLSPLAAFSQKINDPVTYIR
related peptide	musculus		NGGICQYRCIGLRHKIGTCGSPFKCCK
Defensin,	Zophobas	43	FTCDVLGFEIAGTKLNSAACGAHCLALGRRG
isoforms B and	atratus		GYCNSKSVCVCR
C
defensin-3	Macaca	96	MRTLVILAAILLVALQAQAEPLQARTDEATAA
	mulatta		QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
			KNMACYCRIPACLAGERRYGTCFYRRRVWA
			FCC
defensin-8	Macaca	96	MRTLVILAAILLVALQAQAEPLQARTDEATAA
	mulatta		QEQIPTDNPEVWSLAWDESLAPKDSVPGLR
			KNMACYCRIPACLAGERRYGTCFYLRRVWA
			FCC
defensin-like	Mus	5	ICSPK
gene 1C-1	musculus
Defensin-like	Ornithorhynchus	42	FVQHRPRDCESINGVCRHKDTVNCREIFLAD
peptide 1	anatinus		CYNDGQKCCRK
(DLP-1)
Defensin-like	Ornithorhynchus	42	IMFFEMQACWSHSGVCRDKSERNCKPMAW
peptide 2/4	anatinus		TYCENRNQKCCEY
(DLP-2/DLP-4)
Defensin-like	Ornithorhynchus	38	FEMQYCWSHSGVCRDKSERNNKPMAWTYC
peptide 3	anatinus		ENRQKKCEF
(DLP-3)
Defensin-like	Mesobuthus	61	MTYAILIIVSLLPISDGISNVVDKYCSENPLDCN
protein TXKS2	martensii		EHCLKTKNQIGICHGANGNEKCSCMES
Demidefensin 2	Macaca	76	MRTFALLTAMLLLVALHAQAEARQARADEAA
	mulatta		AQQQPGADDQGMAHSFTWPENAALPLSESA
			KGLRCICTRGFCRLL
Demidefensin 3	Macaca	76	MRTLALHTAMLLLVALHAQAEARQARADEAA
	mulatta		AQQQPGADDQGMAHSFTWPENAALPLSESE
			RGLRCICVLGICRLL
Dermaseptin 1	Phyllomedusa	34	ALWKTMLKKLGTMALHAGKAALGAAADTISQ
(DS I)	sauvagei		GTQ
Dermaseptin BI	Phyllomedusa	78	MDILKKSLFLVLFLGLVSLSICEEEKRENEDEE
precursor	bicolor		KQDDEQSEMKRAMWKDVLKKIGTVALHAGK
(Dermaseptin			AALGAVADTISQGEQ
B1)
Dermaseptin	Phyllomedusa	77	MAFLKKSLFLVLFLGLVSLSVCEEEKRENEDE
DRG3	bicolor		EEQEDDEQSEEKRALWKTIIKGAGKMIGSLA
precursor			KNLLGSQAQPESEQ
(Dermaseptin
3)
Dermatoxin	Phyllomedusa	77	MAFLKKSLFLVLFLGLVPLSLCESEKREGENE
precursor	bicolor		EEQEDDQSEEKRSLGSFLKGVGTTLASVGKV
			VSDQFGKLLQAGQG
Diptericin A	Protophormia	82	DEKPKLILPTPAPPNLPQLVGGGGGNRKDGF
	terraenovae		GVSVDAHQKVWTSDNGGHSIGVSPGYSQHL
			PGPYGNSRPDYRIGAGYSYNF
diptericin B	Protophormia	41	DEKPKLVLPSXAPPNLPQLVGGGGGNNKXG
	terraenovae		XXVSINAAQKV
diptericin C	Protophormia	39	DEKPKLIXPXXAPXNLXQLVGGGGGNNKKXX
	terraenovae		GVXVXXAQ
Diptericin D	Protophormia	101	MKLFYLLVICALSLAVMADEKPKLILPTPAPPN
precursor	terraenovae		LPQLVGGGGGNRKDGFGVSVDAHQKVWTS
			DNGRHSIGVTPGYSQHLGGPYGNSRPDYRI
			GAGYSYNFG
Dolabellanin	Dolabella	33	SHQDCYEALHKCMASHSKPFSCSMKFHMCL
B2	auricularia		QQQ
Drosocin	Drosophila	64	MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT
	melanogaster		SHPRPIRVRREALAIEDHLTQAAIRPPPILPA
Drosocin	Drosophila	64	MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT
	melanogaster		SHPRPIRVRREALAIEDHLTQAAIRPPPILPV
Drosocin	Drosophila	64	MKFTIVFLLLACVFAMGVATPGKPRPYSPRPT
CG10816-PA	melanogaster		SHPRPIRVRREALAIEDHLTQAAIRPPPILPA
Drosocin	Drosophila	64	MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT
precursor	melanogaster		SHPRPIRVRREALAIEDHLAQAAIRPPPILPA
Drosomycin	Drosophila	44	DCLSGRYKGPCAVWDNETCRRVCKEEGRS
	melanogaster		SGHCSPSLKCWCEGC
Drosomycin	Drosophila	70	MMQIKYLFALFAVLMLVVLGANEADADCLSG
precursor	melanogaster		RYKGPCAVWDNETCRRVCKEEGRSSGHCS
(Cysteine-rich			PSLKCWCEGC
peptide)
enbocin	Bombyx mori	59	MNFTRIIFFLGVVVFATASGKPWNIFKEIERAV
			ARTRDAVISAGPAVATVAAATSVASG
Enhancer of	Sus scrofa	32	RADTQTYQPYNKDWIKEKIYVLLRRQAQQAG
rudimentary			K
homolog
[Contains:
Antibacterial
peptide 3910]
(Fragment)
entenic beta	Bubalus	64	MRLHHLLLALLFLVLSAGSGFTQGVRNPQSC
defensin	bubalis		HRNKGICVPIRCPGNMRQIGTCLGPPVKCCR
preproprotein			RK
Enteric beta-	Bos taurus	64	MRLHHLLLTLLFLVLSAGSGFTQGISNPLSCR
defensin			LNRGICVPIRCPGNLRQIGTCFTPSVKCCRW
precursor			R
Eosinophil	Cavia	233	MKLLLLLALLLGAVSTRHLKVDTSSLQSLRGE
granule major	porcellus		ESLAQDGETAEGATREATAGALMPLPEEEE
basic protein 1			MEGASGSEDDPEEEEEEEEEVEFSSELDVS
precursor			PEDIQCPKEEDTVKFFSRPGYKTRGYVMVGS
(MBP-1)			ARTFNEAQWVCQRCYRGNLASIHSFAFNYQ
			VQCTSAGLNVAQVWIGGQLRGKGRCRRFV
			WVDRTVWNFAYWARGQPWGGRQRGRCVT
			LCARGGHWRRSHCGKRRPFVCTY
EP2e (ANTI-	Mus	69	MKVLLLFAVFFCFVQGNSGDIPPGIRNTVCLM
microbial-like	musculus		QQGHCRLFMCRSGERKGDICSDPWNRCCV
protein BIN-1B			PYSVKDRR
homolog)
Esculentin-1	Rana	46	GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVR
	esculenta		TGIDIAGCKIKGEC
Esculentin-1A	Rana	46	GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVR
	esculenta		TGIDIAGCKIKGEC
Esculentin-1B	Rana	84	MFTLKKPLLLIVLLGMISLSLCEQERNADEEE
precursor	esculenta		GSEIKRGIFSKLAGKKLKNLLISGLKNVGKEV
			GMDVVRTGIDIAGCKIKGEC
Esculentin-2A	Rana	37	GILSLVKGVAKLAGKGLAKEGGKFGLELIACKI
	esculenta		AKQC
Esculentin-2B	Rana	37	GLFSILRGAAKFASKGLGKDLTKLGVDLVACK
	berlandieri		ISKQC
Esculentin-2B	Rana	37	GIFSLVKGAAKLAGKGLAKEGGKFGLELIACKI
	esculenta		AKQC
Esculentin-2L	Rana	37	GILSLFTGGIKALGKTLFKMAGKAGAEHLACK
	luteiventris		ATNQC
Esculentin-2P	Rana pipiens	37	GFSSIFRGVAKFASKGLGKDLARLGVNLVAC
			KISKQC
Formaecin 1	Myrmecia	16	GRPNPVNNKPTPHPRL
	gulosa
Formaecin 2	Myrmecia	16	GRPNPVNTKPTPYPRL
	gulosa
Gaegurin-1	Rana rugosa	33	SLESLIKAGAKFLGKNLLKQGACYAACKASKQ
			C
Gaegurin-2	Rana rugosa	33	GIMSIVKDVAKNAAKEAAKGALSTLSCKLAKT
			C
Gaegurin-3	Rana rugosa	33	GIMSIVKDVAKTAAKEAAKGALSTLSCKLAKT
			C
Gaegurin-4	Rana rugosa	80	MFTMKKSLLFLFFLGTISLSLCEEERSADEDD
precursor			GGEMTEEEVKRGILDTLKQFAKGVGKDLVKG
			AAQGVLSTVSCKLAKTC
Gaegurin-5	Rana rugosa	65	MFTLKKSLLLLFFLGTISLSLCEEERNADEEEK
precursor			RDVEVEKRFLGALFKVASKVLPSVFCAITKKC
Gaegurin-6	Rana rugosa	24	FLPLLAGLAANFLPTIICKISYKC
Gal-1 alpha	Gallus gallus	65	MRIVYLLLPFILLLAQGAAGSSQALGRKSDCF
			RKNGFCAFLKCPYLTLISGKCSRFHLCCKRIW
			G
gallinacin	Gallus gallus	39	GRKSDCFRKSGFCAFLKCPSLTLISGKCSRF
			YLCCKRIW
gallinacin	Gallus gallus	36	LFCKGGSCHFGGCPSHLIKVGSCFGFRSCCK
			WPWNA
Gallinacin 1	Gallus gallus	39	GRKSDCFRKNGFCAFLKCPYLTLISGKCSRF
alpha			HLCCKRIW
Gallinacin 1	Gallus gallus	65	MRIVYLLLPFILLLAQGAAGSSQALGRKSDCF
precursor			RKSGFCAFLKCPSLTLISGKCSRFYLCCKRIW
			G
Gallinacin 2	Gallus gallus	64	MRILYLLFSLLFLALQVSPGLSSPRRDMLFCK
precursor			GGSCHFGGCPSHLIKVGSCFGFRSCCKWPW
			NA
Gastric	Sus scrofa	42	YAEGTFISDYSIAMDKIRQQDFVNWLLAQKG
inhibitory			KKSDWKHNITQ
polypeptide
(GIP)
(Glucose-
dependent
insulinotropic
polypeptide)
Gloverin	Hyalophora	130	DVTWDKNIGNGKVFGTLGQNDDGLFGKAGF
	cecropia		KQQFFNDDRGKFEGQAYGTRVLGPAGGTTN
			FGGRLDWSDKNANAALDISKQIGGRPNLSAS
			GAGVWDFDKNTRLSAGGSLSTMGRGKPDV
			GVHAQFQHDF
Gomesin	Acanthoscurria	18	QCRRLCYKQRCVTYCRGR
	gomesiana
GP-	Cavia	31	RRCICTTRTCRFPYRRLGTCLFQNRVYTFCC
CS2 = CORTIC
OSTATIC
peptide
(Fragment)
Hadrurin	Hadrurus	41	GILDTIKSIASKVWNSKTVQDLKRKGINWVAN
	aztecus		KLGVSPQAA
Hemiptericin	Pyrrhocoris	133	DVELKGKGGENEGFVGLKAQRNLYEDDRTS
	apterus		LSGTVKGQSQWKDPYPAQHAGMARLDGTR
			TLIENDRTKVTGSGFAQREVATGMRPHDSFG
			VGVEATHNIYKGKNGEVDVFGGVQRQWNTP
			DRHQARGGIRWRF
Hepcidin	Mus	83	MALSTRTQAACLLLLLLASLSSTTYLQQQMR
antimicrobial	musculus		QTTELQPLHGEESRADIAIPMQKRRKRDINFP
peptide 2			ICRFCCQCCNKPSCGICCEE
hepcidin	Danio rerio	91	MKLSNVFLAAVVILTCVCVFQITAVPFIQQVQ
antimicrobial			DEHHVESEELQENQHLTEAEHRLTDPLVLFR
peptide			TKRQSHLSLCRFCCKCCRNKGCGYCCKF
precursor
Hepcidin	Morone	85	MKTFSVAVAVAVVLAFICLQESSAVPVTEVQE
precursor	chrysops x		LEEPMSNEYQEMPVESWKMPYNNRHKRHS
	Morone		SPGGCRFCCNCCPNMSGCGVCCRF
	saxatilis
Hepcidin	Mus	83	MALSTRTQAACLLLLLLASLSSTTYLHQQMR
precursor	musculus		QTTELQPLHGEESRADIAIPMQKRRKRDTNF
			PICIFCCKCCNNSQCGICCKT
Hepcidin	Rattus	84	MALSTRIQAACLLLLLLASLSSGAYLRQQTRQ
precursor	norvegicus		TTALQPWHGAESKTDDSALLMLKRRKRDTN
			FPICLFCCKCCKNSSCGLCCIT
Hepcidin	Oncorhynchus	61	LQVLTEEVGSIDSPVGEHQQPGGESMRLPE
precursor	mykiss		HFRFKRXSHLSLCRWCCNCCHNKGXGFCCK
(Fragment)			F
Histone H2A	Bufo	39	AGRGKQGGKVRAKAKTRSSRAGLQFPVGRV
[Contains:	gargarizans		HRLLRKGNY
Buforin I;
Buforin II]
(Fragment)
Histone H2A	Hippoglossus	51	SGRGKTGGKARAKAKTRSSRAGLQFPVGRV
[Contains:	hippoglossus		HRLLRKGNYAHRVGAGAPVYL
Hipposin]
(Fragment)
Histone H2B-1	Ictalurus	20	PDPAKTAPKKGSKKAVTKXA
(Antibacterial	punctatus
histone-like
protein 1)
(HLP-1)
(Fragment)
Histone H2B-3	Ictalurus	17	PDPAKTAPKKKSKKAVT
(Antibacterial	punctatus
histone-like
protein 3)
(HLP-3)
(Fragment)
holotricin 1	Holotrichia	43	VTCDLLSLQIKGIAINDSACAAHCLAMRRKGG
	diomphalia		SCKQGVCVCRN
Holotricin 2	Holotrichia	127	MMKLVIALCLIGISAAYVVPVYYEIYPEDATFD
precursor	diomphalia		EADIEPQLSPAELHHGSIRERRSLQPGAPSFP
			MPGSQLPTSVSGNVEKQGRNTIATIDAQHKT
			DRYDVRGTWTKVVDGPGRSKPNFRIGGSYR
			W
holotricin 2	Holotrichia	127	MMKLVIALCLIGISAAYVVPVYYEIYPEDATFD
precursor	diomphalia		EADIEPQLSPAELHHGSIRERRSLQPGAPSLS
			QLPTSVSGNVEKQGRPMPGNTIATIDAQHKT
			DRYDVRGTVDGPGRSKPNFRIGGSWTKVYR
			W
Holotricin 3	Holotrichia	104	MNKLIILGLACIIAVASAMPYGPGDGHGGGHG
precursor	diomphalia		GGHGGGHGNGQGGGHGHGPGGGFGGGH
			GGGHGGGGRGGGGSGGGGSPGHGAGGG
			YPGGHGGGHHGGYQTHGY
Hymenoptaecin	Apis mellifera	129	MKFIVLVLFCAVAYVSAQAELEPEDTMDYIPT
precursor			RFRRQERGSIVIQGTKEGKSRPSLDIDYKQR
			VYDKNGMTGDAYGGLNIRPGQPSRQHAGFE
			FGKEYKNGFIKGQSEVQRGPGGRLSPYFGIN
			GGFRF
Indolicidin	Bos taurus	14	ILPWKWPWWPWRRX
Indolicidin	Bos taurus	144	MQTQRASLSLGRWSLWLLLLGLVVPSASAQ
precursor			ALSYREAVLRAVDQLNELSSEANLYRLLELDP
			PPKDNEDLGTRKPVSFTVKETVCPRTIQQPA
			EQCDFKEKGRVKQCVGTVTLDPSNDQFDLN
			CNELQSVILPWKWPWWPWRRG
Insect Defensin	Protophormia	40	ATCDLLSGTGINHSACAAHCLLRGNRGGYCN
A (NMR, 10	terraenovae		GKGVCVCRN
Structures) -
Chai
Interferon-	Mus sp.	15	SETAPAETPAPAKAE
activated
antimicrobial
protein
(Fragment)
Japonicin-1	Rana	14	FFPIGVFCKIFKTC
	japonica
Japonicin-2	Rana	21	FGLPMLSILPKALCILLKRKC
	japonica
Lactoferricin	Bos taurus	25	FKCRRWQWRMKKLGAPSITCVRRAF
lactoferrin	Sus scrofa	703	MKLFIPALLFLGTLGLCLAAPKKGVRWCVIST
precursor			AEYSKCRQWQSKIRRTNPMFCIRRASPTDCI
			RAIAAKRADAVTLDGGLVFEADQYKLRPVAA
			EIYGTEENPQTYYYAVAWKKGFNFQNQLQG
			RKSCHTGLGRSAGWNIPIGLLRRFLDWAGPP
			EPLQKAVAKFFSQSCVPCADGNAYPNLCQL
			CIGKGKDKCACSSQEPYFGYSGAFNCLHKGI
			GDVAFVKESTVFENLPQKADRDKYELLCPDN
			TRKPVEAFRECHLARVPSHAWARSVNGKE
			NSIWELLYQSQKKFGKSNPQEFQLFGSPGQ
			QKDLLFRDATIGFLKIPSKIDSKLYLGLPYLTAI
			QGLRETAAEVEARQAKVVWCAVGPEELRKC
			RQWSSQSSQNLNCSLASTTEDCIVQVLKGEA
			DAMSLDGGFIYTAGKCGLVPVLAENQKSRQS
			SSSDCVHRPTQGYFAVAWRKANGGITWNS
			VRGTKSCHTAVDRTAGWNIPMGLLVNQTGS
			CKFDEFFSQSCAPGSQPGSNLCALCVGNDQ
			GVDKCVPNSNERYYGYTGAFRCLAENAGDV
			AFVKDVTVLDNTNGQNTEEWARELRSDDFE
			LLCLDGTRKPVTEAQNCHLAVAPSHAWSRK
			EKAAQVEQVLLTEQAQFGRYGKDCPDKFCL
			FRSETKNLLFNDNTECLAQLQGKTTYEKYLG
			SEYVTAIANLKQCSVSPLLEACAFMMR
Lactotransferrin	Bos taurus	708	MKLFVPALLSLGALGLCLAAPRKNVRWCTIS
precursor			QPEWFKCRRWQWRMKKLGAPSITCVRRAF
(Lactoferrin)			ALECIRAIAEKKADAVTLDGGMVFEAGRDPY
[Contains:			KLRPVAAEIYGTKESPQTHYYAVAVVKKGSN
Lactoferricin B			FQLDQLQGRKSCHTGLGRSAGWIIPMGILRP
(LFCIN B)]			YLSWTESLEPLQGAVAKFFSASCVPCIDRQA
			YPNLCQLCKGEGENQCACSSREPYFGYSGA
			FKCLQDGAGDVAFVKETTVFENLPEKADRDQ
			YELLCLNNSRAPVDAFKECHLAQVPSHAWA
			RSVDGKEDLIWKLLSKAQEKFGKNKSRSFQL
			FGSPPGQRDLLFKDSALGFLRIPSKVDSALYL
			GSRYLTTLKNLRETAEEVKARYTRVVWCAVG
			PEEQKKCQQWSQQSGQNVTCATASTTDDCI
			VLVLKGEADALNLDGGYIYTAGKCGLVPVLAE
			NRKSSKHSSLDCVLRPTEGYLAVAWKKANE
			GLTWNSLKDKKSCHTAVDRTAGWNIPMGLIV
			NQTGSCAFDEFFSQSCAPGADPKSRLCALC
			AGDDQGLDKCVPNSKEKYYGYTGAFRCLAE
			DVGDVAFVKNDTVWENTNGESTADWAKNLN
			REDFRLLCLDGTRKPVTEAQSCHLAVAPNHA
			VVSRSDRAAHVKQVLLHQQALFGKNGKNCP
			DKFCLFKSETKNLLFNDNTECLAKLGGRPTY
			EEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
Lebocin 1/2	Bombyx mori	179	MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPP
precursor			TQRPIIRTARQAGQEPLWLYQGDNVPRAPST
			ADHPILPSKIDDVQLDPNRRYVRSVTNPENN
			EASIEHSHHTVDTGLDQPIESHRNTRDLRFLY
			PRGKLPVPTPPPFNPKPIYIDMGNRYRRHAS
			DDQEELRQYNEHFLIPRDIFQE
Lebocin 3	Bombyx mori	179	MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPP
precursor (LEB			TQRPITRTVRQAGQEPLWLYQGDNVPRAPS
3)			TADHPILPSKIDDVQLDPNRRYVRSVTNPENN
			EASIEHSHHTVDIGLDQPIESHRNTRDLRFLY
			PRGKLPVPTLPPFNPKPIYIDMGNRYRRHAS
			EDQEELRQYNEHFLIPRDIFQE
lectin-L6	Limulus	221	VQWHQIPGKLMHITATPHFLWGVNSNQQIYL
	polyphemus		CRQPCYDGQWTQISGSLKQVDADDHEVWG
			VNRNDDIYKRPVDGSGSVVVRVSGKLKHVSA
			SGYGYIWGVNSNDQIYKCPKPCNGAWTQVN
			GRLKQIDGGQSMVYGVNSANAIYRRPVDGS
			GSWQQISGSLKHITGSGLSEVFGVNSNDQIY
			RCTKPCSGQWSLIDGRLKQCDATGNTIVGVN
			SVDNIYRSG
Limulus factor	Tachypleus	394	MKVLLLVAFLLGTTLAYPQDDDGPVWGGSS
D	tridentatus		NDNDDGGISSRVGNPQSGFGNCECVPYYLC
			KDNNIIIDGSGLLDPRKKPVASKEPKLSARLG
			PEGPSGCGPFHVCCIAPETSTVKPYTHQCGF
			RNVNGINKRILSPNGKDLSEFGEWPWQGAVL
			KVEGKVNIFQCGAVLIDSYHLLTVAHCVYKFT
			LENAFPLKVRLGEWDTQNTNEFLKHEDYEVE
			KIYIHPKYDDERKNLWDDIAILKLKAEVSFGPH
			IDTICLPNNQEHFAGVQCVVTGWGKNAYKNG
			SYSNVLREVHVPVITNDRCQELLRKTRLSEW
			YVLYENFICAGGESNADSCKGDGGGPLTCW
			RKDGTYGLAGLVSWGINCGSPNVPGVYVRV
			SNYLDWITKITGRPISDYWPRS
Lingual	Bos taurus	64	MRLHHLLLALLFLVLSAGSGFTQGVRNSQSC
antimicrobial			RRNKGICVPIRCPGSMRQIGTCLGAQVKCCR
peptide			RK
precursor
Liver-	Bos taurus	77	MWHLKLFAVLMICLLLLAQVDGSPIPQQSSAK
expressed			RRPRRMTPFWRAVSLRPIGASCRDDSECITR
antimicrobial			LCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver-	Macaca	77	MWHLKLCAVLMIFLLLLGQTDGSPIPEVSSAK
expressed	mulatta		RRPRRMTPFWRGVSLRPIGASCRDDSECITR
antimicrobial			LCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver-	Mus	76	MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSAK
expressed	musculus		RSRRMTPFWRGVSLRPIGASCRDDSECITRL
antimicrobial			CRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver-	Sus scrofa	77	MWHLKLFAVLVICLLLAVQVHGSPIPELSSAK
expressed			RRPRRMTPFWRAVSLRPIGASCRDDSECLT
antimicrobial			RLCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver-	Cavia	71	SVVLLICLLLLGQVDGSPVPEKSSVKKRLRRM
expressed	porcellus		TPFWRGVSLRPIGASCRDDSECITRLCKKRR
antimicrobial			CSLSVAQE
peptide 2
precursor
(LEAP-2)
(Fragment)
Liver-	Sus scrofa	77	MWHLKLFAVLVICLLLAVQVHGSPIPELSSAK
expressed			RRPRRITPFWRAVSLRPIGASCRDDSECLTR
antimicrobial			LCRKRRCSLSVAQE
protein 2
Lysozyme	Heliothis	141	MQKLTLFVVALAAVVLHCEAKQFSRCGLVQE
	virescens		LRRQGFPEDKLGDWVCLVENESARKTDKVG
			TVNKNGSRDYGLYQINDKYWCSNTSTPGKD
			CNVTCAEMLLDDITKASTCAKKIYKRHKFEAW
			YGWKNHCKGKTLPDISNC
lysozyme (EC	Alopochen	129	KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
3.2.1.17)	aegyptiacus		AAKYESGFNTQATNRNTDGSTDYGILQINSR
			WWCNDGKTPRAKNVCGIPCSVLLRSDITEAV
			KCAKRIVSDGNGMNAWVAWRNRCKGTDVS
			QWIRGCRL
lysozyme (EC	Chrysolophus	129	KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
3.2.1.17)	pictus		AAKFESNFNTHATNRNTDGSTDYGILQINSR
			WWCNDGRTPGSRNLCHIPCSALLSSDITASV
			NCAKKIVSDGNGMNAWVAWRNRCKGTDVN
			AWTRGCRL
lysozyme (EC	Lophophorus	129	KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
3.2.1.17)	impejanus		AAKFESNFNTHATNRNTDGSTDYGILQINSR
			WWCNDGRTPGSRNLCNIPCSALLSSDITASV
			NCAKKIVSDGNGMNAVWAWRNRCKGTDVH
			AWIRGCRL
lysozyme (EC	Manduca	120	KHFSRCELVHELRRQGFPENLMRDWVCLVE
3.2.1.17)	sexta		NESSRYTDKVGRVNKNGSRDYGLFQINDKY
			WCSNGSTPGKDCNVKCSDLLIDDITKASTCA
			KKIYKRHKFQAWYGWRNHCQGSLPDISSC
lysozyme (EC	Ovis aries	129	KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 1			TKWESSYNTKATNYNPGSESTDYGIFQINSK
			WWCNDGKTPNAVDGCHVSCSELMENNIAKA
			VACAKHIVSEQGITAWVAWKSHCRDHDVSS
			YVEGCSL
lysozyme (EC	Rattus	148	MKALLVLGFLLLSASVQAKIYERCEFARTLKR
3.2.1.17) 1	norvegicus		NGMSGYYGVSLADWVCLAQHESNYNTQAR
precursor			NYNPGDQSTDYGIFQINSRYWCNDGKTPRA
			KNACGIPCSALLQDDITQAIQCAKRVVRDPQ
			GIRAWVAWQRHCKNRDLSGYIRNCGV
lysozyme (EC	Bos taurus	129	KTFKRCELARTLKNLGLAGYKGVSLANWMCL
3.2.1.17) 14d,			AKGESNYNTQAKNYNPGSKSTDYGIFQINSK
tracheal			WWCNDGKTPKAVNGCGVSCSALLKDDITQA
			VACAKKIVSQQGITAWVAWKNKCRNRDLTSY
			VKGCGV
lysozyme (EC	Cervus axis	129	KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 2			TKWESSYNTKATNYNPGSESTDYGIFQINSK
			WWCNDGKTPNAVDGCHVACSELMENDIAKA
			VACAKQIVREQGITAWVAWKSHCRDHDVSS
			YVEGCTL
lysozyme (EC	Ovis aries	129	KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 2			TKWESSYNTKATNYNPGSESTDYGIEQINSK
			WWCNDGKTPNAVDGCHVSCSALMENDIEKA
			VACAKHIVSEQGITAWVAWKSHCRDHDVSS
			YVEGCTL
lysozyme (EC	Ovis aries	129	KVFERCELARTLKKLGLDDYKGVSLANWLCL
3.2.1.17) 3			TKWESGYNTKATNYNPGSESTDYGIEQINSK
			WWCNDGKTPNAVDGCHVSCSALMENDIEKA
			VACAKHIVSEQGITAWVAWKSHCRDHDVSS
			YVEGCTL
lysozyme (EC	Bos taurus	130	KVFERCELARSLKRFGMDNFRGISLANWMCL
3.2.1.17) 5a,			ARWESNYNTQATNYNAGDQSTDYGIEQINSH
tracheal			WWCNDGKTPGAVNACHLPCGALLQDDITQA
			VACAKRWSDPQGIRAWVAWRSHCQNQDLT
			SYIQGCGV
lysozyme (EC	Drosophila	140	MKAFIVLVALASGAPALGRTMDRCSLAREMS
3.2.1 .17) B	melanogaster		NLGVPRDQLARWACIAEHESSYRTGVVGPE
precursor			NYNGSNDYGIFQINDYYWCAPPSGRFSYNE
			CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
			WSTWHYCSGWLPSIDDCF
lysozyme (EC	Papio sp.	130	KIFERCELARTLKRLGLDGYRGISLANWVCLA
3.2.1.17) c			KWESDYNTQATNYNPGDQSTDYGIEQINSHY
			WCNDGKTPGAVNACHISCNALLQDNITDAVA
			CAKRVVSDPQGIRAWVAWRNHCQNRDVSQ
			YVQGCGV
lysozyme (EC	Numida	129	KVFGRCELAAAMKRHGLDNYRGYSLGNWVC
3.2.1.17) c	meleagris		AAKFESNFNSQATNRNTDGSTDYGVLQINSR
[validated]			WWCNDGRTPGSRNLCNIPCSALQSSDITATA
			NCAKKIVSDGDGMNAWVAWRKHCKGTDVR
			VWIKGCRL
lysozyme (EC	Coturnix	129	KVYGRCELAAAMKRHGLDKYQGYSLGNWV
3.2.1.17) C	japonica		CAAKFESNFNTQATNRNTDGSTDYGILQINS
precursor			RWWCNDGRTPGSRNLCNIPCSALLSSDITAS
			VNCAKKIVSDVHGMNAWVAWRNRCKGTDV
			NVWIRGCRL
lysozyme (EC	Hyalophora	132	CRSWQFALHCDAKRFTRCGLVQELRRRGFD
3.2.1.17) c	cecropia		ETLMSNWVCLVENESGRFTDKIGKVNKNGS
precursor			RDYGLFQINDKYWCSKGSTPGKDCNVTCNQ
			LLTDDISVAATCAKKIYKRHKFDAWYGWKNH
			CQHGLPDISDC
lysozyme (EC	Phasianus	147	MRSLLILVLCFLPLAAPGKVYGRCELAAAMKR
3.2.1.17) c	colchicus		MGLDNYRGYSLGNVWCAAKFESNFNTGATN
precursor			RNTDGSTDYGILQINSRWWCNDGRTPGSKN
[validated]			LCHIPCSALLSSDITASVNCAKKIVSDGDGMN
			AWVAWRKHCKGTDVNVWIRGCRL
lysozyme (EC	Drosophila	140	MKAFIVLVALALAAPALGRTLDRCSLAREMSN
3.2.1.17) E	melanogaster		LGVPRDQLARWACIAEHESSYRTGWGPEN
precursor			YNGSNDYGIFQINDYYWCAPPSGRFSYNEC
			GLSCNALLTDDITHSVRCAQKVLSQQGWSA
			WSTWHYCSGWLPSIDDCF
lysozyme (EC	Rhea	185	RTNCYGDVSRIDTTGASCKTAKPEKLNYCGV
3.2.1.17) g	americana		AASRKIAERDLRSMDRYKTLIKKVGQKLCVEP
			AVIAGIISRESHAGKALKNGWGDNGNGFGLM
			QVDRRSHKPVGEWNGERHLIQGTEILISMIKA
			MQRKFPRWTKEQQLKGGISAYNAGPGNVRT
			YERMDIGTTHDDYANDVVARAQYYKQHGY
lysozyme (EC	Casuarius	185	QTGCYGWNRIDTTGASCETAKPEKLNYCGV
3.2.1.17) g	casuarius		AASRKIAEGDLQSMDRYKTLIKKVGQKLCVD
[validated]			PAVIAGIISRESHAGKALKDGWGDNGNGFGL
			MQVDKRSHTPVGKWNGERHLTQGTEILISMI
			KKIQKKFPRWTKEQQLKGGISAYNAGSGNVR
			TYERMDIGTTHNDYANDVVARAQYYKQHGY
lysozyme (EC	Drosophila	140	MKAFIVLVALACAAPAFGRTMDRCSLAREMS
3.2.1.17)	melanogaster		NLGVPRDQLNKWACIAEHESSYRTGVVGPE
precursor			NYNGSNDYGIFQINDYYWCAPPSGRFSYNE
			CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
			WSTWHYCSGWLPSIDDCF
lysozyme (EC	Opisthocomus	145	MLFFGFLLAFLSAVPGTEGEIISRCELVKILRE
3.2.1.17)	hoazin		HGFEGFEGTTIADWICLVQHESDYNTEAYNN
precursor,			NGPSRDYGIFQINSKYWCNDGKTSGAVDGC
stomach			HISCSELMTNDLEDDIKCAKKIARDAHGLTPW
			YGWKNHCEGRDLSSYVKGC
lysozyme (EC	Drosophila	139	MKAFFALVLLPLPLCLAGRTLDRCSLAREMA
3.2.1.17) S	melanogaster		DLGVPRDQLDKWTCIAQHESDYRTWVVGPA
precursor			NSDGSNDYGIFQINDLYWCQADGRFSYNEC
			GLSCNALLTDDITNSVRCAQKVLSQQGWSA
			WAVWHYCSGWLPSIDECF
lysozyme (EC	Drosophila	81	PNTDGSNDYGIFQINDLYWCQPSSGKFSHN
3.2.1.17) X	melanogaster		GCDVSCNALLTDDIKSSVRCALKVLGQQGW
			SAWSTWHYCSGYLPPIDDCFV
Lysozyme	Drosophila	140	MKAFIVLVALACAAPAFGRTMDRCSLAREMS
A/C/D	melanogaster		NLGVPRDQLARWACIAEHESSYRTGVVGPE
precursor (EC			NYNGSNDYGIFQINDYYWCAPPSGRFSYNE
3.2.1.17) (1,4-			CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
beta-N-			WSTWHYCSGWLPSIDDCF
acetylmurami-
dase A/C)
Lysozyme C	Callipepla	129	KVFGRCELAAAMKRHGLDNYRGYSLGNWVC
(EC 3.2.1.17)	californica		AAKFESNFNSQATNRNTDGSTDYGVLQINSR
(1,4-beta-N-			WWCNDGRTPGSRNLCNIPCSALLSSDITATV
acetylmurami-			NCAKKIVSDGNGMNAWVAWRNRCKGTDVH
dase C)			AWIRGCRL
Lysozyme C	Colinus	130	MKVFGRCELAAAMKRHGLDNYRGYSLGNW
(EC 3.2.1.17)	virginianus		VCAAKFESNFNSQATNRNTDGSTDYGVLQIN
(1,4-beta-N-			SRWWCNDGKTPGSRNLCNIPCSALLSSDITA
acetylmurami-			TVNCAKKIVSDGNGMNAWVAWRNRCKGTD
dase C)			VQAWIRGCRL
Lysozyme C	Columba livia	127	KDIPRCELVKILRRHGFEGFVGKTVANWVCL
(EC 3.2.1.17)			VKHESGYRTTAFNNNGPNSRDYGIFQINSKY
(1,4-beta-N-			WCNDGKTRGSKNACNINCSKLRDDNIADDIQ
acetylmurami-			CAKKIAREARGLTPWVAWKKYCQGKDLSSY
dase C)			VRGC
Lysozyme C	Equus asinus	129	KVFSKCELAHKLKAQEMDGFGGYSLANWVC
(EC 3.2.1.17)			MAEYESNFNTRAFNGKNANGSYDYGLFQLN
(1,4-beta-N-			SKWWCKDNKRSSSNACNIMCSKLLDDNIDD
acetylmurami-			DISCAKRVVRDPKGMSAWKAWVKHCKDKDL
dase C)			SEYLASCNL
Lysozyme C	Ortalis vetula	129	KIYKRCELAAAMKRYGLDNYRGYSLGNWVC
(EC 3.2.1.17)			AARYESNYNTQATNRNSNGSTDYGILQINSR
(1,4-beta-N-			WWCNDGRTPGTKNLCHISCSALMGADIAPS
acetylmurami-			VRCAKRIVSDGDGMNAWVAWRKHCKGTDV
dase C)			STWIKDCKL
Lysozyme C	Oryctolagus	130	KIYERCELARTLKKLGLDGYKGVSLANWMCL
(EC 3.2.1.17)	cuniculus		AKWESSYNTRATNYNPGDKSTDYGIFQINSR
(1,4-beta-N-			YWCNDGKTPRAVNACHIPCSDLLKDDITQAV
acetylmurami-			ACAKRWSDPQGIRAWVAWRNHCQNQDLTP
dase C)			YIRGCGV
Lysozyme C	Syrmaticus	129	KVYGRCELAAAMKRLGLDNFRGYSLGNWVC
(EC 3.2.1.17)	soemmerringii		AAKFESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N-			WWCNDGRTPGSRNLCNIPCSALLSSDTIASV
acetylmurami-			NCAKKIVSDGNGMNAWVAWRKRCKGTDVN
dase C) (CPL)			AWTRGCRL
Lysozyme C	Felis catus	20	KIFTKCELARKLRAEGMDGF
(EC 3.2.1.17)
(1,4-beta-N-
acetylmurami-
dase C)
(Fragment)
Lysozyme C	Pseudocheirus	49	SKMKKCEFAKIAKEQHMDGYHGVSLADWVC
(EC 3.2.1.17)	peregrinus		LVNNESDFNTKAINRNKGI
(1,4-beta-N-
acetylmurami-
dase C)
(Fragment)
Lysozyme C	Lophura	129	KVYGRCELAAAMKRLGLDNYRGYSLGNWVNC
(EC 3.2.1.17)	leucomelanos		AAKYESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N-			WWCNDGKTPGSRNLCHIPCSALLSSDITASV
acetylmurami-			NCAKKIVSDGNGMNAWVAWRNRCKGTDVS
dase)			VWTRGCRL
Lysozyme C	Pavo	129	KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
(EC 3.2.1.17)	cristatus		AAKFESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N-			WWCNDGRTPGSRNLCNIPCSALLSSDITASV
acetylmurami-			NCAKKIVSDRNGMNAWVAWRNRCKGTDVH
dase)			AWIRGCRL
Lysozyme C	Phasianus	130	GKVYGRCELAAAMKRMGLDNYRGYSLGNW
(EC 3.2.1.17)	versicolor		VCAAKFESNFNTGATNRNTDGSTDYGILQIN
(1,4-beta-N-			SRWWCNDGRTPGSKNLCHIPCSALLSSDITA
acetylmurami-			SVNCAKKIVSDGDGMNAWVAWRKHCKGTD
dase)			VNVWIRGCRL
Lysozyme C	Syrmaticus	129	KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
(EC 3.2.1.17)	reevesi		AAKFESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N-			WWCNDGRTPGSRNLCHISCSALLSSDITASV
acetylmurami-			NCAKKIVSDRNGMNAWVAWRNRCKGTDVN
dase)			AWIRGCRL
Lysozyme C 1	Cervus axis	129	KVFERCELARTLKELGLDGYKGVSLANWLCL
and 2 (EC			TKWESSYNTKATNYNPGSESTDYGIFQINSK
3.2.1.17) (1,4-			WWCDDGKTPNAVDGCHVACSELMENNIDKA
beta-N-			VTCAKQIVREQGITAWVAWKSHCRGHDVSS
acetylmurami-			YVEGCTL
dase C)
Lysozyme C 1	Bos taurus	147	MKALIILGFLFLSVAVQGKVFERCELARTLKKL
precursor (EC			GLDGYKGVSLANWLCLTKWESSYNTKATNY
3.2.1.17) (1,4-			NPGSESTDYGIFQINSKWWCNDGKTPNAVD
beta-N-			GCHVSCSELMENDIAKAVACAKQIVSEQGITA
acetylmurami-			WVAWKSHCRDHDVSSYVEGCTL
dase C)
Lysozyme C 2	Bos taurus	147	MKALVILGFLFLSVAVQGKVFERCELARTLKK
precursor (EC			LGLDGYKGVSLANWLCLTKWESSYNTKATN
3.2.1.17) (1,4-			YNPSSESTDYGIFQINSKWWCNDGKTPNAV
beta-N-			DGCHVSCSELMENDIAKAVACAKHIVSEQGIT
acetylmurami-			AWVAWKSHCRDHDVSSYVEGCTL
dase C)
Lysozyme C 3	Bos taurus	147	MKALIILGFLFLSVAVQGKVFERCELARTLKKL
precursor (EC			GLDGYKGVSLANWLCLTKWESSYNTKATNY
3.2.1.17) (1,4-			NPSSESTDYGIFQINSKWWCNDGKTPNAVD
beta-N-			GCHVSCSELMENDIAKAVACAKHIVSEQGITA
acetylmurami-			WVAWKSHCRDHDVSSYVQGCTL
dase C)
Lysozyme C I	Tachyglossus	125	KILKKQELCKNLVAQGMNGYQHITLPNWVCT
(EC 3.2.1.17)	aculeatus		AFHESSYNTRATNHNTDGSTDYGILQINSRY
(1,4-beta-N-			WCHDGKTPGSKNACNISCSKLLDDDITDDLK
acetylmurami-			CAKKIAGEAKGLTPWVAWKSKCRGHDLSKF
dase C)			KC
Lysozyme C II	Oncorhynchus	144	MRAVVVLLLVAVASAKVYDRCELARALKASG
precursor (EC	mykiss		MDGYAGNSLPNWVCLSKWESSYNTQATNR
3.2.1.17) (1,4-			NTDGSTDYGIFQINSRYWCDDGRTPGAKNV
beta-N-			CGIRCSQLLTADLTVAIRCAKRWLDPNGIGA
acetylmurami-			WVAWRLHCQNQDLRSYVAGCGV
dase C)
Lysozyme C	Coturnix	147	MRSLLVLVLCFLPLAALGKVYGRCELAAAMK
precursor (EC	japonica		RHGLDKYQGYSLGNWVCAAKFESNFNTQAT
3.2.1.17) (1,4-			NRNTDGSTDYGILQINSRWWCNDGRTPGSR
beta-N-			NLCNIPCSALLSSDITASVNCAKKIVSDVHGM
acetylmurami-			NAWVAWRNRCKGTDVNAWIRGCRL
dase C)
Lysozyme C	Meleagris	147	MRSLLILVLCFLPLAALGKVYGRCELAAAMKR
precursor (EC	gallopavo		LGLDNYRGYSLGNWVCAAKFESNFNTHATN
3.2.1.17) (1,4-			RNTDGSTDYGILQINSRWWCNDGRTPGSKN
beta-N-			LCNIPCSALLSSDITASVNCAKKIASGGNGMN
acetylmurami-			AWVAWRNRCKGTDVHAWIRGCRL
dase C)
Lysozyme C	Presbytis	148	MKALTILGLVLLSVTVQGKIFERCELARTLKKL
precursor (EC	entellus		GLDGYKGVSLANWVCLAKWESGYNTEATNY
3.2.1.17) (1,4-			NPGDESTDYGIFQINSRYWCNNGKTPGAVD
beta-N-			ACHISCSALLQNNIADAVACAKRVVSDPQGIR
acetylmurami-			AWVAWRNHCQNKDVSQYVKGCGV
dase C)
Lysozyme C	Gallus gallus	147	MRSLLILVLCFLPLAALGKVFGRCELAAAMKR
precursor (EC			HGLDNYRGYSLGNWVCAAKFESNFNTQATN
3.2.1.17) (1,4-			RNTDGSTDYGILQINSRWWCNDGRTPGSRN
beta-N-			LCNIPCSALLSSDITASVNCAKKIVSDGNGMN
acetylmurami-			AWVAWRNRCKGTDVQAWIRGCRL
dase C)
(Allergen Gal d
4) Gal d IV)
Lysozyme C,	Rattus	148	MKALLVLGFLLLSASVQAKVFKHCELARILRS
type 2	norvegicus		SALAGYRGVSLENWMCMAQHESNFDTEAIN
precursor (EC			YNSTDQSTDYGIFQINSRYWCNDGKTPRAVN
3.2.1.17) (1,4-			AGGIPCSALLQDDITQAIQCAKRVVRDPQGIR
beta-N-			AWVAWQRHCQNRDLSGYIRNCGV
acetylmurami-
dase C)
Lysozyme C,	Mus	148	MKTLLTLGLLLLSVTAQAKVYERCEFARTLKR
type M	musculus		NGMAGYYGVSLADWVCLAQHESNYNTRATN
precursor (EC			YNRGDQSTDYGIFQINSRYWCNDGKTPRAV
3.2.1.17) (1,4-			NACGINCSALLQDDITAAIQCAKRWRDPQGI
beta-N-			RAWVAWRAHCQNRDLSQYIRNCGV
acetylmurami-
dase C)
Lysozyme C,	Mus	148	MKALLTLGLLLLSVTAQAKVYNRCELARILKR
type P	musculus		NGMDGYRGVKLADWVCLAQHESNYNTRAT
precursor (EC			NYNRGDRSTDYGIFQINSRYWCNDGKTPRS
3.2.1.17) (1,4-			KNACGINCSALLQDDITAAIQCAKRVVRDPQG
beta-N-			IRAWVAWRTQCQNRDLSQYIRNCGV
acetylmurami-
dase C)
Lysozyme C-1	Anas	147	MKALLTLVFCLLPLAAQGKVYSRCELAAAMK
precursor (EC	platyrhynchos		RLGLDNYRGYSLGNWVCAANYESGFNTQAT
3.2.1.17) (1,4-			NRNTDGSTDYGILQINSRWWCDNGKTPRSK
beta-N-			NACGIPCSVLLRSDITEAVRCAKRIVSDGDGM
acetylmurami-			NAWVAWRNRCRGTDVSKWIRGCRL
dase C)
Lysozyme C-3	Anas	129	KVYERCELAAAMKRLGLDNYRGYSLGNWVC
(EC 3.2.1.17)	platyrhynchos		AANYESSFNTQATNRNTDGSTDYGILEINSR
(1,4-beta-N-			WWCDNGKTPRAKNACGIPCSVLLRSDITEAV
acetylmurami-			KCAKRIVSDGDGMNAWVAWRNRCKGTDVS
dase)			RWIRGCRL
Lysozyme G	Anser anser	185	RTDCYGNVNRIDTTGASCKTAKPEGLSYCGV
(EC 3.2.1.17)			SASKKIAERDLQAMDRYKTIIKKVGEKLCVEP
(1,4-beta-N-			AVIAGIISRESHAGKVLKNGWGDRGNGFGLM
acetylmurami-			QVDKRSHKPQGTWNGEVHITQGTTILINFIKTI
dase) (Goose-			QKKFPSWTKDQQLKGGISAYNAGAGNVRSY
type lysozyme)			ARMDIGTTHDDYANDVVARAQYYKQHGY
Lysozyme G	Cygnus	185	RTDCYGNVNRIDTTGASCKTAKPEGLSYCGV
(EC 3.2.1.17)	atratus		PASKTIAERDLKAMDRYKTIIKKVGEKLCVEP
(1,4-beta-N-			AVIAGIISRESHAGKVLKNGWGDRGNGFGLM
acetylmurami-			QVDKRSHKPQGTWNGEVHITQGTTILTDFIK
dase) (Goose-			RIQKKFPSWTKDQQLKGGISAYNAGAGNVRS
type lysozyme)			YARMDIGTTHDDYANDVVARAQYYKQHGY
Lysozyme G	Struthio	185	RTGCYGDVNRVDTTGASCKSAKPEKLNYCG
(EC 3.2.1.17)	camelus		VAASRKIAERDLQSMDRYKALIKKVGQKLCV
(1,4-beta-N-			DPAVIAGIISRESHAGKALRNGWGDNGNGFG
acetylmurami-			LMQVDRRSHKPVGEWNGERHLMQGTEILIS
dase) (Goose-			MIKAIQKKFPRWTKEQQLKGGISAYNAGPGN
type lysozyme)			VRSYERMDIGTTHDDYANDVVARAQYYKQH
			GY
Lysozyme G	Gallus gallus	211	MLGKNDPMCLVLVLLGLTALLGICQGGTGCY
precursor (EC			GSVSRIDTTGASCRTAKPEGLSYCGVRASRT
3.2.1.17) (1,4-			IAERDLGSMNKYKVLIKRVGEALCIEPAVIAGII
beta-N-			SRESHAGKILKNGWGDRGNGFGLMQVDKRY
acetylmurami-			HKIEGTWNGEAHIRQGTRILIDMVKKIQRKFP
dase) (Goose-			RWTRDQQLKGGISAYNAGVGNVRSYERMDI
type lysozyme)			GTLHDDYSNDVVARAQYFKQHGY
Lysozyme P	Drosophila	141	MKAFLVICALTLTAVATQARTMDRCSLAREM
precursor (EC	melanogaster		SKLGVPRDQLAKWTCIAQHESSFRTGVVGPA
3.2.1.17) (1,4-			NSNGSNDYGIFQINNKYWCKPADGRFSYNE
beta-N-			CGLSCNALLTDDITNSVKCARKIQRQQGWTA
acetylmurami-			WSTWKYCSGSLPSINSCF
dase P)
Lysozyme	Chlamys	137	MMYFVLLCLLATGTTYGAHNFATGIVPQSCL
precursor	islandica		ECICKTESGCRAIGCKFDVYSDSCGYFQLKQ
			AYWEDCGRPGGSLTSCADDIHCSSQCVQHY
			MSRYIGHTSCSRTCESYARLHNGGPHGCEH
			GSTLGYWGHVQGHGC
Lysozyme	Bombyx mori	137	MQKLIIFALWLCVGSEAKTFTRCGLVHELRK
precursor (EC			HGFEENLMRNWVCLVEHESSRDTSKTNTNR
3.2.1.17) (1,4-			NGSKDYGLFQINDRYWCSKGASPGKDCNVK
beta-N-			CSDLLTDDITKAAKCAKKIYKRHRFDAWYGW
acetylmurami-			KNHCQGSLPDISSC
dase)
Lysozyme	Hyalophora	139	MTKYVILLAVLAFALHCDAKRFTRCGLVQELR
precursor (EC	cecropia		RLGFDETLMSNWVCLVENESGRFTDKIGKVN
3.2.1.17) (1,4-			KNGSRDYGLFQINDKYWCSKGTTPGKDCNV
beta-N-			TCNQLLTDDISVAATCAKKIYKRHKFDAWYG
acetylmurami-			WKNHCQHGLPDISDC
dase)
Maculatin 1.1	Litoria	21	GLFGVLAKVAAHVVPAIAEHF
[Contains:	genimaculata
Maculatin
1.1.1]
Maculatin 1.2	Litoria	23	GLFGVLAKVASHVVPAIAEHFQA
	genimaculata
Maculatin 2.1	Litoria	18	GFVDFLKKVAGTIANVVT
	genimaculata
Maculatin 3.1	Litoria	26	GLLQTIKEKLESLESLAKGIVSGIQA
	genimaculata
Magainins	Xenopus	303	MFKGLFICSLIAVICANALPQPEASADEDMDE
precursor	laevis		REVRGIGKFLHSAGKFGKAFVGEIMKSKRDA
			EAVGPEAFADEDLDEREVRGIGKFLHSAKKF
			GKAFVGEIMNSKRDAEAVGPEAFADEDLDER
			EVRGIGKFLHSAKKFGKAFVGEIMNSKRDAE
			AVGPEAFADEDLDEREVRGIGKFLHSAKKFG
			KAFVGEIMNSKRDAEAVGPEAFADEDFDERE
			VRGIGKFLHSAKKFGKAFVGEIMNSKRDAEA
			VGPEAFADEDLDEREVRGIGKFLHSAKKFGK
			AFVGEIMNSKRDAEAVDDRRWVE
Melittin-like	Rana	22	FIGSALKVLAGVLPSIVSWVKQ
peptide (MLP)	temporaria
Metchnikowin	Drosophila	52	MQLNLGAIFLALLGVMATTTSVLAEPHRRQG
	melanogaster		PIFDTRPSPFNPNQPRPGPIY
Metchnikowin	Drosophila	52	MQLNLGAIFLALLGVMATATSVLAEPHRHQG
precursor	melanogaster		PIFDTRPSPFNPNQPRPGPIY
MGD1	Mytilus	57	CPNNYQCHRHCKSIPGRCGGYCGGWHRLR
antimicrobial	galloprovincialis		CTCYRCGGRREDVEDIEDIFDNEAADRF
peptide
(Fragment)
Misgurin	Misgurnus	21	RQRVEELSKFSKKGAAARRRK
	anguillicaudatus
Moricin 1	Bombyx mori	66	MNILKFFFVFIVAMSLVSCSTAAPAKIPIKAIKT
precursor			VGKAVGKGLRAINIASTANDVENFLKPKKRKH
Moricin 2	Bombyx mori	66	MNILKLFFVFIVAMSLVSCSTAAPAKIPIKAIKT
precursor			VGKAVGKGLRAINIASTANDVENFLKPKKRKH
myeloid	Ovis aries	160	METQRASLSLGRRSLWLLLLGLVLASARAQA
antimicrobial			LSYREAVLRAVDQLNEKSSEANLYRLLELDP
peptide 29			PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
precursor			AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
			CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
			RIAG
Myeloid	Ovis aries	165	METQRAGLSLGRWSLRLLLLGLVLPSASTRS
antimicrobial			FSYREAVLRAVDQFNERSAEANLYRLLELDP
peptide			PPEQDAEDRGARKPVSFKVKETVCPRTSQQ
precursor			PVEQCDFRKNGLVKQCVGTVTRYWIRGDFDI
			TCKDIQNVGLFGRLRDSLQRGGQKILEKAERI
			GDRIKDIFRG
Myticin A	Mytilus	96	MKATILLAVLVAVFVAGTEAHSHACTSYWCG
precursor	galloprovincialis		KFCGTASCTHYLCRVLHPGKMCACVHCSRV
			NNPFRVNQVAKSINDLDYTPIMKSMENLDNG
			MDML
Myticin B	Mytilus	96	MKATMLLAVVVAVFVAGTEAHPHVCTSYYCS
precursor	galloprovincialis		KFCGTAGCTRYGCRNLHRGKLCFCLHCSRV
			KFPFGATQDAKSMNELEYTPIMKSMENLDNG
			MDML
Mytilin A	Mytilus edulis	34	GCASRCKAKCAGRRCKGWASASFRGRCYC
			KCFRC
Mytilin B	Mytilus edulis	34	SCASRCKGHCRARRCGYYVSVLYRGRCYCK
			CLRC
Mytilin B	Mytilus	103	MKAAVILAIALVAILAVHEAEASCASRCKGHC
antimicrobial	galloprovincialis		RARRCGYYVSVLYRGRCYCKCLRCSSEHSM
peptide			KFPENEGSSPSDMMPQMNENENTEFGQDM
precursor			PTGETEQGETGI
Mytimycin	Mytilus edulis	33	DCCRKPFRKHCWDCTAGTPYYGYSTRNIFG
(Fragment)			CTC
Neutrophil	Rattus	94	MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQ
antibiotic	norvegicus		EQLVMEDQDISISFGGDKGTALQDADVKAGV
peptide NP-1			TCYCRRTRCGFRERLSGACGYRGRIYRLCC
precursor			R
(Neutrophil
defensin 1)
(RatNP-1)
Neutrophil	Rattus	94	MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQ
antibiotic	norvegicus		EQLVMEDQDISISFGGDKGTALQDADVKAGV
peptide NP-2			TCYCRSTRCGFRERLSGACGYRGRIYRLCC
precursor			R
(Neutrophil
defensin 2)
(RatNP-2)
Neutrophil	Rattus	87	MRTLTLLTTLLLLALHTQAESPQGSTKEAPDE
antibiotic	norvegicus		EQDISVFFGGDKGTALQDAAVKAGVTCSCRT
peptide NP-3			SSCRFGERLSGACRLNGRIYRLCC
precursor
(Neutrophil
defensin 3)
(RatNP-3a)
Neutrophil	Rattus	87	MRTLILLTTLLLLALHTQAESPQGSTKEAPDE
antibiotic	norvegicus		EQDISVFFGGDKGTALQDAAVKAGVTCSCRT
peptide NP-3			SSCRFGERLSGACRLNGRIYRLCC
precursor
(Neutrophil
defensin 3)
(RatNP-3b)
Neutrophil	Oryctolagus	95	MRTLALLAAILLVTLQAQAELHSGMADDGVD
antibiotic	cuniculus		QQQPRAQDLDVAVYIKQDETSPLEVLGAKAG
peptide NP-4			VSCTCRRFSCGFGERASGSCTVNGVRHTLC
precursor			CRR
(Microbicidal
peptide NP-4)
Neutrophil	Rattus	93	MRTLTLLITLLLLALHTQAESPQERAKAAPDQ
antibiotic	norvegicus		DMVMEDQDIFISFGGYKGTVLQDAVVKAGQA
peptide NP-4			CYCRIGACVSGERLTGACGLNGRIYRLCCR
precursor
(Neutrophil
defensin 4)
(RatNP-4)
Neutrophil	Oryctolagus	95	MRTLALLAAILLVTLQAQAELHSGMADDGVD
antibiotic	cuniculus		QQQPRAQDLDVAVYIKQDETSPLEVLGAKAG
peptide NP-5			VFCTCRGFLCGSGERASGSCTINGVRHTLCC
precursor			RR
(Microbicidal
peptide NP-5)
neutrophil beta-	Bos taurus	60	MRLHHLLLALLFLVLSAASGISGPLSCGRNGG
defensin 12			VCIPIRCPVPMRQIGTCFGRPVKCCRSW
neutrophil beta-	Bos taurus	54	MRLHHLLLVLLFLVLSAGSGFTQWRNPQSC
defensin 5			RWNMGVCIPISCPGNMRQIGTCS
Neutrophil	Cavia	178	MGTPRDAASGGPRLLLPLLLLLLLTPATAWVL
cationic	porcellus		SYQQAVQRAVDGINKNLADNENLFRLLSLDT
antibacterial			QPPGDNDPYSPKPVSFTIKETVCTKMLQRPL
polypeptide of			EQCDFKENGLVQRCTGTVTLDSAFNVSSLSC
11 kDa			LGGRRFRRMVGLRKKFRKTRKRIQKLGRKIG
			KTGRKVWKAWREYGQIPYPCRI
Neutrophil	Cavia	93	MRTVPLFAACLLLTLMAQAEPLPRAADHSDT
cationic peptide	porcellus		KMKGDREDHVAVISFWEEESTSLEDAGAGA
1 precursor			GRRCICTTRTCRFPYRRLGTCIFQNRVYTFC
(Neutrophil			C
defensin)
(GPNP)
(Corticostatic
peptide GP-
CS1) (CP-1)
Neutrophil	Cavia	93	MRTVPLFAACLLLTLMAQAEPLPRAADHSDT
cationic peptide	porcellus		KMKGDREDHVAVISFWEEESTSLQDAGAGA
1B precursor			GRRCICTTRTCRFPYRRLGTCIFQNRVYTFC
(Neutrophil			C
defensin) (CP-
1B) (GNCP)
Neutrophil	Cavia	93	MRTVPLFAACLLLTLMAQAEPLPRAADHSDT
cationic peptide	porcellus		KMKGDREDHVAVISFWEEESTSLQDAGAGA
2 precursor			GRRCICTTRTCRFPYRRLGTCLFQNRVYTFC
(CP-2) (GNCP)			C
(GNCP-2)
Neutrophil	Mesocricetus	33	VTCFCRRRGCASRERHIGYCRFGNTIYRLCC
defensin 1	auratus		RR
(HANP-1)
Neutrophil	Mesocricetus	31	CFCKRPVCDSGETQIGYCRLGNTFYRLCCR
defensin 2	auratus		Q
(HANP-2)
Neutrophil	Macaca	30	ACYCRIPACLAGERRYGTCFYMGRVWAFCC
defensin 2	mulatta
(RMAD-2)
Neutrophil	Mesocricetus	33	VTCFCRRRGCASRERLIGYCRFGNTIYGLCC
defensin 3	auratus		RR
(HANP-3)
Neutrophil	Mesocricetus	33	VTCFCKRPVCDSGETQIGYCRLGNTFYRLCC
defensin 4	auratus		RQ
(HANP-4)
Neutrophil	Macaca	96	MRTLVILAAILLVALQAQAEPLQARTDEATAA
defensins 1, 3	mulatta		QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
and 8			KNMACYCRIPACLAGERRYGTCFYLGRVWA
precursor			FCC
(RMAD)
Neutrophil	Macaca	94	MRTIAILAAILLFALLAQAKSLQETADDAATQE
defensins 4	mulatta		QPGEDDQDLAVSFEENGLSTLRASGSQARR
and 5			TCRCRFGRCFRRESYSGSCNINGRIFSLCCR
precursor
(RMAD)
Neutrophil	Macaca	94	MRTIAILAAILLFALLAQAKSLQETADEAATQE
defensins 6	mulatta		QPGEDDQDLAVSFEENGLSTLRASGSQARR
and 7			TCRCRFGRCFRRESYSGSCNINGRISSLCCR
precursor
NK-lysin	Sus scrofa	129	PGLAFSGLTPEHSALARAHPCDGEQFCQNLA
precursor			PEDPQGDQLLQREELGLICESCRKIIQKLEDM
(NKL)			VGPQPNEDTVTQAASRVCDKMKILRGVCKKI
(Fragment)			MRTFLRRISKDILTGKKPQAICVDIKICKEKTG
			LI
Nonhistone	Oncorhynchus	69	PKRKSATKGDEPARRSARLSARPVPKPAAKP
chromosomal	mykiss		KKAAAPKKAVKGKKAAENGDAKAEAKVQAA
protein H6			GDGAGNAK
(Histone T)
[Contains:
Oncorhyncin
III]
Oligosacchar-	Bos taurus	190	MSRRYTPLAWVLLALLGLGAAQDCGSIVSRG
ide-binding			KWGALASKCSQRLRQPVRYVVVSHTAGSVC
protein			NTPASCQRQAQNVQYYHVRERGWCDVGYN
			FLIGEDGLVYEGRGWNTLGAHSGPTWNPIAI
			GISFMGNYMHRVPPASALRAAQSLLACGAAR
			GYLTPNYEVKGHRDVQQTLSPGDELYKIIQQ
			WPHYRRV
Opistoporin 1	Opistophthalmus	44	GKVWDWIKSTAKKLWNSEPVKELKNTALNAA
	carinatus		KNLVAEKIGATPS
Opistoporin 2	Opistophthalmus	44	GKVWDWIKSTAKKLWNSEPVKELKNTALNAA
	carinatus		KNFVAEKIGATPS
Pandinin 1	Pandinus	44	GKVWDWIKSAAKKIWSSEPVSQLKGQVLNA
	imperator		AKNYVAEKIGATPT
Pandinin 2	Pandinus	24	FWGALAKGALKLIPSLFSSFSKKD
	imperator
Parabutoporin	Parabuthus	45	FKLGSFLKKAWKSKLAKKLRAKGKEMLKDYA
	schlechteri		KGLLEGGSEEVPGQ
Penaeidin-1	Litopenaeus	50	YRGGYTGPIPRPPPIGRPPLRLVVCACYRLSV
(Pen-1) (P1)	vannamei		SDARNCCIKFGSCCHLVK
Penaeidin-2a	Litopenaeus	72	MRLVVCLVFLASFALVCQGEAYRGGYTGPIP
precursor (Pen-	vannamei		RPPPIGRPPFRPVCNACYRLSVSDARNCCIK
2a) (Pen-2)			FGSCCHLVKG
(P2)
Penaeidin-2b	Litopenaeus	72	MRLVVCLVFLASFALVCQGEAYRGGYTGPIP
precursor (Pen-	vannamei		RPPPIGRPPLRPVCNACYRLSVSDARNCCIK
2b)			FGSCCHLVKG
Penaeidin-2d	Litopenaeus	72	MRLVVCLVFLASFALVCQGGAQRGGFTGPIP
precursor (Pen-	setiferus		RPPPHGRPPLGPICNACYRLSFSDVRICCNFL
2d)			GKCCHLVKG
Penaeidin-3a	Litopenaeus	82	MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ
3a) (P3-a)			ARSCCSRLGRCCHVGKGYSG
Penaeidin-3b	Litopenaeus	82	MRLVVCLVFLASFALVCQGQVYKGGYTRPVP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ
3b) (P3-b)			ARSCCSRLGRCCHVGKGYSG
Penaeidin-3c	Litopenaeus	81	MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPFVRPVPGGPIGPYNGCPVSCRGiSFSQA
3c) (P3-c)			RSCCSRLGRCCHVGKGYSG
Penaeidin-3d	Litopenaeus	82	MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA
3d)			RSCCSRLGRCCHVGKGYSG
Penaeidin-3e	Litopenaeus	82	MRLVVCLVFLAPFALVCHGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ
3e)			ARSCCSRLGRCCHVGKGYSG
Penaeidin-3f	Litopenaeus	82	MRLVACLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA
3f)			RSCCSRLGRCCHVGKGYSG
Penaeidin-3g	Litopenaeus	82	MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPISPYNGCPVSCRGISFSQ
3g)			ARSCCSRLGRCCHVGKGYSG
Penaeidin-3h	Litopenaeus	82	MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA
3h)			RSYCSRLGRCCHVGKGYSG
Penaeidin-3i	Litopenaeus	82	MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen-	vannamei		RPPPFVRPLPGGPIGPYNGRPVSCRGISFSQ
3i)			ARSCCSRLGRCCHVGKGYSG
Penaeidin-3j	Litopenaeus	81	MRLVVCLVFLASFALVCQGQVYKGGYTRPVP
precursor (Pen-	vannamei		RPPFVRPLPGGPIGPYNGCPVSCRGISFSQA
3j)			RSCCSRLGRCCHVGKGYSG
Penaeidin-3k	Litopenaeus	75	MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen-	setiferus		RPYVRPVVSYNACTLSCRGITTTQARSCCTR
3k)			LGRCCHVAKGYSG
Penaeidin-3l	Litopenaeus	75	MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen-	setiferus		RPYVRPVVSYNVCTLSCRGITTTQARSCCTR
3l)			LGRCCHVAKGYSG
Penaeidin-3m	Litopenaeus	75	MRLVVCLVFLASFALVCQGQGCKGPYTRPIL
precursor (Pen-	setiferus		RPYVRPVVSYNACTLSCRGITTTQARSCCTR
3m)			LGRCCHVAKGYSG
Penaeidin-3n	Litopenaeus	75	MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen-	setiferus		RPYVRPVVSYNACTLSCRGITTTQARSCSTR
3n)			LGRCCHVAKGYSG
Penaeidin-4a	Litopenaeus	67	MRLVVCLVFLASFALVCQGHSSGYTRPLPKP
precursor (Pen-	vannamei		SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC
4a)			CHRG
Penaeidin-4c	Litopenaeus	67	MRLVVCLVFLASFALVCQGYSSGYTRPLPKP
precursor (Pen-	vannamei		SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC
4c)			CHRG
Penaeidin-4d	Litopenaeus	67	MRLLVCLVFLASFAMVCQGHSSGYTRPLRKP
precursor (Pen-	setiferus		SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC
4d)			CHLG
Phormicin	Protophormia	94	MKFFMVFVVTFCLAVCFVSQSLAIPADAAND
precursor	terraenovae		AHFVDGVQALKEIEPELHGRYKRATCDLLSG
(Insect			TGINHSACAAHCLLRGNRGGYCNGKGVCVC
defensins A			RN
and B)
Phylloxin	Phyllomedusa	64	MVFLKKSLLLVLFVGLVSLSICEENKREEHEEI
precursor	bicolor		EENKEKAEEKRGWMSKIASGIGTFLSGMQQ
			G
Pleurocidin	Pseudopleur-	25	GWGSFFKKAAHVGKHVGKAALHTYL
	onectes
	americanus
Pleurocidin 2	Pseudopleur-	68	MKFTATFLMMAIFVLMVEPGECGWGSFFKKA
precursor	onectes		AHVGKHVGKAALTHYLGDKQELNKRAVDED
	americanus		PNVIVFE
Pleurocidin	Pseudopleur-	68	MKFTATFLMIAIFVLMVEPGECGWGSFFKKA
prepropoly-	onectes		AHVGKHVGKAALTHYLGDKQELNKRAVDED
peptide	americanus		PNVIVFE
Pleurocidin	Pseudopleur-	68	MKFTATFLMMFIFVLMVEPGECGWGSIFKHG
prepropoly-	onectes		RHAAKHIGHAAVNHYLGEQQDLDKRAVDED
peptide	americanus		PNVIVFE
Pleurocidin	Pseudopleur-	60	MKFTATFLMIAIFVLMVEPGECGWGSFFKKA
prepropoly-	onectes		AHVGKHVGKAALTHYLGDKQELNKRAVDE
peptide	americanus
(Fragment)
Pleurocidin	Pseudopleur-	60	MKFTATFLMMFIFVLMVEPGECGWGSIFKHG
prepropoly-	onectes		RHAAKHIGHAAVNHYLGEQQDLDKRAVDE
peptide	americanus
(Fragment)
Pleurocidin-like	Pseudopleur-	89	MKFTATFLLLFIFVLMVDLGEGRRKKKGSKRK
prepropoly-	onectes		GSKGKGSKGKGRWLERIGKAGGIIIGGALDH
peptide	americanus		LGQGQVQGPDYDYQEGEELNKRAVDE
(Fragment)
Pleurocidin-like	Pseudopleur-	72	MKFTATFLLLFIFVLMVDLGEGRRKRKWLRRI
prepropoly-	onectes		GKGVKIIGGAALDHLGQGQVQGQDYDYQEG
peptide	americanus		QELNKRAVDE
(Fragment)
Pleurocidin-like	Pseudopleur-	61	MKFTATFLVLSLVVLMAEPGECFLGALIKGAI
prepropoly-	onectes		HGGRFIHGMIQNHHGYDEQQELNKRAVDE
peptide	americanus
(Fragment)
Polyphemusin I	Limulus	18	RRWCFRVCYRGFCYRKCR
	polyphemus
Polyphemusin	Limulus	18	RRWCFRVCYKGFCYRKCR
II	polyphemus
Ponericin G1	Pachycondyla	30	GWKDWAKKAGGWLKKKGPGMAKAALKAAM
	goeldii		Q
Ponericin G2	Pachycondyla	30	GWKDWLKKGKEWLKAKGPGIVKAALQAATQ
	goeldii
Ponericin G3	Pachycondyla	30	GWKDWLNKGKEWLKKKGPGIMKAALKAATQ
	goeldii
Ponericin G4	Pachycondyla	29	DFKDWMKTAGEWLKKKGPGILKAAMAAAT
	goeldii
Ponericin G5	Pachycondyla	30	GLKDWVKIAGGWLKKKGPGILKAAMAAATQ
	goeldii
Ponericin G6	Pachycondyla	18	GLVDVLGKVGGLIKKLLP
	goeldii
Ponericin G7	Pachycondyla	19	GLVDVLGKVGGLIKKLLPG
	goeldii
Ponericin L1	Pachycondyla	24	LLKELWTKMKGAGKAVLGKIKGLL
	goeldii
Ponericin L2	Pachycondyla	24	LLKELWTKIKGAGKAVLGKIKGLL
	goeldii
Ponericin W1	Pachycondyla	25	WLGSALKIGAKLLPSWGLFKKKKQ
	goeldii
Ponericin W2	Pachycondyla	25	WLGSALKIGAKLLPSWGLFQKKKK
	goeldii
Ponericin W3	Pachycondyla	26	GIWGTLAKIGIKAVPRVISMLKKKKQ
	goeldii
Ponericin W4	Pachycondyla	26	GIWGTALKWGVKLLPKLVGMAQTKKQ
	goeldii
Ponericin W5	Pachycondyla	24	FWGALIKGAAKLIPSWGLFKKKQ
	goeldii
Ponericin W6	Pachycondyla	20	FIGTALGIASAIPAIVKLFK
	goeldii
Preprodefensin	Boophilus	74	MRGIYICLXFVLXCGLVSGLADVPAESEMAHL
	microplus		RVRRGFGCPFNQGACHRHCRSIRRRGGYCA
			GLIKQTCTCYRN
preprodefensin	Ixodes	76	MKVLAVSLAFLLIAGLISTSLAQNEEGGEKELV
	ricinus		RVRRGGYYCPFFQDKCHRHCRSFGRKAGY
			CGGFLKKTCICVMK
Probable	Riptortus	678	MRSPRVIHLACVIAYIVAVEAGDKPVYLPRPT
antibacterial	clavatus		PPRPIHPRLAREVGWELEGQGLSPLSEAELL
peptide			PEVRERRSPVDKGGYLPRPTPPRPVYRSRR
polyprotein			DASLESELSPLSVAEVLPEVRERRSPVDKGG
precursor			YLPRPTPPRPVYRSRRDASLESELSPLSEAE
			VLPEVRERRSPVDKGGYLPRPTPPRPVYRS
			RRVASLESELSPLSEAEVLPEVRERRSPVDK
			GGYLPRPTPPRPVYRSRRDASLESELSPLSE
			EEVLPEVRERGSPVDKGGYLPRPTPPRPVY
			RSRRDASLESELSPLSVAEDLPEVRERRSPV
			DKGGYLPRPTPPRPVYRSRRDASLESELSPL
			SEAEVLPEVRERRSPVDKGGYLPRPTPPRPV
			YRSRRDASLESELSPLSEAEVLPEVRERRSP
			VDKGGYLPRPTPPRPVYRSRRDASLESELSP
			LSEAEVLPEVRERRSPVDKGGYLPRPTPPRP
			VYRSRRDASLESELSPLSEAEVLPEVRERRS
			PVDKGGYLPRPTPPRPVYRSRRDATLESELS
			PSSEAEVLPEVRERRSPVDKGGYLPRPTPPR
			PVYRSRRDASLESELSPLSEAEVLPEVRERR
			SPVDKGGYLPRPTPPRPVYRSRRDASLESEL
			SPLSEAEGLPEVRERRSPGGQGGYLPRPTP
			RTPLCRSRRDANLDAEQSPVSEGWLPEVR
Probable	Riptortus	150	MHIARFCLLSSMAVLALSAGYVSGAVIEIPDEI
antibacterial	clavatus		LDSARFISLYSDGLRQKRQLNLSGPGSEHAG
peptide			TIRLDGQRNIFDNGRTRVDGTGSYQLDYARG
precursor			MKPIHGAGLGAEVNHNIWRGRGGQSLDLYG
			GATRQFNFGNRPNEWGAHGGIRYNF
Proenkephalin	Bos taurus	263	MARFLGLCTWLLALGPGLLATVRAECSQDCA
A precursor			TCSYRLARPTDLNPLACTLECEGKLPSLKTW
[Contains:			ETCKELLQLTKLELPPDATSALSKQEESHLLA
Synenkephalin			KKYGGFMKRYGGFMKKMDELYPLEVEEEAN
Met-enkephalin			GGEVLGKRYGGFMKKDAEEDDGLGNSSNLL
(Opioid growth			KELLGAGDQREGSLHQEGSDAEDVSKRYGG
factor) (OGF);			FMRGLKRSPHLEDETKELQKRYGGFMRRVG
Met-			RPEWWMDYQKRYGGFLKRFAEPLPSEEEG
enkephalin-			ESYSKEVPEMEKRYGGFMRF
Arg-Gly-Leu;
Leu-
enkephalin;
Enkelytin; Met-
enkephalin-
Arg-Phe]
Prophenin-1	Sus scrofa	212	LLLLALVVPSASAQALSYREAVLRAVDRLNEQ
precursor (PF-			SSEANLYRLLELDQPPKADEDPGTPKPVSFT
1) (C6)			VKETVCPRPTRQPPELCDFKENGRVKQCVG
(Fragment)			TVTLDQIKDPLDITCNEGVRRFPWWWPFLRR
			PRLRRQAFPPPNVPGPRFPPPNFPGPRFPP
			PNFPGPRFPPPNFPGPRFPPPNFPGPPFPPP
			IFPGPWFPPPPPFRPPPFGPPRFPGRR
Prophenin-2	Sus scrofa	228	METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PF-			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
2) (PR-2) (C12)			PPKADEDPGTPKPVSFTVKETVCPRPTRRPP
(Prophenin-1			ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
like)			EGVRRFPWWWPFLRRPRLRRQAFPPPNVP
			GPRFPPPNVPGPRFPPPNFPGPRFPPPNFP
			GPRFPPPNFPGPPFPPPIFPGPWFPPPPPFR
			PPPFGPPRFPGRR
Protegrin 1	Sus scrofa	149	METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG-			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
1) (Neutrophil			PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
peptide 1)			ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
			EVQGVRGGRLCYCRRRFCVCVGRG
Protegrin 2	Sus scrofa	147	METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG-			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
2)			PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
			ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
			EVQGVRGGRLCYCRRRFCICVG
Protegrin 3	Sus scrofa	149	METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG-			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
3)			PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
			ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
			EVQGVRGGGLCYCRRRFCVCVGRG
Protegrin 4	Sus scrofa	149	METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG-			LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
4)			PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
			ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
			EVQGVRGGRLCYCRGWCFCVGRG
Protegrin 5	Sus scrofa	149	METQRASLCLGRWSLWLLLLGLVVPSASAQ
precursor (PG-			ALSYREAVLRAVDRLNEQSSEANLYRLLELD
5)			QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
			PELCDFKENGRVKQCVGTVTLDQIKDPLDITC
			NEVQGVRGGRLCYCRPRFCVCVGRG
Protegrin-1	Sus scrofa	19	RGGRLCYCRRRFCVCVGRX
Pseudin 1	Pseudis	24	GLNTLKKVFQGLHEAIKLINNHVQ
	paradoxa
Pseudin 2	Pseudis	24	GLNALKKVFQGIHEAIKLINNHVQ
	paradoxa
Pseudin 3	Pseudis	23	GINTLKKVIQGLHEVIKLVSNHE
	paradoxa
Pseudin 4	Pseudis	23	GINTLKKVIQGLHEVIKLVSNHA
	paradoxa
Putative	Litopenaeus	188	MKGIKAVILCGLFTAVLAGKYRGFGQPLGGL
antimicrobial	setiferus		GVPGGGVGVGVGGGLGGGLGGGLGGGLG
peptide			GGLGGGLGGLGGGLGGLGGGLGGGLGGGL
			GGGLGGGLGGSHGTSDCRYWCKTPEGQAY
			CCESAHEPETPVGTKPLDCPQVRPTCPRFH
			GPPTTCSNDYKCAGLDKCCFDRCLGEHVCK
			PPSFFGQQIFG
Putative	Litopenaeus	123	MKGLGVILCCVLAVVPAHAGPGGFPGGVPG
antimicrobial	setiferus		RFPSATAPPATCRRWCKTPENQAYCCETIFE
peptide			PEAPVGTKPLDCPQVRPTCPRFHGPPVTCS
			SDYKCGGVDKCCFDRCLGEHVCKPPSFYSQ
			FP
Putative	Litopenaeus	141	MKGLGVILCCVLAVVPAHAGPGGFSGGVPG
antimicrobial	setiferus		GFPGGRPGGFPGGVPGGFPSATAPPATCRR
peptide			WCKTPENQAYCCETIFEPEAPVGTKPLDCPQ
			VRPTCPPTRFGGRPVTCSSDYKCGGLDKCC
			FDRCLGEHVCKPPSFYSQFR
Putative	Litopenaeus	163	MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial	vannamei		GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide			GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
			GQAYCCESAHEPETPVGTKILDCPQVRPTCP
			RFHGPPTTCSNDYKCAGLDKCCFDRCLGEH
			VCKPPSFFGSQVFG
Putative	Litopenaeus	163	MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial	vannamei		GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide			GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
			GQAYCCESAHEPETPVGTKPLDCPQVRPTC
			PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
			HVCKPPSFFGSQVFG
Putative	Litopenaeus	169	MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial	vannamei		GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide			GLGVGGGLGVGGGLGVGGGLGTGTSDCRY
			WCKTPEGQAYCCESAHEPETPVGTKILDCP
			QVRPTCPRFHGPPTTCSNDYKCAGLDKCCF
			DRCLGEHVCKPPSFFGSQVFG
Putative	Litopenaeus	163	MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial	vannamei		GGPGGSVGVGGGFPGGGLGVGGGLGVGG
peptide			GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
			GQAYCCESAHEPETPVGTKPLDCPQVRPTC
			PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
			HVCKPPSFFGSQVFG
Putative	Litopenaeus	151	MKGIKAVILCGLFTAVLAGKFRGFGRPFGGL
antimicrobial	vannamei		GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide			GLGTGTSDCRYWCKTPEGQAYCCESAHEPE
			TPVGTKPLDCPQVRPTCPRFHGPPTTCSND
			YKCAGLDKCCFDRCLGEHVCKPPSFFGSQV
			FG
Putative	Litopenaeus	163	MKGIKAVILCGLFTAVLAGKFRGFGRPFGGL
antimicrobial	vannamei		GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide			GLGVGGGLGVGGGLGTGTSDYRYWCKTPE
			GQAYCCESAHEPETPVGTKPLDCPQVRPTC
			PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
			HVCKPPSFFGSQVFG
Putative beta	Mus	79	MKTFLFLFAVLFFLDPAKNAFFDEKCSRVNG
defensin	musculus		RCTASCLKNEELVALCQKNLKCCVTVQPCGK
			SKSNQSDEGSGHMGTWG
Putative beta	Mus	63	MPQTFFVFCFLFFVFLQLFPGTGEIAVCETCR
defensin	musculus		LGRGKCRRACIESEKIVGWCKLNFFCCRERI
Putative beta	Mus	64	MRIFSLIVAGLVLLIQLYPAWGTLYRRFLCKK
defensin	musculus		MNGQCEAECFTFEQKIGTCQANFLCCRKRK
			EH
Putative beta	Mus	67	MRTLCSLLLICCLLFSYTTPAANSIIGVSEMER
defensin	musculus		CHKKGGYCYFYCFSSHKKIGSCFPEWPRCC
			KNIK
Putative beta	Mus	77	MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQ
defensin	musculus		LARCYKFGGFCYNSMCPPHTKFIGNCHPDHL
			HCCINMKELEGST
Putative beta	Mus	73	MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQ
defensin	musculus		LTRCYKFGGFCHYNICPGNSRFMSNCHPENL
			RCGKNIKQF
Putative	Mesobuthus	61	MTYAILIIVSLLLISDRISNVVDKYGSENPLDCN
potassium	martensii		EHCLKTKNQIGICHGANGNEKCSCMES
channel
blocker TXKs2
PYLa/PGLa	Xenopus	64	MYKQIFLCLIIAALCATIMAEASAFADADEDDD
precursor	laevis		KRYVRGMASKAGAIAGKIAKVALKALGRRDS
Pyrrhocoricin	Pyrrhocoris	20	VDKGSYLPRPTPPRPIYNRN
	apterus
Ranalexin	Rana	66	MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor	catesbeiana		RDNPDERDVEVEKRFLGGLIKIVPAMICAVTK
			KC
Ranalexin-1CA	Rana	20	FLGGLMKAFPALICAVTKKC
	clamitans
Ranalexin-1CB	Rana	20	FLGGLMKAFPAIICAVTKKC
	clamitans
Ranatuerin-1C	Rana	25	SMLSVLKNLGKVGLGLVACKINKQG
	clamitans
RANATUERIN-	Rana	28	GLLDTIKGVAKTVAASMLDKLKCKISGC
2B	berlandieri
Ranatuerin-	Rana	31	GLFLDTLKGAAKDVAGKLLEGLKCKIAGGKP
2CA	clamitans
Ranatuerin-	Rana	27	GLFLDTLKGLAGKLLQGLKGIKAGCKP
2CB	clamitans
RANATUERIN-	Rana	32	GILSSIKGVAKGVAKNVAAQLLDTLKCKITGC
2LB	luteiventris
RANATUERIN-	Rana pipiens	27	LMDTVKNVAKNLAGHMLDKLKCKITGC
2P
RANATUREIN-	Rana	32	GILDSFKGVAKGVAKDLAGKLLDKLKGKITGC
2LA	luteiventris
Rhinocerosin	Oryctes	142	MMKLYIVFGFIAFSAAYVVPEGYYEPEYYPAD
precursor	rhinoceros		GYESERVARASPAELIFDEDLADEPEVEEPQ
			YYIRTRRSLQPGAPNFPMPGSQLPTSITSNIE
			KQGPNTAATINAQHKTDRYDVGATWSKVIRG
			PGRSKPNWSIGGTYRW
Royalism	Apis mellifera	95	MKIYFIVGLLFMAMVAIMAAPVEDEFEPLEHF
precursor			ENEERADRHRRVTGDLLSFKGQVNDSAGAA
(Defensin)			NGLSLGKAGGHGEKVGGIGRKTSFKDLWDK
			RFG
Rugosin A	Rana rugosa	33	GLLNTFKDWAISIAKGAGKGVLTTLSGKLDKS
			C
Rugosin B	Rana rugosa	33	SLFSLIKAGAKFLGKNLLKQGAQYAACKVSKE
			C
Rugosin C	Rana rugosa	37	GILDSFKQFAKGVGKDLIKGAAQGVLSTMSC
			KLAKTC
Sapecin B	Sarcophaga	88	MKFLTSLLLLFVVVMVSAVNLSMAKESANQL
precursor	peregrina		TERLQELDGAAIQEPAELNRHKRLTCEIDRSL
			CLLHCRLKGYLRAYCSQQKVCRCVQ
Sapecin C	Sarcophaga	40	ATCDLLSGIGVQHSACALHCVFRGNRGGYCT
	peregrina		GKGICVCRN
Sapecin	Sarcophaga	94	MKSFIVLAVTLCLAAFFMGQSVASPAAAAEES
precursor	peregrina		KFVDGLHALKTIEPELHGRYKRATCDLLSGTG
			INHSACAAHCLLRGNRGGYCNGKAVCVCRN
Sarcotoxin IA	Sarcophaga	63	MNFQNIFIFVALILAVFAGQSQAGWLKKIGKKI
precursor	peregrina		ERVGQHTRDATIQGLGIAQQAANVAATARG
Sarcotoxin IB	Sarcophaga	63	MNENKVFIEVALILAVFAGQSQAGWLKKIGKKI
precursor	peregrina		ERVGQHTRDATIQVIGVAQQAANVAATARG
Sarcotoxin IC	Sarcophaga	39	GWLRKIGKKIERVGQHTRDATIQVLGIAQQAA
	peregrina		NVAATAR
Sarcotoxin ID	Sarcophaga	40	GWIRDFGKRIERVGQHTRDATIQTIAVAQQAA
	peregrina		NVAATLKG
Sarcotoxin II-1	Sarcophaga	265	MKSFVLFAACMAIIALGSLAHAYPQKLPVPIPP
precursor	peregrina		PSNPPVAVLQNSVATNSKGGQDVSVKLSAT
			NLGNNHVQPIAEVFAEGNTKGGNVLRGATV
			GVQGHGLGASVTKTQTDTKIKGLDFQPQLSS
			STLALQGDRLGASISRDVNRGVSDTFTKSVS
			ANVFRNDNHNLDATVFRSDVRQNNGFNFQK
			TGGMLDYSHANGHGLNAGLTHFSGIGNQAN
			VGGSSTLFKSNDGSLSLKANAGGSQWLSGP
			FSNQRDYNVGLSLTHHGCGG
Sarcotoxin II-2	Sarcophaga	294	MKSFVFFAACFAIVALNSLAHAYPQKLPVPIP
precursor	peregrina		PPTNPPVAAFHNSVATNSKGGQDVSVKLAAT
			NLGNKHVQPIAEVFAKGNTQGGNVLRGATV
			GVQGHGLGASVTKTQDGIAESFRKQAEANL
			RLGDSASLIGKVSQTDTKIKGIDFKPQLSSSSL
			ALQGDRLGASISRDVNRGVSDTLTKSISANVF
			RNDNHNLDASVFRSDVRQNNGFNFQKTGG
			MLDYSHANGHGLNAGLTRFSGIGNQANVGG
			YSTLFRSNDGLTSLKANAGGSQWLSGPFAN
			QRDYSFGLGLSHNAWRG
Sarcotoxin II-3	Sarcophaga	294	MKSFVLFAACMAIVALSSLAHAYPQKLPVPIP
precursor	peregrina		PPTNPPVAAFHNSVATNSKGGQDVSVKLXAT
			NLGNKHVQPIAEVFAEGNTKGGNVIRGATVG
			VQGHGLGASVTKSGNGIAESFRKQAEANLRL
			GDSASLIGKVSQTDTKIKGIDFKPQLSSSSLAL
			QGDRLGASISRDVNRGVSDTLTKSISANVFR
			NDNHNLDASVFRSDVRQNNGFNFQKTGGML
			DYSHANGHGLNAGLTRFSGIGNQANVGGYS
			TLFRSNDGLTSLKANAGGSQWLSGPFANQR
			DYSFGLGLSHNAWRG
Sarcotoxin IIA	Sarcophaga	294	MKSFVFFAACMAIIALSSLVQAYPQKLPVPIPP
precursor	peregrina		PTNPPVAAFHNSVATNSKGGQDVSVKLAATN
			LGNKHVQPIAEVFAEGNTKGGNVLRGATVGV
			QGHGLGASVTKSQDGIAESFRKQAEANLRLG
			DSASLIGKVSQTDTKIKGIDFKPQLSSSSLALQ
			GDRLGASISRDVNRGVSDTLTKSVSANLFRN
			DNHNLDASVFRSDVRQNNGFNFQKTGGMLD
			YSHANGHGLNAGLTRFSGIGNQATVGGYSTL
			FRSNDGLTSLKANAGGSQWLSGPFANQRDY
			SFGLGLSHNAWRG
Scorpine	Pandinus	94	MNSKLTALIFLGLIAIAYCGWINEEKIQKKIDER
precursor	imperator		MGNTVLGGMAKAIVHKMAKNEFQCMANMD
			MLGNCEKHCQTSGEKGYCHGTKCKCGTPLS
			Y
Secretogranin I	Bos taurus	646	MQPAALLGLLGATVVAAVSSMPVDIRNHNEE
precursor (Sgl)			VVTHCIIEVLSNALLKSSAPPITPECRQVLKKN
(Chromogranin			GKELKNEEKSENENTRFEVRLLRDPADTSEA
B) (CgB)			PGLSSREDSGEGDAQVPTVADTESGGHSRE
[Contains:			RAGEPPGSQVAKEAKTRYSKSEGQNREEEM
GAWK peptide;			VKYQKRERGEVGSEERLSEGPGKAQTAFLN
Secretolytin]			QRNQTPAKKEELVSRYDTQSARGLEKSHSR
			ERSSQESGEETKSQENWPQELQRHPEGQE
			APGESEEDASPEVDKRHSRPRHHHGRSRPD
			RSSQEGNPPLEEESHVGTGNSDEEKARHPA
			HFRALEEGAEYGEEVRRHSAAQAPGDLQGA
			RFGGRGRGEHQALRRPSEESLEQENKRHGL
			SPDLNMAQGYSEESEEERGPAPGPSYRARG
			GEAAAYSTLGQTDEKRFLGETHHRVQESQR
			DKARRRLPGELRNYLDYGEEKGEEAARGKW
			QPQGDPRDADENREEARLRGKQYAPHHITE
			KRLGELLNPFYDPSQWKSSRFERKDPMDDS
			FLEGEEENGLTLNEKNFFPEYNYDWWEKKP
			FEEDVNWGYEKRNPVPKLDLKRQYDRVAEL
			DQLLHYRKKSAEFPDFYDSEEQMSPQHTAE
			NEEEKAGQGVLTEEEEKELENLAAMDLELQK
			IAEKFSGTRRG
Similar to	Mus	93	MKKLVLLSALVLLAYQVQTDPIQNTDEETNTE
cryptdin-4	musculus		EQPGEEDQAVSVSFGGQEGSALHEKLSRDLI
			CLCRKRRCNRGELFYGTCAGPFLRCCRRRR
Similar to	Mus	93	MKTLVLLSALILLAYQVQTDPIQNTDEETNTEE
cryptdin-4	musculus		QPGEDDQAVSVSFGGQEGSALHEKLSRDLIC
			LCRNRRCNRGELFYGTCAGPFLRCCRRRR
Similar to	Mus	95	MKTLVLLSALVLLAFQVQADPIQNTDEETNTE
cryptdin-4	musculus		EQAGEEDQAVSVSFGDPEGSALHEKSSRDLI
			CYCRKGGCNRGEQVYGTCSGRLLFCCRRR
			HRH
Similar to	Mus	95	MKTLVLLSALVLLAFQVQADPIQNTDEETNTE
cryptdin-4	musculus		EQAGEEDQAVSVSFGDPEGSALHEKSSRDLI
			CYCRKGGCNRGEQVYGTCSGRLLLCCRRR
			HRH
Similar to	Mus	95	MKTLVLLSALVLLAFQVQADPIQNTDEETNTE
cryptdin-4	musculus		EQPGEEDQAVSVSFGDPEGSALHEKSSRDLI
			CYCRKGGCNRGEQVYGTCSGRLLFCCRRR
			HRH
Single WAP	Mus	80	MKLLGLSLLAVTILLCCNMARPEIKKKNVFSK
motif protein 1	musculus		PGYCPEYRVPCPFVLIPKCRRDKGCKDALKC
precursor			CFFYCQMRCVDPWESPE
(Elafin-like
protein I)
Single WAP	Mus	85	MWPNSILVLMTLLISSTLVTGGGVKGEEKRV
motif protein 2	musculus		CPPDYVRCIRQDDPQCYSDNDCGDQEICCF
precursor			WQCGFKCVLPVKDNSEEQIPQSKV
(Elafin-like
protein II)
Spingerin	Pseudacan-	25	HVDKKVADKVLLLKQLRIMRLLTRL
	thotermes
	spiniger
Styelin A	Styela clava	20	GXFGKAFXSVSNFAKKHKTA
(Fragment)
Styelin B	Styela clava	20	GXFGPAFHSVSNFAKKHKTA
(Fragment)
Styelin C	Styela clava	80	MQMKATILIVLVALFMIQQSEAGWFGKAFRSV
precursor			SNFYKKHKTYIHAGLSAATLLGDMTDEEFQE
			FMQDIEQAREEELLSRQ
Styelin D	Styela clava	81	MQMKATILIVLVALFMIQQSEAGWLRKAAKSV
precursor			GKFYYKHKYYIKAAWQIGKHALGDMTDEEFQ
			DFMKEVEQAREEELQSRQ
Styelin E	Styela clava	81	MQMKATILIVLVALFMIQQSEAGWLRKAAKSV
precursor			GKFYYKHKYYIKAAWKIGRHALGDMTDEEFQ
			DFMKEVEQAREEELQSRQ
T22H6.7	Caenorhabditis	195	MFRKLIIATFVLSLCDLANSVTICSSSSLLSTFT
protein (ABF-6)	elegans		DPLCTSWCKVRFCSSGSCRSVMSGSDPTCE
			CESCGFGSWFGSSSDSNSNQPVSGQYYAG
			GSGGEMATPNYGNNNGYNNGYNNGNNMRY
			NDNNGYNTNNGYRGQPTPGYGNSNSNFNS
			NQQYSYQQYYNNRNNQYGNSGYGNAGQAG
			QTGYPSGYQNLKKKR
tachycitin	Tachypleus	98	MASSFMFAVVVLFISLAANVESYLAFRCGRY
precursor	tridentatus		SPCLDDGPNVNLYSCCSFYNCHKCLARLEN
			CPKGLHYNAYLKVCDWPSKAGCTSVNKECH
			LWKTGRK
Tachyplesin I	Tachypleus	77	MKKLVIALCLMMVLAVMVEEAEAKWCFRVCY
precursor	tridentatus		RGICYRRCRGKRNEVRQYRDRGYDVRAIPE
			ETFFTRQDEDEDDDEE
Tachyplesin II	Tachypleus	77	MKKLVIALCLMMVLAVMVEEAEARWCFRVCY
precursor	tridentatus		RGICYRKCRGKRNEVRQYRDRGYDVRAIPD
			ETFFTRQDEDEDDDEE
Tachystatin A2	Tachypleus	67	MKLQNTLILIGCLFLMGAMIGDAYSRCQLQGF
precursor	tridentatus		NCVVRSYGLPTIPCCRGLTCRSYFPGSTYGR
			CQRY
Temporin A	Rana	13	FLPLIGRVLSGIL
	temporaria
Temporin B	Rana	61	MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor	temporaria		RDEPDERDVQVEKRLLPIVGNLLKSLLGK
Temporin C	Rana	13	LLPILGNLLNGLL
	temporaria
Temporin D	Rana	13	LLPIVGNLLNSLL
	temporaria
Temporin E	Rana	13	VLPIIGNLLNSLL
	temporaria
Temporin F	Rana	13	FLPLIGKVLSGIL
	temporaria
Temporin G	Rana	61	MFTLKKSLLLLFFLGTINLSLCEEERDADEER
precursor	temporaria		RDDLEERDVEVEKRFFPVIGRILNGILGK
Temporin H	Rana	58	MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor	temporaria		RDEPDERDVQVEKRLSPNLLKSLLGK
Temporin K	Rana	10	LLPNLLKSLL
	temporaria
Temporin L	Rana	13	FVQWFSKFLGRIL
	temporaria
Temporin-1CA	Rana	13	ELPELAKILTGVL
	clamitans
Temporin-1CB	Rana	13	FLPLFASLIGKLL
	clamitans
Temporin-1CC	Rana	13	FLPFLASLLTKVL
	clamitans
Temporin-1CD	Rana	13	FLPFLASLLSKVL
	clamitans
Temporin-1CE	Rana	13	FLPFLATLLSKVL
	clamitans
Temporin-1Ja	Rana	13	ILPLVGNLLNDLL
	japonica
Temporin-1LA	Rana	13	VLPLISMALGKLL
	luteiventris
Temporin-1LB	Rana	14	NFLGTLINLAKKIM
	luteiventris
Temporin-1LC	Rana	14	FLPILINLIHKGLL
	luteiventris
Temporin-1P	Rana pipiens	13	FLPIVGKLLSGLL
Tenecin 1	Tenebrio	84	MKLTIFALVACFFILQIAAFPLEEAATAEEIEQG
precursor	molitor		EHIRVKRVTCDILSVEAKGVKLNDAACAAHCL
			FRGRSGGYCNGKRVCVCR
Tenecin 3	Tenebrio	96	MKTFVICLILVVAVSAAPDHHDGHLGGHQTG
precursor	molitor		HQGGQQGGHLGGQQGGHLGGHQGGQPGG
			HLGGHQGGIGGTGGQQHGQHGPGTGAGHQ
			GGYKTHGH
Termicin	Pseudacan-	36	ACNFQSCWATCQAQHSIYFRRAFCDRSQCK
	thotermes		CVFVRG
	spiniger
Testis defensin	Mus	41	MKTLVLLSALFLLAFQVQADPIQNTDEETNTE
(Fragment)	musculus		VQPQEEDQA
Testis defensin	Mus	40	MKTLVLLSPSSCWPSRSRLILSKTQMKRLKL
(Fragment)	musculus		RSSQRKRTR
Testis-specific	Mus	83	MRLALLLLAILVATELVVSGKNPILQCMGNRG
beta-defensin-	musculus		FCRSSCKKSEQAYFYCRTFQMCCLQSYVRIS
like protein			LTGVDDNTNWSYEKHWPRIP
Thanatin	Podisus	21	GSKKPVPIIYCNRRTGKCQRM
	maculiventris
Theta Defensin	Macaca	18	GFCRCLCRRGVCRCICTR
1	mulatta
theta defensin	Macaca	76	MRTFALLTAMLLLVALHAQAEARQARADEAA
1a precursor	mulatta		AQQQPGTDDQGMAHSFTWPENAALPLSESA
			KGLRCICTRGFCRLL
theta defensin	Macaca	76	MRTFALLTAMLLLVALHAQAEARQARADEAA
1b precursor	mulatta		AQQQPGADDQGMAHSFTRPENAALPLSESA
			RGLRCLCRRGVCQLL
theta defensin-	Macaca	18	RCICTRGFCRCLCRRGVC
1	mulatta
Tigerinin-1	Hoplobatrachus	11	FCTMIPIPRCY
	tigerinus
Tigerinin-2	Hoplobatrachus	12	RVCFAIPLPICH
	tigerinus
Tigerinin-3	Hoplobatrachus	12	RVCYAIPLPICY
	tigerinus
Tigerinin-4	Hoplobatrachus	11	RVCYAIPLPIC
	tigerinus
tracheal	Bos taurus	64	MRLHHLLLALLFLVLSASSGFTQGVGNPVSC
antimicrobial			VRNKGICVPIRCPGNMKQIGTCVGRAVKCCR
peptide			KK
Tracheal	Bos taurus	64	MRLHHLLLALLFLVLSAWSGFTQGVGNPVSC
antimicrobial			VRNKGICVPIRCPGSMKQIGTCVGRAVKCCR
peptide			KK
precursor
(TAP)
Xenopsin	Xenopus	81	MYKGIFLCVLLAVICANSLATPSSDADEDNDE
precursor	laevis		VERYVRGWASKIGQTLGKIAKVGLKELIQPKR
[Contains:			EAMLRSAEAQGKRPWIL
Xenopsin
precursor
fragment
(XPF);
Xenopsin]

Plant Antimicrobial Peptides
Protein Name	Organism Name	Length	Sequence
22K	Zea mays	206	AVFTVVNQCPFTVWAASVPVGGGR
antifungal			QLNRGESWRITAPAGTTAARIWAR
protein			TGCQFDASGRGSCRTGDCGGVVQC
			TGYGRAPNTLAEYALKQFNNLDFF
			DISLIDGFNVPMSFLPDGGSGCSR
			GPRCAVDVNARCPAELRQDGVCNN
			ACPVFKKDEYCCVGSAANNCHPTN
			YSRYFKGQCPDAYSYPKDDATSTF
			TCPAGTNYKVVFCP
AC-	Amaranthus	29	VGECVRGRCPSGMCCSQFGYCGKG
AMP1 =	caudatus		PKYCG
ANTIMICROBIAL
peptide
Alpha-	Zea mays	206	AVFTVVNQCPFTVWAASVPVGGGR
amylase/			QLNRGESWRITAPAGTTAARIWAR
trypsin			TGCQFDASGRGSCRTGDCGGVVQC
inhibitor			TGYGRAPNTLAEYALKQFNNLDFF
(Antifungal			DISILDGFNVPYSFLPDGGSGCSR
protein)			GPRCAVDVNARCPAELRQDGVCNN
			ACPVFKKDEYCCVGSAANNCHPTN
			YSRYFKGQCPDAYSYPKDDATSTF
			TCPAGTNYKVVFCP
Alpha-	Basella alba	20	GADFQECMKEHSQKQHQHQG
basrubrin
(Fragment)
antifungal	Linum	37	ARFDIQNKCPYTVWAASVPVGGGR
25K protein	usitatissimum		QLNSGQTWXIDAP
antifungal	Diospyros	30	ATFDIQNKXTYTVWAAAWAPSYPG
27K protein	texana		GXKQLD
antifungal 2S	Raphanus	20	PQGPQQRPPLLQQCCNNLLQ
storage	sativus
albumin large
chain
antifungal 2S	Raphanus	30	PAGPFRIPRCRREFQQAQHLRACQ
storage	sativus		QWLHRQ
albumin small
chain
Antifungal	Phytolacca	38	AGCIKNGGRCNASAGPPYCCSSYC
Peptide	americana		FQIAGQSYGVCKNR
Antifungal	Eucommia	41	QTCASRCPRPCNAGLCCSIYGYCG
peptide 1	ulmoides		SGNAYCGAGNCRCQCRG
(EAFP1)
Antifungal	Eucommia	41	QTCASRCPRPCNAGLCCSIYGYCG
peptide 2	ulmoides		SGAAYCGAGNCRCQCRG
(EAFP2)
Antifungal	Gastrodia	171	MAASASTAVILFFAVTTMMSLSAI
protein	elata		PAFASDRLNSDHQLDTGGSLAQGG
			YLFIIQNDCNLVLYDNNRAVWASG
			TNGKASNCFLKMQNDGNLVIYSGS
			RAIWASNTNRQKGNYYLILQRDRN
			VVIYDNSNNAIWATHTNVGNAEIT
			VIPHSNGTAAASGAAQNKVNELYI
			SMY
Antifungal	Gastrodia	169	MASPASSAVIFLFAVAALMSLLAM
protein	elata		PALAASQLNAGQTLGTGQSLAQGP
			DQFVIQNDCNLVLYDSNRVVWASG
			TNGKASGCVLRMQRDGNLVIYSGS
			RVIWASNTNRRDDNYYLLLQRDRN
			VVIYDSSNNAIWATGTNVGNAAIT
			VIPHSNGTAAASGAAQNKVNEYLR
			P
Antifungal	Ipomoea nil	92	MKFCTMFLVVLALASLLLTPSTIM
protein			AQQCGSQARGRLCGNGLCCSQWGY
			CGSTAAYCGAGCQSQCKSTAASAT
			DTTTTANQSTAKSDPAGGAN
Antifungal	Capsicum	85	MKFQVVILVLFALLLTRTSAQNCG
protein	annuum		RQAGRRVCANRLCCSQFGFCGTTR
			EYCGAGCQSNCRRYATDTTGEGEN
			VNNDEHKNNGGPN
Antifungal	Ipomoea nil	91	MKYCTMFIVLLGLGSLLLTPTTIM
protein			AQQCGRQASGRLCGNGLCCSQWGY
			CGSTAAYCGAGCQSQCKSTAASST
			TTTTANQSTAKSDPAGGAN
antifungal	Sinapis alba	25	QKLCERPSGTWSGVCGNNNACKNQ
protein 1			C
antifungal	Brassica	30	QKLCERPSGTWSGVCGNNNACKNQ
protein 1	napus		CINLEK
antifungal	Arabidopsis	27	QKLCERPSGTWSGVCGNSNACKNQ
protein 1	thaliana		CIN
Antifungal	Raphanus	51	XKLCERPSGTWSGVCGNNNACKNQ
Protein 1	sativus		CINLEKARHGSCNYVFPAHKCICY
			FPC
Antifungal	Malva	15	VAGPFRIPPLRREFQ
protein 1	parviflora
large
subunit
(CW-1)
(Fragment)
Anti-fungal	Phytolacca	65	MAKVSSAYLKFALVMILLLSVISA
protein 1	americana		VMSAGCIKNGGRCNASAGPPYCCS
precursor			SYCFQIAGQSYGVCKNR
(PAFP-S)
Antifungal	Malva	16	PAGPFRIPPRXRXEFQ
protein 1	parviflora
small
subunit
(CW-1)
(Fragment)
antifungal	Sinapis alba	26	QKLCQRPSGTWSGVCGNNNACRNQ
protein 2			CI
Antifungal	Malva	20	PEDPQRRYQEXQREXRXQQE
protein 2	parviflora
large
subunit
(CW-2)
(Fragment)
Antifungal	Malva	15	PEDPQRRYQEEQRRE
protein 3	parviflora
(CW-3)
(Fragment)
Antifungal	Malva	37	DRQIDMEEQQLEKLNKQDRXPGLR
protein 4	parviflora		YAAKQQMXTXRMG
(CW-4)
(Fragment)
Antifungal	Malva	38	ITCGQVTSQVAGCLSYLQRGGAPA
protein 5	parviflora		PXXXXGIRNLXXMA
(CW-5)
(Fragment)
Antifungal	Beta vulgaris	46	AICKKPSKFFKGACGRDADCEKAC
protein AX1			DQENWPGGVCVPFLRCECQRSC
Antifungal	Beta vulgaris	46	ATCRKPSMYFSGACFSDTNCQKAC
protein AX2			NREDWPNGKCLVGFKCECQRPC
Antifungal	Gastrodia	129	SDRLNSGHQLDTGGSLAEGGYLFI
protein	elata		IQNDCNLVLYDNNRAVWASGTNGK
GAFP-1			ASGCVLKMQNDGNLVIYSGSRAIW
(Fragment)			ASNTNRQNGNYYLILQRDRNVVIY
			DNSNNAIWATHTNVGNAEITVIPH
			SNGTAAASG
Antifungal	Medicago	72	MEKKSLAGLCFLFLVLFVAQEIVV
protein	sativa		TEARTCENLADKYRGPCFSGCDTH
precursor			CTTKENAVSGRCRDDFRCWCTKRC
Antifungal	Gastrodia	178	MLEWGDGVFCGGCVGYLRGDSVEC
protein	elata		GNCSDRLNSGHQLDTGGSLAQGGY
precursor			LFIIQNDCNLVLYDNNRAVWASGT
			NGKASGCVLKMQNDGNLVIYSGSR
			AIWASNTNRQNGNYYLILQRDRNV
			VIYDNSNNAIWATHTNVGNAEITA
			IPHSNGTAAASGAAQNKVNELYIS
			MYSRSKRIAG
Antifungal	Hordeum	44	ATITWNRCSYTVWPGALPGGGVRL
protein R	vulgare		DPGQRWALNMPAGTAGAAV
(Fragment)
Antifungal	Hordeum	37	ATFTVINKCQYTVWAAAVPAGGGQ
protein S	vulgare		KLDAGQTWSIXXP
(Fragment)
Antifungal	Arabidopsis	80	MAKSATIITFLFAALVLFAAFEAP
protein-like	thaliana		TMVEAQKLCEKPSGTWSGVCGNSN
			ACKNQCINLEGAKHGSCNYVFPAH
			KCICYVPC
Antimicrobial	Pisum	60	ALSFLFLFLFVAQEIVVTEANTCE
detensin	sativum		HLADTYRGVCFTDASCDDHCKNKA
peptide			HLISGTCHNFKC
DRR230-c
(Fragment)
Antimicrobial	Macadamia	76	SAFTVWSGPGCNNRAERYSKCGCS
Peptide 1	integrifolia		AIHQKGGYDFSYTGQTAALYNQAG
			CSGVAHTRFGSSARACNPFGWKSI
			FIQC
Antimicrobial	Mesembryan	64	MAKVSSSLLKFAIVLILVLSMSAI
peptide 1	themum		ISAKCIKNGKGCREDQGPPFCCSG
precursor	crystallinum		FCYRQVGWARGYCKNR
Antimicrobial	Macadamia	102	MASTKLFFSVITVMMLIAMASEMV
peptide 1	integrifolia		NGSAFTVWSGPGCNNRAERYSKCG
precursor			CSAIHQKGGYDFSYTGQTAALYNQ
(AMP1)			AGCSGVAHTRFGSSARACNPFGWK
			SIFIQC
Antimicrobial	Mirabilis	61	LPVAFLKFAIVLILFIAMSAMIEA
peptide 1	jalapa		QCIGNGGRCNENVGPPYCCSGFCL
precursor			RQPGQGYGYCKNR
(AMP1)
(MJ-AMP1)
(Fragment)
Antimicrobial	Amaranthus	30	VGECVRGRCPSGMCCSQFGYCGKG
Peptide 2	caudatus		PKYCGR
Antimicrobial	Mirabilis	63	MAKVPIAFLKFVIVLILFIAMSGM
peptide 2	jalapa		IEACIGNGGRCNENVGPPYCCSGF
precursor			CLRQPNQGYGVCRNR
(AMP2)
(MJ-AMP2)
Antimicrobial	Spinacia	22	XTCESPSHKFKGPCATNRNCES
peptide D1	oleracea
(So-D1)
(Defensin D1)
(Fragment)
Antimicrobial	Spinacia	52	GIFSSRKCKTPSKTFKGICTRDSN
peptide D2	oleracea		CDTSCRYEGYPAGDCKGIRRRCMC
(So-D2)			SKPC
(Defensin D2)
(Fragment)
Antimicrobial	Spinacia	25	GIFSSRKCKTVSKTFRGICTRNAN
peptide D3	oleracea		C
(So-D3)
(Defensin D3)
(Fragment)
Antimicrobial	Spinacia	23	MFFSSKKCKTVSKTFRGPCVRNA
peptide D4	oleracea
(So-D4)
(Defensin D4)
(Fragment)
Antimicrobial	Spinacia	24	MFFSSKKCKTVXKTFRGPCVRNAN
peptide D5	oleracea
(So-D5)
(Defensin D5)
(Fragment)
Antimicrobial	Spinacia	24	GIFSNMYXRTPAGYFRGPXGYXXN
peptide D6	oleracea
(So-D6)
(Defensin D6)
(Fragment)
Antimicrobial	Spinacia	38	GIFSSRKCKTPSKTFKGYCTRDSN
peptide D7	oleracea		CDTSCRYEGYPAGD
(So-D7)
(Defensin D7)
(Fragment)
Antimicrobial	Zea mays	33	RSGRGECRRQCLRRHEGQPWETQE
peptide MBP-1			CMRRCRRRG
Antimicrobial	Capsella	120	MASKTLILLGLFAILLVVSEVSAA
peptide shep-	bursa-		RESGMVKPESEETVQPEGYGGHGG
GRP	pastoris		HGGHGGHGGHGGHGHGGGGHGLDG
			YHGGHGGHGGGYNGGGGHGGHGGG
			YNGGGHHGGGGHGLNEPVQTQPGV
Antimicrobial	Impatiens	333	MVQKGWFGVLLILFICSTLTSADS
peptides	balsamina		KPNPTKEEEPAKKPDEVSVKSGGP
precursor			EVSEDQYRHRCCAWGPGRKYCKRW
(IB-AMP)			CANAEEAAAAIPEASEELAQEEAP
[Contains:			VYSEDQWGRRCCGWGPGRRYCVRW
Basic peptide			CQNAEEAAAAIPEATEKAQEAPVY
AMP3 (IB-			SEDQWGRRCCGWGPGRRYCVRWCQ
AMP3); Basic			NAEEAAAAVAIPEASEKAQEGPVY
peptide AMP1-			SEDQWGRRCCGWGPGRRYCVRWCS
1 (IB-AMP1-			NAADEVATPEDVEPGQYGRRCCNW
1); Basic			GPGRRYCKRWCHNAAEEATLKAFE
peptide AMP1-			EEAAREQPVYSEDQWGRRCCGWGP
2 (IB-AMP1-			GRRYCRRWCQSAEEAAAFQAGEVT
2); Basic			ASLMLIMFKACPCMGPVPSV
peptide AMP1-
3 (IB-AMP1-
3); Basic
peptide A
Antimicrobial	Allium cepa	132	MVRVVSLLAASTFILLIMIISSPY
protein Ace-			ANSQNICPRVNRIVTPCVAYGLGR
AMP1			APIAPCCRALNDLRFVNTRNLRRA
precursor			ACRCLVGVVNRNPGLRRNPRFQNI
			PRDCRNTFVRPFWWRPRIQCGRIN
			LTDKLIYLDAEE
Antimicrobial	Ipomoea nil	41	QQCGRQASGRLCGNRLCCSQWGYC
protein PN-			GSTASYCGAGCQSQCRS
AMP (PN-
AMP1/PN-
AMP2)
antimicrobial	Amaranthus	86	MVNMKCVALIVIVMMAFMMVDPSM
protein	hypochondriacus		GVGECVRGRCPSGMCCSQFGYCGK
precursor			GPKYCGRASTTVDHQADVAATKTA
			KNPTDAKLAGAGSP
Antimicrobial	Phytolacca	37	ACIKNGGRCVASGGPPYCCSNYCL
seed protein	americana		QIAGQSYGVCKKH
(Fragment)
avematin	Avena sativa	26	TTITVVNKCSYTVWPGALPGGGVV
			LD
Basal layer	Zea mays	93	MAKFFNYTIIQGLLMLSMVLLASC
antifungal			AIHAHIISGETEEVSNTGSPTVMV
peptide			TMGANRKIIEDNKNLLCYLRALEY
precursor			CCARTRQCYDDIKKCLEHCRG
Basal layer	Zea mays	96	MVKILDHISIRGFFLLFMVLVASF
antifungal			VGHAQIIRGETKEDNDTKSMTMTT
peptide			MRPGSYVTSMDEKSSLCFEDIKTL
precursor			WYICRTTYHLYRTLKDCLSHCNSM
Basal layer	Zea mays	95	MVKSLDHITIRGLFLLFMFLVASF
antifungal			VGHAQIIRGETKENKDTNSMTMTT
peptide			RPGSYVISMDEKSSLCFLDPRTLW
precursor			YICKITYRLFRTLKDCLEFCHSI
Basal layer	Zea mays	73	MVLLASCVIHAHIISGEIEDVSNT
antifungal			RSPTMMGANRKIIGDNKNLLCYLK
peptide			ALEYCCERTKQCYDDIKKCLEHCH
precursor			S
Beta-basrubin	Basella alba	16	KIMAKPSKFYEQLRGR
(Fragment)
CBP20	Nicotiana	208	GKLSTLLLVLILYFIAAGANAQQC
(Fragment)	tabacum		GRQRGGALCSGNLCCSQFGWCGST
			PEYCSPSQGCQSQCSGGGGGGGGG
			GGGGAQNVRATYHIYNPQNVGWDL
			YAVSAYCSTWDGNKPLAWRRKYGW
			TAFCGPVGPRGRDSCGKCLRVTNT
			GTGAQTTVRIVDQCSNGGLDLDVN
			VFRQLDTDGRGNQRGHLIVNYEFV
			NCGDNMNVLLSPVDKE
CBP20	Nicotiana	211	MGKLSTLLFALVLYVIAAGANAQQ
preproprotein	tabacum		CGRQRGGALCSGNLCCIQFGWCGS
			TQEYCSPSQGCQSQCSGGGGGGGG
			GGGGGGAAQNVRATYHIYNPQNVG
			WDLYAVSAYCSTWDGNKPLAWRRK
			YGWTAFCGPVGPRGRDSCGKCLRV
			TNTGTGAQTTVRIVDQCSNGGLDL
			DVNVFRQLDTDGRGNQRGHLIVNY
			EFVNCGDNMNVLVSPVDKE
chitinase (EC	Nicotiana	378	MANSVTLFSIIFSCFLLRQLVCTN
3.2.1.14)/	tabacum		SQNVIKGGYWFKNSGLALNNIDST
lysozyme (EC			LFTHLFCAFADLNPQSNQLIISPE
3.2.1.17) PZ			NQDSFSQFTSTVQRKNPSVKTFLS
precursor,			IAGGRADTTAYGIMARQPNSRKSF
pathogenesis-			IDSSIRLARQFGFHGLDLDWEYPL
related			SATDMTNLGILLNEWRTAINMEAR
			NSGRAALLLTAAVSYSPRVNGLNY
			PVESVARNLNWINLMAYDFYGPNW
			SPSQTNSHAQLFDPVNHISGSDGI
			NAWIQAGVPTKKLVLGIPFYGYAW
			RLVNPNIHDLRAPAAGKSNVGAVD
			DGSMTYNRIRDYIVQSRATTVYNA
			TIVGDYCYSGSNWISYDDTQSVRN
			KVNYVKGRGLLGYFAWHVAGDQNW
			GLSRTASQTWGVSSQEMK
chitinase (EC	Zea mays	280	MANAPRILALGLLALLCAAAGPAA
3.2.1.14) A			AQNCGCQPNFCCSKFGYCGTTDAY
			CGDGCQSGPCRSGGGGGGGGGGGG
			GGSGGANVANVVTDAFFNGIKNQA
			GSGCEGKNFYTRSAFLSAVNAYPG
			FAHGGTEVEGKREIAAFFAHVTHE
			TGHFCYISEINKSNAYCDASNRQW
			PCAAGQKYYGRGPLQISWNYNYGP
			AGRDIGFNGLADPNRVAQDAVIAF
			KTALWFWMNNVHRVMPQGFGATIR
			AINGALECNGNNPAQMNARVGYYK
			QYCQQLRVDPGPNLIC
chitinase (EC	Zea mays	268	QLVALGLALLCAVAGPAAAQNCGC
3.2.1.14)			QPNVCCSKFGYCGTTDEYCGDGCQ
precursor			SGPCRSGRGGGGSGGGGANVASVV
			TSSFFNGIKNQAGSGCEGKNFYTR
			SAFLSAVKGYPGFAHGGSQVQGKR
			EIAAFFAHATHETGHFCYISEINK
			SNAYCDPTKRQWPCAAGQKYYGRG
			PLQISWNYNYGPAGRAIGFDGLGD
			PGRVARDAVVAFKAALWFWMNSVH
			GVVPQGFGATTRAMQRALECGGNN
			PAQMNARVGYYRQYCRQLGVDPGP
			NLTC
Chitinase,	Nicotiana	377	MANSVTLFAIIFSCFLLQQLVCTN
class V	tabacum		SQNVKGGYWFKDSGLALNNIDSTL
			ETHLFCAFADLNPQLNQLIISPEN
			QDSFRQFTSTVQRKNPSVKTFLSI
			AGGRANSTAYGIMARQPNSRKSFI
			DSSIRLARQLGFHGLDLDWEYPLS
			AADMTNLGTLLNEWRTAINTEARN
			SGRAALLLTAAVSNSPRVNGLNYP
			VESLARNLDWINLMAYDFYGPNWS
			PSQTNSHAQLFDPVNHVSGSDGIN
			AWIQAGVPTKKLVLGIPFYGYAWR
			LVNANIHGLRAPAAGKSNVGAVDD
			GSMTYNRIRDYIVESRATTVYNAT
			IVGDYCYSGSNWISYDDTQTVRNK
			VNYVKGRGLLGYFAWHVAGDQNWG
			LSRTASQTWGVSFQEMK
Chitin-	Hydrangea	15	NSMERVEELRKKLQD
binding	macrophylla
protein HM30
(Fragment)
Chitin-binding	Hordeum	52	ATYHYYRPAQNNWDLGAPAVSAYC
protein N, CBP	vulgare		ATWDASKYGWTAFIVDQCANGGLD
N (Fragments)			LDWN
Circulin A	Chassalia	30	GIPCGESCVWIPCISAALGCSCKN
(CIRA)	parviflora		KVCYRN
Circulin B	Chassalia	31	GVIPCGESCVFIPCISTLLGCSCK
(CIRB)	parviflora		NKVCYRN
Cyclo-	Psychotria	31	SIPCGESCVFIPCTVTALLGCSCK
psychotride A	longipes		SKVCYKN
(CPT)
Cysteine-rich	Brassica	27	QKLCERPSGTWSGVCGNNNACKNQ
antifungal	rapa		CIN
protein 1
(AFP1)
(Fragment)
Cysteine-rich	Sinapis alba	51	QKLCERPSGTWSGVCGNNNACKNQ
antifungal			CINLEKARHGSCNYVFPAHKCICY
protein 1			FPC
(AFP1) (M1)
Cysteine-rich	Raphanus	80	MAKFASIIALLFAALVLFAAFEAP
antifungal	sativus		TMVEAQKLCERPSGTWSGVCGNNN
protein 1			ACKNQCINLEKARHGSCNYVFPAH
precursor			KCICYFPC
(AFP1)
Cysteine-rich	Arabidopsis	80	MAKSATIVTLFFAALVFFAALEAP
antifungal	thaliana		MVVEAQKLCERPSGTWSGVCGNSN
protein 1			ACKNQCINLEKARHGSCNYVFPAH
precursor			KCICYFPC
(AFP1)
(Anther-
specific
protein S18
homolog)
Cysteine-rich	Brassica	23	QKLCERPSGTWSGVCGNNNACKN
antifungal	napus
protein 2
(AFP2)
(Fragment)
Cysteine-rich	Brassica	27	QKLCERPSGTXSGVCGNNNACKNQ
antifungal	rapa		CIR
protein 2
(AFP2)
(Fragment)
Cysteine-rich	Raphanus	80	MAKFASIIVLLFVALVVFAAFEEP
antifungal	sativus		TMVEAQKLCQRPSGTWSGVCGNNN
protein 2			ACKNQCIRLEKARHGSCNYVFPAH
precursor			KCICYFPC
(AFP2)
Cysteine-rich	Sinapis alba	51	QKLCQRPSGTWSGVCGNNNACRNQ
antifungal			CINLEKARHGSCNYVFPAHKCICY
protein 2A			FPC
(AFP2A) (M2A)
Cysteine-rich	Sinapis alba	52	QKLCARPSGTWNSSGNCRNNNACR
antifungal			NFCIKLEKSRHGSCNIPFPSNKCI
protein 2B			CYFPC
(AFP2B) (M2B)
Cysteine-rich	Brassica	79	MAKFASIITLLFAALVVFAAFEAP
antifungal	napus		TMVEAKLCERSSGTWSGVCGNNNA
protein 3			CKNQCIRLEGAQHGSCNYVFPAHK
precursor			CICYFPC
(AFP3)
Cysteine-rich	Raphanus	79	MAKFASIVALLFAALVVFAAFEAP
antifungal	sativus		TVVEAKLCERSSGTWSGVCGNNNA
protein 3			CKNQCIRLEGAQHGSCNYVFPAHK
precursor			CICYFPC
(AFP3)
Cysteine-rich	Raphanus	80	MAKFVSIITLLFVALVLFAAFEAP
antifungal	sativus		TMVEAQKLCERSSGTWSGVCGNNN
protein 4			ACKNQCINLEGARHGSCNYIFPYH
precursor			RCICYFPC
(AFP4)
Defense-	Pisum	46	KTCEHLADTYRGVCFTNASCDDHC
related	sativum		KNKAHLISGTCHNWKCFCTQNC
peptide 1
(Defensin 1)
(Antifungal
protein Psd1)
Defense-	Pisum	47	KTCENLSGTFKGPCIPDGNCNKHC
related	sativum		RNNEHLLSGRCRDDFRCWCTNRC
peptide 2
(Defensin 2)
(Antifungal
protein Psd2)
defensin	Capsicum	75	MAGFSKVIATIFLMMMLVFATDMM
	annuum		AEAKICEALSGNFKGLCLSSRDCG
			NVCRREGFTSGVCRGFPLKCFCRK
			PGA
Defensin	Brassica	80	MAKFVSIITLFFAALVLFAAFEAP
	rapa		TMVKAQKLCERSSGTWSGVCGNNN
			ACKNQCINLEGARHGSCNYVFPYH
			RCICYFPC
Defensin	Helianthus	108	MAKISVAFNAFLLLLFVLAISEIG
	annuus		SVKGELCEKASQTWSGTCGKTKHC
			DDQCKSWEGAAHGACHVRDGKHMC
			FCYFNCSKAQKLAQDKLRAEELAK
			EKIEPEKATAKP
Defensin	Helianthus	41	SHRFQGTCLSDTNCANVCHSERFS
(Fragment)	annuus		GGKCRGFRRRCFCTTHC
defensin 1	Triticum	82	MASTRRMAAAPAVLLLLLLLVATE
precursor	aestivum		MGTMKTAEARTCLSQSHKFKGTCL
			SNSNCAAVCRTENFPDGECNTHLV
			ERKCYCKRTC
defensin AFP1	Heuchera	54	DGVKLCDVPSGTWSGHCGSSSKCS
	sanguinea		QQCKDREHFAYGGACHYQFPSVKC
			FCKRQC
defensin AMP1	Dahlia	50	ELCEKASKTWSGNCGNTGHCDNQC
	merckii		KSWEGAAHGACHVRNGKHMCFCYF
			NC
defensin AMP1	Aesculus	50	LCNERPSQTWSGNCGNTAHCDKQC
	hippocastanum		QDWEKASHGACHKRENHWKCFCYF
			NC
defensin AMP1	Clitoria	49	NLCERASLTWTGNCGNTGHCDTQC
	ternatea		RNWESAKHGACHKRGNWKCFCYFN
			C
defensin AMP2	Dahlia	20	EVCEKASKTWSGNCGNTGHC
	merckii
Defensin CUA1	Helianthus	42	LSHSFKGTCLSDTNCANVCHSERF
(Fragment)	annuus		SGGKCRGFRRRCFCTTHC
Defensin	Elaeis	77	MEHSRRMLPAILLLLFLLMPSEMG
EGAD1	guineensis		TKVAEARTCESQSHKFQGTCLRES
			NCANVCQTEGFQGGVCRGVRRRCF
			CTRLC
Defensin J1-1	Capsicum	75	MAGFSKVVATIFLMMLLVFATDMM
precursor	annuum		AEAKICEASGNFKGLCLSSRDCGN
			VCRREGFTDGSCIGFRLQCFCTKP
			CA
Defensin J1-2	Capsicum	74	MAGFSKVIATIFLMMMLVFATGMV
precursor	annuum		AEARTCESQSHRFKGLCFSKSNCG
			SVCHTEGFNGGHCRGFRRRCFCTR
			HC
Defensin	Brassica	80	MAKVASIVALLFPALVIFAAFEAP
precursor	oleracea		TMVEAQKLCERPSGWNSGVCGNN
			NACKNQCIRLEKARHGSCNYVFPA
			HKCICYFPC
Defensin	Prunus	79	MERSMRLFSTAFVFFLLLAAAGMM
protein 1	persica		MGPMVAEARTCESQSNRFKGTCVS
			TSNCASVCQTEGFPGGHCRGFRRR
			CFCTKHC
Endochitinase	Zea mays	280	MANAPRILALGLLALLCAAAGPAA
A precursor			AQNCGCQPNFCCSKFGYCGTTDAY
(EC 3.2.1.14)			CGDGCQSGPCRSGGGGGGGGGGGG
(Seed			GGSGGANVANVVTDAFFNGIKNQA
chitinase A)			GSGCEGKNFYTRSAFLSAVNAYPG
			FAHGGTEVEGKREIAAFFAHVTHE
			TGHFCYISEINKSNAYCDASNRQW
			PCAAGQKYYGRGPLQISWNYNYGP
			AGRDIGFNGLADPNRVAQDAVIAF
			KTALWFWMNNVHGVMPQGFGATIR
			AINGALECNGNNPAQMNARVGYYK
			QYCQQLRVDPGPNLIC
Endochitinase	Zea mays	269	PQLVALGLALLCAVAGPAAAQNCG
B precursor			CQPNVCCSKFGYCGTTDEYCGDGC
(EC 3.2.1.14)			QSGPCRSGRGGGGSGGGGANVASV
(Seed			VTSSFFNGIKNQAGSGCEGKNFYT
chitinase B)			RSAFLSAVKGYPGFAHGGSQVQGK
(Fragment)			REIAAFFAHATHETGHFCYISEIN
			KSNAYCDPTKRQWPCAAGQKYYGR
			GPLQISWNYNYGPAGRAIGFDGLG
			DPGRVARDAVVAFKAALWFWMNSV
			HGVVPQGFGATTRAMQRALECGGN
			NPAQMNARVGYYRQYCRQLGVDPG
			PNLTC
Fabatin-1	Vicia faba	47	LLGRCKVKSNRFHGPCLTDTHCST
			VCRGEGYKGGDCHGLRRRCMCLC
Fabatin-2	Vicia faba	47	LLGRCKVKSNRFNGPCLTDTHCST
			VCRGEGYKGGDCHGLRRRCMCLC
Floral	Petunia x	103	MARSICFFAVAILALMLFAAYDAE
defensin-like	hybrida		AATCKAECPTWDSVCINKKPCVAC
protein 1			CKKAKFSDGHCSKILRRCLCTKEC
			VFEKTEATQTETFTKDVNTLAEAL
			LEADMMV
Floral	Petunia x	101	MARSICFFAVAILALMLFAAYETE
defensin-like	hybrida		AGTCKAECPTWEGICINKAPCVKC
protein 2			CKAQPEKFTDGHCSKILRRCLCTK
			PCATEEATATLANEVKTMAEALVE
			EDMME
Flower-	Helianthus	78	MKSSMKMFAALLLVVMCLLANEMG
specific	annuus		GPLVVEARTCESQSHKFKGTCLSD
gamma-thionin			TNCANVCHSERFSGGKCRGFRRRC
precursor			FCTTHC
(Defensin
SD2)
Gamma-thionin	Arabidopsis	77	MKLSMRLISAVLIMFMIFVATGMG
homolog	thaliana		PVTVEARTCESQSHRFKGTCVSAS
At2g02100			NCANVCHNEGFVGGNCRGFRRRCF
precursor			CTRHC
Gamma-thionin	Arabidopsis	77	MKFSMRLISAVLFLVMIFVATGMG
homolog	thaliana		PVTVEARTCASQSQRFKGKCVSDT
At2g02120			NCENVCHNEGFPGGDCRGFRRRCF
precursor			CTRNC
Gamma-thionin	Arabidopsis	77	MKLSVRFISAALLLFMVFIATGMG
homolog	thaliana		PVTVEARTCESKSHRFKGPCVSTH
At2g02130			NCANVCHNEGFGGGKCRGFRRRCY
precursor			CTRHC
Gamma-thionin	Arabidopsis	73	MKLSLRLISALLMSVMLLFATGMG
homolog	thaliana		PVEARTCESPSNKFQGVCLNSQSC
At2g02140			AKACPSEGFSGGRCSSLRCYCSKA
precursor			C
Gamma-	Eutrema	80	MAKFASIIALLFAALVLFSAFEAP
thionin 1	wasabi		SMVEAQKLCEKSSGTWSGVCGNNN
precursor			ACKNQCINLEGARHGSCNYIFPYH
			RCICYFPC
gamma-	Lycopersicon	105	MARSIFFMAFLVLAMMLFVTYEVE
thionin-like	esculentum		AQQICKAPSQTFPGLCFMDSSCRK
protein			YCIKEKFTGGHCSKLQRKCLCTKP
precursor			CVFDKISSEVKATLGEEAKTLSEW
			LEEEIMME
Gastrodianin-	Gastrodia	171	MAASASTAVILFFAVTTMMSLSAI
MGM protein	elata		PAFASDRLNSGHQLDTGGSLAQGG
			YLFIIQNDCNLVLYDNNRAVWASG
			TNGKASGCMLKMQNDGNLVIYSGS
			RAIWASNTNRQNGNYYLILQRDRN
			VVIYDNSNNAIWATHTNVGNAEIT
			VIPHSNGTAAASGAAQNKVNELYI
			SMY
Gastrodianin-	Gastrodia	171	MAASASTAVILFFAVTTMMSLSAI
MNF protein	elata		PAFASDRLNSGHQLDTGGSLAQGG
			YLFIIQNDCNLVLYDNNRAVWASG
			TNGKASNCFLKMQNDGNLVIYSGS
			RAIWASNTNRQNGNYYLILQRDRN
			VVIYDNSNNAIWATHTNVGNAEIT
			VIPHSNGTAAASGAAQNKVNELYI
			SMY
Gastrodianin-	Gastrodia	171	MAASASTAVILFFAVTTVMSLSAI
VGM protein	elata		PAFASDRLNSGHQLDTGGSLAQGG
			YLFIIQNDCNLVLYDNNRAVWASG
			TNGKASGCMLKMQNDGNLVIYSGS
			RAIWASNTNRQNGNYYLILQRDRN
			VVIYDNSNNAIWATHTNVGNAEIT
			VIPHSNGTAAASGAAQNKVNELYI
			SMY
Gastrodianin-	Gastrodia	171	MAASASTAVILFFAVTTVMSLSAI
VNF protein	elata		PAFASDRLNSGHQLDTGGSLAQGG
			YLFIIQNDCNLVLYDNNRAVWASG
			TNGKASNCFLKMQNDGNLVIYSGS
			RAIWASNTNRQNGNYYLILQRDRN
			VVIYDNSNNAIWATHTNVGNAEIT
			VIPHSNGTAAASGAAQNKVNELYI
			SMY
Genomic DNA,	Arabidopsis	73	MENKFFAAFFLLLVLFSSQEIIGG
chromosome 5,	thaliana		EGRTCQSKSHHFKYMCTSNHNCAI
P1 clone:MBK5			VCRNEGFSGGRCHGFHRRCYCTRL
			C
Ginkbilobin	Ginkgo	40	ANTAFVSSAHNTQKIPAGAPFNRN
(GNL)	biloba		LRAMLADLRQNAAFAG
(Fragment)
Hevein	Hevea	204	MNIFIVVLLCLTGVAIAEQCGRQA
precursor	brasiliensis		GGKLCPNNLCCSQWGWCGSTDEYC
(Major			SPDHNCQSNCKDSGEGVGGGSASN
hevein)			VLATYHLYNSQDHGWDLNAASAYC
[Contains:			STWDANKPYSWRSKYGWTAFCGPV
Hevein			GAHGQSSCGKCLSVTNTGTGAKTT
(Allergen Hev			VRIVDQCSNGGLDLDVNVFRQLDT
b 6); Win-			DGKGYERGHITVNYQFVDCGDSFN
like protein]			PLFSVMKSSVIN
hevein-like	Euonymus	320	MKYLWVFIVFSIAVLSHACSAQQC
antimicrobial	europaeus		GRQAGNRRCANNLCCSQYGYCGRT
peptide			NEYCCTSQGCQSQCRRCGVRTVGE
			IVVGDIGGIISKGMFNNILKHRDD
			DACEGKGFYTYEAFVAAARSFPAF
			GSTGDDATRKREIAAFLAQTSHET
			SAGWPSAPDGPYAWGYCFVRERNP
			PSKYCDTTTPCPKSYYGRGPIQLT
			WNYNYEQAGRAIGADLLNNPDLVA
			TDAVISFKTAIWFWMTAQSSKPSC
			HDVITGSWRPSASDNSVCHVPDYA
			VVTNIISGEIEYGKSRNPQVEDRI
			EFFKRYCQILGVSPGKCYEERTFV
			SGLMMETI
hevein-like	Euonymus	305	MKYLWVFIVFSIAVLSLACSAQQC
antimicrobial	europaeus		GRQAGNRRCPNNLCCSQFGYCGRT
peptide			NEYCCTGFGCQSNCRRCGVRTVGE
			DVVGDIGGIISKGMFNNILKHRDD
			DACEGKGFYTYEAFVAAARSFPAF
			GSTGDDTTRKREIAAFLAQTSHET
			SGGRPSAPDGPYAWGYCFVKERNP
			PSKYCDTITPCPKSYYGRGPLQLT
			WNYNYAQAGRAIGVDLLNNPDLVA
			TDAVTSFKTAIWFWMTAHSSKPSC
			HDVITGSWRPSASDNSVRHVPDYA
			VVTNIINGEIEYGKSRNPQVEDRI
			EFFKRYCQILGVSPGKF
Leaf-specific	Hordeum	137	MAPSKSIKSVVICVLILGLVLEQV
thionin	vulgare		QVEGKSCCKDTLARNCYNTCHFAG
precursor			GSRPVCAGACRCKIISGPKCPSDY
(Clone DB4)			PKLNLLPESGEPDVTQYCTIGCRN
			SVCDNMDNVFRGQEMKFDMGLCSN
			ACARFCNDGAVIQSVEA
Lectin-like	Gastrodia	111	QSSPGILLNQPASMASPASSAVIF
protein	elata		FFAVAALMSLLAMPALAASQLNAG
(Fragment)			QTLGTGQSLAQGPNQFIIQNDCNL
			VLYASNKAVWATGTNGKASGCVLR
			MQRDGNLVIYSGSKV
Nicotiana	Nicotiana	47	RECKTESNTFPGICITKPPCRKAC
Alata Plant	tabacum		ISEKFTDGHCSKILRRCLCTKPC
Defensin 1
(Nad1)
osmotin	Nicotiana	250	MSNNMGNLRSSFVFFLLALVTYTY
precursor	tabacum		AATIEVRNNCPYTVWAASTPIGGG
			RRLDRGQTWVINAPRGTKMARVWG
			RTNCNFNAAGRGTCQTGDCGGVLQ
			CTGWGKPPNTLAEYALDQFSGLDF
			WDISLVDGFNIPMTFAPTNPSGGK
			CHAIHCTANINGECPRELRVPGGC
			NNPCTTFGGQQYCCTQGPCGPTFF
			SKFFKQRCPDAYSYPQDDPTSTFT
			CPGGSTNYRVIFCPNGQAHPNFPL
			EMPGSDEVAK
Osmotin-like	Nicotiana	251	MSHLTTFLVFFLLAFVTYTYASGV
protein	tabacum		FEVHNNCPYTVWAAATPVGGGRRL
precursor			ERGQSWWFWAPPGTKMARIWGRTN
(Patho-			CNFDGAGRGWCQTGDCGGVLECKG
genesis-			WGKPPNTLAEYALNQFSNLDFWDI
related			SVIDGFNIPMSFGPTKPGPGKCHG
protein PR-			IQCTANINGECPGSLRVPGGCNNP
5D)			CTTFGGQQYCCTQGPCGPTELSRW
			FKQRCPDAYSYPQDDPTSTFTCTS
			WTTDYKVMFCPYGSAHNETTNFPL
			EMPTSTHEVAK
Osmotin-like	Lycopersicon	238	FFFLLAFVTYTYAATFEVRNNCPY
protein TPM-1	esculentum		TVWAASTPIGGGRRLDRGQTWVIN
precursor (PR			APRGTKMARIWGRTNCNFDGDGRG
P23)			SCQTGDCGGVLQCTGWGKPPNTLA
(Fragment)			EYALDQFSNLDFWDISLVDGFNIP
			MTFAPTNPSGGKCHAIHCTANING
			ECPGSLRVPGGCNNPCTTFGGQQY
			CCTQGPCGPTDLSRFFKQRCPDAY
			SYPQDDPTSTFTCPSGSTNYRVVF
			CPNGVTSPNFPLEMPSSDEEAK
pathogenesis-	Lycopersicon	233	AFVTYTYAATFEVRNNCPYTVWAA
related	esculentum		STPIGGGRRLDRGQTWVINAPRGT
protein P23			KMARIWGRTNCNFDGAGRGSCQTG
precursor			DCGGVLQCTGWGKPPNTLAEYALD
			QFSNLDFWDISLVDGFNIPMTFAP
			TNPSGGKCHAIHCTANINGECPGS
			LRVPGGCNNPCTTFGGQQYCCTQG
			PCGPTDLSRFFKQRCPDAYSYPQD
			DPTSTFTCPSGSTNYRVVFCPNGV
			TSPNFPLEMPSSDEEAK
plant	Arabidopsis	76	MKVSPRLNSALLLLFMILATVMGL
defensin	thaliana		VTVEARTCETSSNLFNGPCLSSSN
protein,			CANVCHNEGFSDGDCRGFRRRCLC
putative			TRPC
(PDF2.4)
plant	Arabidopsis	122	MERIPSLASLVSLLIIFATVVNQT
defensin-	thaliana		RASICNDRLGLCDGCDQRCKAKHG
fusion			PSCESKCDGPVGMLLCTCTYECGP
protein,			TKLCNGGLGNCGESCNEQCCDRNC
putative			AQRYNGGHGYCNTLDDFSLCLCKY
			PC
Plant	Pyrus	81	LVSTAFVLVLLLATIEMGPMGVEA
defensin-like	pyrifolia		RTESSKAVEGKICEVPSTLFKGLC
protein			FSSNNCKHTCRKEQFTRGHCSVLT
(Fragment)			RACVCTKKC
probable	Arabidopsis	80	MAKFCTTITLILVALVLFADFEAP
antifungal	thaliana		TIVKAELCKRESETWSGRCVNDYQ
protein			CRDHCINNDRGNDGYCAGGYPWYR
[imported]			SCFCFFSC
Probable	Arabidopsis	80	MAKSAAIITFLFAALVLFAAFEAP
cysteine-rich	thaliana		IMVEAQKLCEKPSGTWSGVCGNSN
antifungal			ACKNQCINLEGAKHGSCNYVFPAH
protein			KCICYFPC
At2g26010
precursor
(AFP)
Probable	Arabidopsis	80	MAKFASIITFIYAALVLFAAFEVP
cysteine-rich	thaliana		TMVEAQKLCEKPSGTWSGVCGNSN
antifungal			ACKNQCINLEGAKHGSCNYVFPAH
protein			KCICYVPC
At2g26020
precursor
(AFP)
Probable	Arabidopsis	80	MAKFASIITLIFAALVLFAAFDAP
cysteine-rich	thaliana		AMVEAQKLCEKPSGTWSGVCGNSN
antifungal			ACKNQCINLEGAKHGSCNYVFPAH
protein LCR77			KCICYVPC
precursor
(AFP)
Protease	Pyrus	87	MEPSMRLISAAFVLILLLATTEMG
inhibitor-	pyrifolia		PMGVEAKSKSSKEVEKRTCEAASG
like protein			KFKGMCFSSNNCANTCAREKFDGG
			KCKGFRRRCMCTKKC
Protease	Pyrus	87	MERSMRLVSAAFVLVLLLAATEMG
inhibitor-	pyrifolia		PMGVEARTESSKAVEGKICEVPST
like protein			LFKGLCFSSNNCKHTCRKEQFTRG
			HCSVLTRACVCTKKC
Proteinase	Capsicum	78	MAHSMRFFAIVLLLAMLVMATEMG
inhibitor	annuum		PMRIVEARTCESQSHRFKGVCASE
precursor			TNCASVCQTEGFSGGDCRGFRRRC
			FCTRPC
Putative	Arabidopsis	78	MASSYTLMLFLCLSIFLIASTEMM
defensin AMP1	thaliana		AVEGRICERRSKTWTGFCGNTRGC
protein			DSQCKRWERASHGACHAQFPGFAC
			FCYFNC
Putative	Picea abies	83	MADKGVGSRLSALFLLVLLVISIG
plant			MMQLEPAEGRTCKTPSGKFKGVCA
defensin			SRNNCKNVCQTEGFPSGSCDFHVA
SPI1B			NRKCYCSKPCP
sormatin	Sorghum	22	AVFTVVNRCPYTVWAASVPVGG
	bicolor
TOM P14A	Lycopersicon	41	AVHNDARAQVGVGPMSXDANLASR
protein	esculentum		AQNYANSRAXDXNLIXS
(Fragment)
TOM P14B	Lycopersicon	35	DXLAVHNDARAQVGAGPMDANLAS
pathogenesis-	esculentum		RAQNXANSRAG
related PR-1
protein
(Fragments)
TOM P14C	Lycopersicon	97	DYLNAHNAARRQVGVGPMTXDNRL
pathogenesis-	esculentum		AAFAQNYANQRADXRMQHSGGPYG
related PR-1			ENLAAAFPQLNCQAGKVCGHYTQV
protein			VWRNSVRLGCARVRCNNGWYFITC
(Fragments)			N
trimatin	Triticum	23	ATITVVNRCSYTVWPGALPGGGA
	aestivum
Vicilin	Macadamia	666	MAINTSNLCSLLFLLSLFLLSTTV
	integrifolia		SLAESEFDRQEYEECKRQCMQLET
			SGQMRRCVSQCDKRFEEDIDWSKY
			DNQDDPQTDCQQCQRRCRQQESGP
			RQQQYCQRRCKEICEEEEEYNRQR
			DPQQQYEQCQERCQRHETEPRHMQ
			TCQQRCERRYEKEKRKQQKRYEEQ
			QREDEEKYEERMKEEDNKRDPQQR
			EYEDCRRRCEQQEPRQQYQCQRRC
			REQQRQHGRGGDLINPQRGGSGRY
			EEGEEKQSDNPYYFDERSLSTRFR
			TEEGHISVLENFYGRSKLLRALKN
			YRLVLLEANPNAFVLPTHLDADAI
			LLVTGGRGALKMIHRDNRESYNLE
			CGDVIRIPAGTTFYLINRDNNERL
			HIAKFLQTISTPGQYKEFFPAGGQ
			NPEPYLSTFSKEILEAALNTQAER
			LRGVLGQQREGVIISASQEQIREL
			TRDDSESRRWHIRRGGESSRGPYN
			LFNKRPLYSNKYGQAYEVKPEDYR
			QLQDMDVSVFIANITQGSMMGPFF
			NTRSTKVVVVASGEADVEMACPHL
			SGRHGGRRGGKRHEEEEDVHYEQV
			KARLSKREAIVVPVGHPVVFVSSG
			NENLLLFAFGINAQNNHENFLAGR
			ERNVLQQIEPQAMELAFAAPRKEV
			EELFNSQDESIFFPGPRQHQQQSS
			RSTKQQQPLVSILDFVGF
Vicilin	Macadamia	666	MAINTSNLCSLLFLLSLFLLSTTV
	integrifolia		SLAESEFDRQEYEECKRQCMQLET
			SGQMRRCVSQCDKRFEEDIDWSKY
			DNQEDPQTECQQCQRRCRQQESGP
			RQQQYCQRRCKEICEEEEEYNRQR
			DPQQQYEQCQKHCQRRETEPRHMQ
			TCQQRCERRYEKEKRKQQKRYEEQ
			QREDEEKYEERMKEEDNKRDPQQR
			EYEDCRRRCEQQEPRQQHQCQLRC
			REQQRQHGRGGDMMNPQRGGSGRY
			EEGEEEQSDNPYYFDERSLSTRFR
			TEEGHISVLENFYGRSKLLRALKN
			YRLVLLEANPNAFVLPTHLDADAI
			LLVIGGRGALKMIHHDNRESYNLE
			CGDVIRIPAGTTFYLINRDNNERL
			HIAKFLQTISTPGQYKEFFPAGGQ
			NPEPYLSTFSKEILEAALNTQTEK
			LRGVFGQQREGVIIRASQEQIREL
			TRDDSESRHWHIRRGGESSRGPYN
			LFNKRPLYSNKYGQAYEVKPEDYR
			QLQDMDLSVFIANVTQGSMMGPFF
			NTRSTKVVVVASGEADVEMACPHL
			SGRHGGRGGGKRHEEEEDVHYEQV
			RARLSKREAIVVLAGHPVVFVSSG
			NENLLLFAFGINAQNNHENFLAGR
			ERNVLQQIEPQAMELAFAAPRKEV
			EESFNSQDQSIFFPGPRQHQQQSP
			RSTKQQQPLVSILDFVGF
Vicilin	Macadamia	625	QCMQLETSGQMRRCVSQCDKRFEE
(Fragment)	integrifolia		DIDWSKYDNQEDPQTECQQCQRRC
			RQQESDPRQQQYCQRRCKEICEEE
			EEYNRQRDPQQQYEQCQKRCQRRE
			TEPRHMQICQQRCERRYEKEKRKQ
			QKRYEEQQREDEEKYEERMKEGDN
			KRDPQQREYEDCRRHCEQQEPRLQ
			YQCQRRCQEQQRQHGRGGDLMNPQ
			RGGSGRYEEGEEKQSDNPYYFDER
			SLSTRFRTEEGHISVLENFYGRSK
			LLRALKNYRLVLLEANPNAFVLPT
			HLDADAILLVIGGRGALKMIHRDN
			RESYNLECGDVIRIPAGTTFYLIN
			RDNNERLHIAKFLQTISTPGQYKE
			FFPAGGQNPEPYLSTFSKEILEAA
			LNTQTERLRGVLGQQREGVIIRAS
			QEQIRELTRDDSESRRWHIRRGGE
			SSRGPYNLFNKRPLYSNKYGQAYE
			VKPEDYRQLQDMDVSVFIANITQG
			SMMGPFFNTRSTKVVVVASGEADV
			EMACPHLSGRHGGRGGGKRHEEEE
			EVHYEQVRARLSKREAIVVLAGHP
			VVFVSSGNENLLLFAFGINAQNNH
			ENFLAGRERNVLQQIEPQAMELAF
			AASRKEVEELFNSQDESIFFPGPR
			QHQQQSPRSTKQQQPLVSILDFVG
			F
Wheatwin1	Triticum	146	MAARPMLVVALLCAAAAAATAQQA
precursor	aestivum		TNVRATYHYYRPAQNNWDLGAPAV
(Patho-			SAYCATWDASKPLSWRSKYGWTAF
genesis-			CGPAGAHGQASCGKCLQVTNPATG
related			AQITARIVDQCANGGLDLDWDTVF
protein 4a)			TKIDTNGIGYQQGHLNVNYQFVDC
(Protein			RD
0.14)
Wheatwin2	Triticum	148	MTMAARLMLVAALLCAAAAAATAQ
precursor	aestivum		QATNVRATYHYYRPAQNNWDLGAP
(Patho-			AVSAYCATWDASKPLSWRSKYGWT
genesis-			AFCGPAGAHGQAACGKCLRVTNPA
related			TGAQITARIVDQCANGGLDLDWDT
protein 4b)			VFTKIDTNGIGYQQGHLNVNYQFV
			DCRD
Zeamatin	Zea mays	206	AVFTVVNQCPFTVWAASVPVGGGR
			QLNRGESWRITAPAGTTAARIWAR
			TGCKFDASGRGSCRTGDCGGVLQC
			TGYGRAPNTLAEYALKQFNNLDFF
			DISLIDGFNVPMSFLPDGGSGCSR
			GPRCAVDVNARCPAELRQDGVCNN
			ACPVFKKDEYCCVGSAANDCHPTN
			YSRYFKGQCPDAYSYPKDDATSTF
			TCPAGTNYKVVFCP
Zeamatin	Zea mays	227	MAGSVAIVGIFVALLAVAGEAAVF
precursor			TVVNQCPFTVWAASVPVGGGRQLN
			RGESWRITAPAGTTAARIWARTGC
			KFDASGRGSCRTGDCGGVLQCTGY
			GRAPNTLAEYALKQFNNLDFFDIS
			LIDGFNVPMSFLPDGGSGCSRGPR
			CAVDVNARCPAELRQDGVCNNACP
			VFKKDEYCCVGSAANDCHPTNYSR
			YFKGQCPDAYSYPKDDATSTFTCP
			AGTNYKVVFCP

TABLE 2
{PRIVATE} Defensins
Name	Organism	Sequence
HNP-1	Human	ACYCRIPACIAGERRYGTCIYQGRLWAFCC
HNP-2	Human	C YCRIPACIAGERRYGTCIYQGRLWAFCC
HNP-3	Human	DCYCRIPACIAGERRYGTCIYQGRLWAFCC
HNP-4	Human	VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRV
NP-1	Rabbit	VVCACRRALCLPRERRAGFCRIRGRIHPLCCRR
NP-2	Rabbit	VVCACRRALCLPLERRAGFCRIRGRIHPLCCRR
NP-3A	Rabbit	GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR
NP-3B	Rabbit	GRCVCRKQLLCSYRERRIGDCKIRGVRFPFCCPR
NP-4	Rabbit	VSCTCRRFSCGFGERASGSCTVNGVRHTLCCRR
NP-5	Rabbit	VFCTCRGFLCGSGERASGSCTINGVRHTLCCRR
RatNP-1	Rat	VTCYCRRTRCGFRERLSGACGYRGRIYRLCCR
Rat-NP-3	Rat	C SCRYSSCRFGERLLSGACRLNGRIYRLCC
Rat-NP-4	Rat	ACTCRIGACVSGERLTGACGLNGRIYRLCCR
GPNP	Guinea pig	RRCICTTRTCRFPYRRLGTCIFQNRVYTFCC

B. Growth Factors

In some embodiments of the present invention, trophic factor combinations for treating injured nervous systems comprise one or more growth factors. Growth factors useful in the present invention include, but are not limited to, the following broad classes of cytoactive compounds: Insulin, Insulin like growth factors such as IGF-I, IGF-IB, IGF-II, and IGF-BP; Heparin-binding growth factors such as Pleiotrophin (NEGF1) and Midkine (NEGF2); PC-cell derived growth factors (PCDGF); Epidermal Growth Factors such as α-EGF and β-EGF; EGF-like molecules such as Keratinocyte-derived growth factor (which is identical to KAF, KDGF, and amphiregulin) and vaccinia virus growth factor (VVGF); Fibroblast Growth Factors such as FGF-1 (Basic FGF Protein), FGF-2 (Acidic FGF Protein), FGF-3 (Int-2), FGF-4 (Hst-1), FGF-5, FGF-6, and FGF-7 (identical to KGF); FGF-Related Growth Factors such as Endothelial Cell Growth Factors (e.g., ECGF-α and ECGF-β); FGF- and ECGF-Related Growth Factors such as Endothelial cell stimulating angiogenesis factor and Tumor angiogenesis factor, Retina-Derived Growth Factor (RDGF), Vascular endothelium growth factors (VEGF, VEGF-B, VEGF-C, and VEGF-D), Brain-Derived Growth Factor (BDGF A- and -B), Astroglial Growth Factors (AGF 1 and 2), Omentum-derived factor (ODF), Fibroblast-Stimulating factor (FSF), and Embryonal Carcinoma-Derived Growth Factor; Neurotrophic Growth Factors such as α-NGF, β-NGF, γ-NGF, Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF); Glial Growth Factors such as GGF-I, GGF-II, GGF-III, Glia Maturation Factor (GMF), and Glial-Derived Nuerotrophic Factor (GDNF); Organ-Specific Growth Factors such as Liver Growth Factors (e.g., Hepatopoietin A, Hepatopoietin B, and Hepatocyte Growth Factors (HCGF or HGF), Prostate Growth Factors (e.g., Prostate-Derived Growth Factors [PGF] and Bone Marrow-Derived Prostate Growth Factor), Mammary Growth Factors (e.g., Mammary-Derived Growth Factor 1 [MDGF-1] and Mammary Tumor-Derived Factor [MTGF]), and Heart Growth Factors (e.g., Nonmyocyte-Derived Growth Factor [NMDGF]); Cell-Specific Growth Factors such as Melanocyte Growth Factors (e.g., Melanocyte-Stimulating Hormone [α-, β-, and γ-MSH] and Melanoma Growth-Stimulating Activity [MGSA]), Angiogenic Factors (e.g., Angiogenin, Angiotropin, Platelet-Derived ECGF, VEGF, and Pleiotrophin), Transforming Growth Factors (e.g., TGF-α, TGF-β, and TGF-like Growth Factors such as TGF-β₂, TGF-β₃, TGF-e, GDF-1, GDF-9, CDGF and Tumor-Derived TGF-β-like Factors), ND-TGF, and Human epithelial transforming factor [h-TGFe]); Regulatory Peptides with Growth Factor-like Properties such as Bombesin and Bombesin-like peptides (e.g., Ranatensin, and Litorin], Angiotensin, Endothelin, Atrial Natriuretic Factor, Vasoactive Intestinal Peptide, and Bradykinin; Cytokines such as connective tissue growth factor (CTGF), the interleukins IL-1 (e.g., Osteoclast-activating factor (OAF), Lymphocyte-activating factor (LAF), Hepatocyte-stimulating factor (HSF), Fibroblast-activating factor (FAF), B-cell-activating factor (BAF), Tumor inhibitory factor 2 (TIF-2), Keratinocyte-derived T-cell growth factor (KD-TCGF)), IL-2 (T-cell growth factor (TCGF), T-cell mitogenic factor (TCMF)), IL-3 (e.g., Hematopoietin, Multipotential colony-stimulating factor (multi-CSF), Multilineage colony-stimulating activity (multi-CSA), Mast cell growth factor (MCGF), Erythroid burst-promoting activity (BPA-E), IL-4 (e.g., B-cell growth factor I (BCGF-I), B-cell stimulatory factor I (BSF-1)), IL-5 (e.g., B-cell growth factor II (BCGF-II), Eosinophil colony-stimulating factor (Eo-CSF), Immunoglobulin A-enhancing factor (IgA-EF), T-cell replacing factor (TCRF)), IL-6 (B-cell stimulatory factor 2 (BSF-2), B-cell hybridoma growth factor (BCHGF), Interferon β₂ (IFN-B), T-cell activating factor (TAF), IL-7 (e.g., Lymphopoietin 1 (LP-1), Pre-B-cell growth factor (pre-BCGF)), IL-8 (Monocyte-derived neutrophil chemotacetic factor (MDNCF), Granulocyte chemotatic factor (GCF), Neutrophil-activating peptide 1 (NAP-1), Leukocyte adhesion inhibitor (LAI), T-lymphocyte chemotacetic factor (TLCF)), IL-9 (e.g., T-cell growth factor III (TCGF-III), Factor P40, MegaKaryoblast growth factor (MKBGF), Mast cell growth enhancing activity (MEA or MCGEA)), IL-10 (e.g., Cytokine synthesis inhibitory factor (CSIF)), IL-11 (e.g., Stromal cell-derived cytokine (SCDC)), IL-12 (e.g., Natural killer cell stimulating factor (NKCSF or NKSF), Cytotoxic lymphocyte maturation factor (CLMF)), TNF-α (Cachectin), TNF-β (Lymphotoxin), LIF (Differentiation-inducing factor (DIF), Differentiation-inducing activity (DIA), D factor, Human interleukin for DA cells (HILDA), Hepatocyte stimulating factor III (HSF-III), Cholinergic neuronal differentiation factor (CNDF), CSF-1 (Macrophage colony-stimulating factor (M-CSF)), CSF-2 (Granulocyte-macrophage colony-stimulating factor (GM-CSF)), CSF-3 (Granulocyte colony-stimulating factor (G-CSF)), and erythropoietin; Platelet-derived growth factors (e.g., Placental growth factor (PlGF), PDGF-A, PDGF-B, PDGF-AB, p28-sis, and p26-cis), and Bone Morphogenetic proteins (e.g., BMP and BMP-15), neuropeptides (e.g., Substance P, calcitonin gene-regulated peptide, and neuropeptide Y), and neurotransmitters (e.g., norepinephrine and acetylcholine).

Suitable growth factors may be obtained from commercial sources, purified from natural sources, or be produced by recombinant methods. Recombinant growth factors can be produced from wild-type coding sequences or from variant sequences that encode functional growth factors. Suitable growth factors also include analogs that may be smaller peptides or other molecules having similar binding and biological activity as the natural growth factors. Methods for producing growth factors are described in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and 5,410,019; all of which are incorporated herein by reference.

C. Neurotrophins

The trophic factor combinations provided herein also can include one or more neurotrophic growth factors such as Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF).

Nerve growth factor s, such as α-NGF, β-NGF, γ-NGF, and the like, are neurotrophins. In an embodiment, the trophic factor combination does not include a nerve growth factor, which results in lessened pain.

D. Neuropeptides

The trophic factor combinations provided herein also can include one or more neuropeptides, e.g., PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide (MAB-alpha-NP); Beta-SG neuropeptide (MAB-beta-NP)); Pheromone biosynthesis activating neuropeptide (M); PBAN-type neuropeptides (e.g., Diapause hormone (DH); Alpha-SG neuropeptide (Alpha-SGNP); Beta-SG neuropeptide (Beta-SGNP); Pheromone biosynthesis activating neuropeptide I (PBAN-I) (BoM)); Neuropeptides B/W receptor type 2 (G protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7) (Fragment); neuropeptides [similarity]; Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide (PACAP)); Pol-RFamide neuropeptides; Antho-RFamide neuropeptides type 1; LWamide neuropeptides (e.g., LWamide I; Metamorphosin A (LWamide II) (MMA); LWamide III; LWamide IV; LWamide V; LWamide VI; LWamide VII; LWamide VIII; LWamide IX); Antho-RFamide neuropeptides type 2; Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide-27 (PACAP-27) (P)); Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide-27 (PACAP-27) (P)); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWS); Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide (PACAP)]; FMRFamide-like neuropeptides); PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide); Pheromone biosynthesis activating neuropeptide (AgI-PBAN); Gamma-SG neuropeptide; FMRFamide-related neuropeptides; Myomodulin neuropeptides (e.g., GLQMLRL-amide; QIPMLRL-amide; SMSMLRL-amide; SLSMLRL-amide; Myomodulin A (PMSMLRL-amide)); FMRFamide neuropeptides; neuropeptides (e.g., Substance P, calcitonin gene-regulated peptide, and neuropeptide Y); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWamide III; LWamide IV; LWamide V; LWamide VI; Metamorphosin A (MMA); Mwamide) (Fragment); PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide); Pheromone biosynthesis activating neuropeptide (HeA-PBAN); Gamma-SG neuropeptide; Antho-RFamide neuropeptides; Neuropeptides capa receptor (Cap2b receptor); Neuropeptides B/W receptor type 2 (G protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7); FMRFamide-like neuropeptides [e.g., Neuropeptide AF 10 (GFGDEMSMPGVLRF-amide); Neuropeptide AF20 (GMPGVLRF-amide); Neuropeptide AF3 (AVPGVLRF-amide); Neuropeptide AF4 (GDVPGVLRF-amide); N PBAN-type neuropeptides [e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide; Pheromone biosynthesis activating neuropeptide (HeZ-PBAN); Gamma-SG neuropeptide; FMRFamide neuropeptides type FMRF-1 (Fragment); Abdominal ganglion neuropeptides L5-67 (e.g., Luqin; Luqin-B; Luqin-C; Proline-rich mature peptide (PRMP)); FMRFamide neuropeptides type FMRF-2; FMRFamide neuropeptides type FMRF-4 (Fragment); Myomodulin neuropeptides (e.g., Myomodulin A (MM-A) (PMSMLRL-amide) (Neuron B16 peptide); Myomodulin B (MM-B) (GSYRMMRL-amide); Myomodulin D (MM-D) (GLSMLRL-amide); Myomodulin F (MM-F); LWamide neuropeptides (e.g., LWamide I; LWamide II; Metamorphosin A (MMA); Iwamide) (Fragment) (Substance P, calcitonin gene-regulated peptide, and neuropeptide Y.)

E. Other Components

The trophic factor combinations can be used with various delivery systems. In some embodiments, the trophic factor combination is mixed with a viscous substance to increase the viscosity of the combination. The increased viscosity retains the trophic factor combination at the site of the injury longer than it would be retained in the absence of the viscous substance. The viscous substance can be, for example, a polysaccharide, such as hyaluranic acid.

In another embodiment, the trophic factor combination is delivered in a slow release formula, such as in a matrix, for example, a woundhealing matrix, either with or without a viscous substance. In an embodiment, the matrix is a hydrogel, such as a hydrogel disclosed in U.S. Patent Application No. US 20030083389A1, which describes hydrogels wherein a polymer matrix is modified to contain a bifunctional poly(alkylene glycol) molecule covalently bonded to the polymer matrix. The hydrogels can be cross-linked using, for example, glutaraldehyde. The hydrogels can also be crosslinked via an interpenetrating network of a photopolymerizable acrylates. In one embodiment of the invention, the components of the trophic factor combination are incorporated into the hydrogel, for example, through covalent bonds to poly(alkylene glycol) molecules of the hydrogel or through entrainment within the hydrogel. In other embodiments, the matrix is a collagen gel matrix, which can be impregnated with a trophic factor combination. Other matrices can also be used.

The trophic factor combination can also be delivered in a base solution, such as UW solution (DuPont Critical Care, Waukegan, Ill.), or other base solutions.

The neurochemical combinations can be used in conjunction with cell therapy, where transfected cells are produced to release the ingredients and obtain continual delivery of a trophic factor combination. For example, embryonic or adult stem cells can be modified to express trophic factors, antimicrobial peptides, and other relevant neurochemicals, to deliver the trophic factor combination endogenously to the injured spinal cord. In the case of genetically modified cell transplants, the transfected cells can be tagged with cell surface antigens so that the cells can be controlled. For example, antibodies targeting the specific antigen could be used to kill the implanted cells after therapeutic results have been achieved.

Delivery of the neurochemical combinations can also be achieved by media with spaced supports, such as sponges, gels, or biopolymers.

F. Exemplary Formulations

A trophic factor combination includes one or more antimicrobial peptide and/or one or more substance having an antimicrobial peptide effect, alone or with one or more of the following trophic factors: growth factors, neuropeptides, and neurotrophins. Another trophic factor combination includes a viscous substance, such as hyaluronic acid, among others. Another trophic factor combination includes other cytoactive compounds, such as one or more cytokine and/or one or more chemokine. Non-limiting examples of these trophic factor combinations are provided in Tables 3a-3h below. It will be recognized that the trophic factor combinations can comprise one or more antimicrobial polypeptides (e.g., a defensin such as BNP-1). The trophic factor combinations described below can also comprise one or more trophic factors above. Accordingly, in some preferred embodiments, the trophic factor combination is supplemented with one or more of the following trophic factors: trehalose (Sigma, St. Louis Mo.; e.g., about 15 mM), substance P (Sigma; e.g., about 10 μg/ml), IGF-1 (Collaborative Biologicals; e.g., about 10 ng/ml), EGF (Sigma; e.g., about 10 ng/ml), and BDNF (2 μg/ml). In some preferred embodiments, the trophic factor combination is also supplemented with insulin (1-200 units, preferably 40 units) prior to use. In some embodiments, an antimicrobial polypeptide is not included in the trophic factor combination.

In some exemplary embodiments, EGF and/or IGF-1 are included in the trophic factor combination at a concentration of about 1 ng/ml to about 100 ng/ml, most preferably about 10 ng/ml. In other exemplary embodiments, substance P is included at a concentration of about 0.1 μg/ml to about 100 μg/ml, most preferably about 2.5 μg/ml.

It will be recognized that the Tables below provide formulations that are exemplary and non-limiting. For example, alterations in the specific substances used and the number of those substances are all within the scope of the invention. In some embodiments, the antimicrobial polypeptide and/or substance having an antimicrobial peptide effect and/or one or more trophic factor, are provided in stable form that can be reconstituted. Methods for stabilization include, for example, lyophilization. In embodiments where the antimicrobial polypeptide and/or one or more growth factors are provided in lyophilized form, they can conveniently reconstituted prior to use, for example, in sterile water or in an aliquot of a base medium (e.g., UW solution), prior to addition to a base medium (e.g., hyaluronic acid, UW solution).

Alternatively, the at least one microbial polypeptide and/or one or more trophic factor can be provided as a separate composition (i.e., a “bullet”) that is added to a base medium. In preferred embodiments, the bullet contains an antimicrobial peptide and/or a substance having an antimicrobial peptide effect and/or one or more trophic factor as described above. In some embodiments, the bullet contains an antimicrobial peptide and/or a substance having an antimicrobial peptide effect and/or one or more of the trophic factor as described above in concentrations that provide the appropriate concentration when added to a specific volume of the base medium, where used.

TABLE 3a
Component Type        Substance
Antimicrobial peptide BNP-1

TABLE 3b
Component Type        Substance
Antimicrobial peptide BNP-1
Growth factor         IGF-1

TABLE 3c
Component Type        Substance
Antimicrobial peptide BNP-1
Neuropeptide          Substance P

TABLE 3d
Component Type        Substance
Antimicrobial peptide BNP-1
Neurotrophin          BDNF

TABLE 3e
Component Type        Substance
Antimicrobial peptide BNP-1
Growth factor         IGF-1
Neuropeptide          Substance P

TABLE 3f
Component Type        Substance
Antimicrobial peptide BNP-1
Growth factor         IGF-1
Neurotrophin          BDNF

TABLE 3g
Component Type        Substance
Antimicrobial peptide BNP-1
Neuropeptide          Substance P
Neurotrophin          BDNF

TABLE 3h
Component Type        Substance
Antimicrobial peptide BNP-1
Growth factor         IGF-1
Neuropeptide          Substance P
Neurotrophin          BDNF

It is contemplated that the trophic factor combination can be provided in a pre-formulated form, such as in a kit format. The kit can include (1) at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect and (2) a neurotrophin. The kit can also include a viscous substance. At least one of a growth factor and a neuropeptide can also be included.

II. Uses of Trophic Factor Combinations and Their Individual Components

It is contemplated that the trophic factor combinations and their individual components described above may be utilized in a variety of procedures related to injury to the nervous system and other medical procedures. It is contemplated that the trophic factor combinations and their individual components can be used for the treatment of any part of the nervous system, including the central nervous system and the peripheral nervous system.

In one embodiment, the trophic factor combinations or one or more of their individual components are used during surgery of the disc and/or other portions of the nervous system. In an embodiment, a trophic factor combination or one or more of their individual components applied to surgical hardware and/or other implants, such as surgical screws, plates, pins, clamps, wires, pins, rods, nails, probes, spinal fixation devices, and the like. In another embodiment, a trophic factor combination or one or more of their individual components is applied directly during surgery, such as to a surgical opening, for example, an incision, a section, or any other opening. In one embodiment, a trophic factor combination or one or more of their individual components is applied to one or more tissue, nerve, organ, or cavity. A trophic factor combination or one or more of their individual components can also be applied to a surgical instrument such that when the instrument is used, the trophic factor combination or one or more of their individual components is delivered to injury and/or surrounding tissue, fluid, organ, and the like.

In use, an injury to the nervous system is identified. At least one component of the trophic factor combination is applied to the injury to the nervous system.

In some embodiments, the trophic factor combinations can be utilized to reduce body weight loss post injury in injured animals treated with the combination when compared to injured animals not treated with the trophic factor combination. Preferably, the decrease in loss of body weight is improved by at least 25% and more preferably by at least 50% as compared to animals not receiving the trophic factor combination. In some embodiments, the trophic factor combinations are used to strengthen motor recovery in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. In some embodiments, the trophic factor combinations are used to increase evoked potential amplitudes in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. In some embodiments, the trophic factor combinations are used to lower the current required to evoke a response (threshold current) in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. Application of the trophic factor combination according to the invention can also have at least one of the following additional effects: reduced pain in the animal, a neuroprotective effect, triggered neuronal plasticity, reduced inflammation, and growth of new cells.

EXAMPLES

The following examples serve to illustrate certain preferred embodiments and aspects of the present invention and are not to be construed as limiting the scope thereof.

Example 1

Materials and Methods

Experiments were performed on 3-5 month old male Sprague-Dawley (SD) and Lewis rats that were housed individually with free access to food and water. Rats were placed into four groups: 1) spinally injured SD rats without a trophic factor combination administered (n=8), 2) spinally injured SD rats with a trophic factor combination (n=2); 3) spinally injured Lewis rats without a trophic factor combination administered (n=5), and 4) spinally injured Lewis rats with a trophic factor combination administered (n=2).

Spinal cord injury. Rats were anesthetized with medetomidine (75 μg/kg i.m.) and isoflurane in oxygen. After oro-tracheal intubation, anesthesia was maintained with isoflurane in oxygen and rats were mechanically ventilated. A laminectomy was made at the second cervical vertebral level to allow the second cervical spinal segment and the cranial segment of the third cervical spinal segment to be exposed. A 1-mm-long left-sided hemisection was made in the cranial segment of C₂ and the section aspirated with a fine tipped glass pipette. The surgical wound was closed using standard techniques. All animals were allowed to recover and received atipamezole (0.1 mg/kg i.v.) to antagonize the anesthetic effects of medetomidine. Buprenorphine (50 μg/kg i.v.) and carprofen (5 mg/kg i.v.) were administered for postsurgical pain control. Analgesics were repeated as required over the next 2 days.

Trophic Factor Combination. The trophic factor combination (also referred to as the trophic factor combination) was made by adding 10 ug of BNP-1 (bactenecin), 100 ng of insulin-like growth factor (IGF-1), and 25 mg of Substance P to 200 ul of distilled water.

Trophic factor combination administration. Prior to closure of the surgical wound, hyaluronic acid (Hylartin V, sodium hyalurate) (10%) was added to the neurotrophin mixture to thicken the solution and improve retention at the site of spinal injury. Two ug of BDNF was added to 0.4-0.45 ml of the mixture. The mixture (0.4-0.45 ml) was then administered using a syringe and 22-gauge needle into the hemisection cavity. The wound was closed immediately after injection.

Experimental preparation. Two weeks after surgical spinal injury, respiratory motor output was measured from both phrenic nerves using two distinct experimental techniques. First, spontaneous (brain-stem driven) phrenic motor activity was measured in anesthetized rats during standardized conditions. Second, spontaneous activity was removed by hyperventilating the rats and evoke potentials were elicited by spinal stimulation to evaluate the strength of the spinal pathways contributing to motor recovery.

Isoflurane anesthesia was induced in a closed chamber and maintained (2.5-3.5%) via nose cone while rats were tracheotomized. Rats were mechanically ventilated following tracheal cannulation. Following femoral venous catheterization rats were converted to urethane anesthesia (1.6 g/kg) then bilaterally vagotomized and paralyzed with pancuronium bromide (2.5 mg/kg, i.v.). Blood pressure was monitored via a femoral arterial catheter and pressure transducer (Gould P231D, Valley View, Ohio). End-tidal CO₂ was monitored with a rapidly responding analyzer (Novametrix, Wallingford, Conn.). Arterial partial pressures of O₂ (PaO₂) and CO₂ (PaCO₂) as well as pH were determined from 0.2 ml blood samples (ABL-500, Radiometer, Copenhagen, Denmark); unused blood was returned to the animal. Rectal temperature was maintained (37-39° C.) with a heated table. Phrenic nerves were isolated with a dorsal approach, cut distally, desheathed, bathed in mineral oil and placed on bipolar silver electrodes. Nerve activity was amplified (1000-10,000×) and filtered (100-10,000 Hz bandpass; model 1800, A-M Systems, Carlsborg, Wash.).

Spontaneous phrenic motor output. In all rats, the CO₂ apneic threshold for inspiratory activity in the phrenic nerve contralateral to hemisection was determined after waiting a minimum of one hour following conversion to urethane anesthesia. This delay allowed blood pressure and respiratory motor output to stabilize. The procedure to establish the apneic threshold began by increasing the ventilator frequency until inspiratory activity ceased. Ventilator rate was then decreased slowly until inspiratory activity re-appeared. The end-tidal CO₂ partial pressure (P_ETCO₂) corresponding to the onset of inspiratory bursting was defined as the CO₂ apneic threshold. P_ETCO₂ was maintained 3 mmHg above the apneic threshold by adjusting the ventilator pump rate and inspired CO₂ content. After the CO₂ apneic threshold and baseline PaCO₂ levels were established, 30-45 minutes were allowed to attain stable baseline conditions.

Evoked phrenic potentials. Rats were hyperventilated (PaCO₂<30 mmHg) to prevent spontaneous inspiratory efforts. A monopolar tungsten electrode (5 MΩ, A-M Systems) was inserted contralateral to the spinal hemisection and adjacent to the C2 dorsal roots. The electrode tip was placed in or in close proximity to the ventrolateral funiculus (1.8-2.3 mm below the dorsal root entry zone). Electrode position was selected by maximizing the amplitude of a short latency (<1.0 ms) evoked potential in the phrenic nerve contralateral to SCI. Stimulus-response relationships were obtained by applying current pulses (20-1000 μA, 0.2 ms duration) with a stimulator (model S88, Grass Instruments, Quincy, Mass.) and stimulus isolation unit (model PSIU6E, Grass Instruments). Phrenic potentials were digitized and analyzed with P-CLAMP software (Axon Instruments, Foster City, Calif.).

Results:

Body Weight. Body weight decreased by 2 weeks post-injury in rats that had received a spinal hemisection (FIG. 1). Decreased body mass may represent disuse atrophy of skeletal muscles or inadequate caloric intake. Reduced food consumption may occur secondary to spinal cord injury because of motor paresis, reduced locomotor coordination, and/or decreased appetite. Spinally injured rats that received the trophic factor combination had significantly less reduction in body weight compared to the control group (FIG. 1).

Spontaneous Phrenic Nerve Activity. Spontaneous recovery of phrenic motor function on the injured side was evident as inspiratory bursts that were in synchrony with phrenic motor activity on the uninjured side. Phrenic motor recovery was present in all spinally injured rats regardless of treatment. However, the magnitude of this recovery differed between groups (FIG. 2). Administration of the trophic factor combination at the time of injury strengthened motor recovery at 2 weeks post-injury as evident by the significantly larger peak inspiratory voltage during baseline recording conditions (FIG. 2). Phrenic peak inspiratory voltage is correlated to tidal volume. Although tidal volume was not measured in these rats, it is reasonable to assume that the increased peak inspiratory voltage would translate to larger tidal volumes in these animals compared to spinally injured rats that did not receive the trophic factor combination.

Evoked Phrenic Nerve Potentials. Evoked potentials were recorded from the phrenic nerve on the side of injury (FIG. 3). Consistent with the effects of treatment on spontaneous phrenic nerve activity data, administration of trophic factor combination at the time of injury significantly increased evoked potential amplitudes compared to rats that only received a spinal injury.

In addition, a strong trend existed for the current required to evoke a response (threshold current) to be lower after trophic factor combination administration compared to the control group (FIG. 4). Collectively, these data suggest that the trophic factor combination strengthens motor recovery via a spinal mechanism that strengthens existing synaptic pathways onto phrenic motoneurons.

Example 2

This study was performed to determine whether application of a trophic factor combination can improve motor function after spinal cord injury (SCI). In this study, the trophic factor combination of Example 1 was applied and included insulin-like growth factor (IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin (BNP-1), and substance P. The trophic factor combination was applied to test whether this combination would augment spontaneous respiratory motor recovery in a well-defined model of high cervical incomplete spinal cord injury (C2 hemisection). The trophic factor combination was applied to the injured spinal cord at the time of surgical injury. At 2 weeks post-injury, respiratory motor output was recorded bilaterally from phrenic nerves in urethane anesthetized, vagotomized, and mechanically ventilated spinally injured Lewis male rats (SCI-only: n=6; SCI+ trophic factor combination; n=6, with some of these rats being the same as the rats in Example 1). Body weight decreased in all rats after injury. However, the change in body weight was significantly less after trophic factor combination treatment (see FIG. 5; p<0.05). Spontaneous recovery of phrenic motor output on the side of injury was present in all rats and represents activation of a latent population of bulbospinal premotor synaptic pathways to ipsilateral phrenic motoneurons that cross the spinal midline caudal to injury. The trophic factor combination increased the amplitude of phrenic inspiratory bursts on the injured side when measured as rectified and moving-averaged voltages and indexed to the maximal amplitude during hypercapnia (see FIG. 5; p<0.05). In contrast, the trophic factor combination did not alter phrenic motor output on the side opposite injury. Thus, combined treatment with the trophic factor combination improves phrenic motor recovery after C2 hemisection by selectively augmenting crossed spinal synaptic pathways.

Example 3

Subtractive studies. Experiments can be performed on rats in accordance with the methods described in Example 2 except that fewer than all four components, i.e., insulin-like growth factor (IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin (BNP-1), and substance P, of the trophic factor combination can be used (except for one or more controls using all four components). Different components can also be used. For example, a different growth factor (and/or neurotrophin and/or neuropeptide and/or antimicrobial peptide) can be used than the one listed above. Studies can also be run using only one component, i.e., either IGF-1, BDNF, BNP-1, or substance P or any other trophic factor to determine the effects of the individual components. Studies can also be performed using combinations of two of the components and using combinations of three of the components to determine whether all four components are needed to achieve the desired results.

Example 4

Experiments can be performed on dogs having herniated discs. Traditionally, many dogs undergo surgical treatment of disc herniation, but no trophic factor combination has been administered during such surgery. Four naïve dogs can be first treated to test for unanticipated common severe negative effects of the trophic factor combination. Once this is done, 50 dogs presenting to the Veterinary Medical Teaching Hospital (VTMH) at the University of Wisconsin with severe spinal cord dysfunction can be tested.

Trophic factor combination. The trophic factor combination can be formulated of insulin like growth factor-1 (IGF-1) (10 ng/ml), substance P (2.5 μg/ml), bactenecin (1 μg/ml) and brain derived neurotrophic factor (BDNF) (2 μg/ml). The factors can be dissolved in a 1% hyaluronic acid solution. The hyaluronic acid is used in order to increase the contact time of the factors with the tissues.

Dogs that are clinical patients. Surgery can be performed under general anesthesia. A hemilaminectomy can be done at the site of the disc herniation. A 22-gauge catheter can be placed through the dura mater and arachnoid membrane and inserted in the subarachnoid space just caudal to the disc herniation. One ml of the trophic factor combination can be injected in the subarachnoid space. The surgery site can be closed routinely.

After recovery from anesthesia, intravenous lactated Ringer's solution and analgesics can be continued until the dog is able to drink on its own and does not appear painful. Neurologic examinations can be done twice a day. The dogs can be discharged to the owner when they are considered not to need pain medication, can urinate on their own, and are eating and drinking. Follow up examinations can be scheduled as appropriate clinically.

Pain or discomfort during surgery can be alleviated by maintenance of a surgical plane of anesthesia and constant rate infusion (CRI) of fentanyl 10 μg/kg/hr. The fentanyl CRI can be continued up to 12 hours post operatively at a dose of 2-5 μg/kg/hr. A Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of 72 hours) can be administered as a routine postoperative treatment. Butorphanol can be further administered if the dogs demonstrate discomfort and can be given as long as clinical signs of pain, as indicated by abnormal posturing, vocalization, or discomfort upon palpation of the surgical wound site are present.

Immediately after surgery, the dogs can be monitored continuously until the animals are able to drink water on their own sufficient to maintain their hydration. After this recovery period, the animals can be checked a minimum of 3 times daily to determine if they are experiencing pain or discomfort. The dogs can be evaluated by physical exam, neurological exam, and direct palpation of the surgical wound. The dogs can receive routine recumbent care.

Dogs can be monitored post-surgically for cardiovascular stability by physical exam, pulse character, capillary refill time, heart rate, respiratory rate, and packed cell volume, if needed. Fluids can be administered if needed to maintain hydration. Postoperative discomfort can be alleviated by administration of fentanyl CRI (10 μg/kg/hr) during surgery and fentanyl CRI (2-5 μg/kg/hr) after surgery or butorphanol (0.2-0.4 mg/kg/IV or SQ) every 4-6 hours thereafter and a Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of 72 hours).

Example 5

Safety trial of trophic factor combination on dogs. The toxicity of the trophic factor combination described in Example 4 was tested on dogs. Four beagle dogs were studied over a three-day period. While the dogs were anesthetized, the trophic factor combination described in Example 4 in hyaluronic acid was injected into 1) the lumbar cerebrospinal fluid (2 dogs) and 2) the cisterna magna cerebrospinal fluid (2 dogs). In all four cases, the dogs recovered easily and showed no signs of toxic reactions. There was no evidence for chronic pain on neurological exam. All dogs were euthanized on the third day of the study. In summary, no adverse reactions were observed in any animal.

It is understood that the various preferred embodiments are shown and described above to illustrate different possible features of the invention and the varying ways in which these features may be combined. Apart from combining the different features of the above embodiments in varying ways, other modifications are also considered to be within the scope of the invention.

The invention is not intended to be limited to the preferred embodiments described above, but rather is intended to be limited only by the claims set out below. Thus, the invention encompasses all alternate embodiments that fall literally or equivalently within the scope of these claims.

Claims

1. A composition comprising: A. an effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect; and B. an effective amount of a neurotrophin.

2. The composition of claim 1, further comprising an effective amount of at least one of a growth factor and a neuropeptide.

3. The composition of claim 1, further comprising an effective amount of a growth factor.

4. The composition of claim 3, wherein the antimicrobial peptide is BNP-1, the neurotrophin is BDNF, and the growth factor is IGF-1.

5. The composition of claim 1, further comprising an effective amount of a neuropeptide.

6. The composition of claim 5, wherein the antimicrobial peptide is BNP-1, the neurotrophin is BDNF, and the neuropeptide is Substance P.

7. The composition of claim 1, further comprising an effective amount of a growth factor and an effective amount of a neuropeptide.

8. The composition of claim 7, wherein the antimicrobial peptide is BNP-1, the neurotrophin is BDNF, the growth factor is IGF-1, and the neuropeptide is Substance P.

9. The composition of claim 1, wherein the antimicrobial peptide is BNP-1 and the neurotrophin is BDNF.

10. The composition of claim 9, further comprising an effective amount of IGF-1 and an effective amount of Substance P.

11. The composition of claim 1, further comprising a viscous substance.

12. The composition of claim 1, further comprising a matrix.

13. The composition of claim 10, wherein the matrix comprises a hydrogel.

14. A method of treating an injury to a nervous system of an animal, the method comprising: A. identifying the injury to the nervous system; and B. applying to the injury an effective amount of at least one of antimicrobial peptide and a substance having an antimicrobial peptide effect.

15. The method of claim 14, wherein the at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect is combined with an effective amount of one or more trophic factors selected from the group consisting of a growth factor, a neurotrophin, and a neuropeptide.

16. The method of claim 14, wherein the injury to the nervous system comprises a spinal cord injury.

17. The method of claim 14, wherein the applying step produces an effect on the animal, the effect selected from the group consisting of reduced pain, neuronal plasticity, a neuroprotective effect, reduced body weight loss, increased motor recovery, increased evoked potential amplitudes, and lowered threshold current.

18. A kit comprising: A. at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect; and B. a neurotrophin.

19. The kit of claim 18, further comprising a viscous substance.

20. The kit of claim 18, further comprising at least one of a growth factor and a neuropeptide.