Method of using lectins for therapy of diseases transmittable by sexual contact

Abstract

In order to prevent conception and/or the spread of sexually transmitted diseases (STD's) one or more lectins capable of binding sperm and/or the pathogenic microorganisms responsible for STD's are administered to the vagina prior to sexual intercourse. The lectins immobilize the sperm to render them incapable of fertilization and also bind to the microorganisms to render them non-pathogenic or to the cells to prevent infection by the microorganisms. Lectins can also be administered to treat sexually transmitted vaginal infections. The invention also encompasses a device for to be placed in the vault of the vagina which comprises a ring which surrounds the cervix and a membrane spanning the central aperture of the ring to prevent the direct contact of ejaculate with the cervical tissues. The device is impregnated or coated with lectins and releases them into the vaginal environment over a period of time.

Description

BACKGROUND OF THE INVENTION

[0002] 1. Field of the Invention

[0003] This invention relates generally to methods of contraception and prophylaxis against diseases transmittable by sexual contact and therapy of such diseases, and more particularly to a method using intravaginally administered lectins for contraception and to protect against the transmission of diseases that are transmissible by sexual contact and to treat such diseases. The invention also relates to devices for intravaginal administration of lectins.

[0004] 2. Brief Summary of the Prior Art

[0005] Sexually transmitted diseases (STD's) are epidemic in this country and worldwide. Furthermore, other diseases that have not traditionally been considered to be STD's have also been found to be transmitted by sexual contact, e.g., hepatitis B. The medical and public health problems associated with these epidemics have motivated a search for methods of controlling these diseases by limiting their transmission from person to person. Similarly, although many methods of contraception have been employed, no universally satisfactory method has been developed.

[0006] Hitherto it has been generally agreed that barrier methods which prevent the contact of body fluids between individuals are the most effective means of preventing transmission of such diseases. Such barrier methods are also effective contraceptive procedures. However, such methods are somewhat inconvenient and require some cooperation between individuals.

[0007] An alternative method for preventing the transmission of sexually transmitted diseases is to kill the pathogenic microorganisms in semen and vaginal secretions so that they are incapable of invading the tissues and causing the disease. While intravaginally placed spermatocides have been used for contraception, alone or in combination with barrier methods, antimicrobial materials have not been so used to prevent STD's, probably because many of such materials are irritating to adjacent tissues.

[0008] Administration of biologically active materials to the vagina for whatever purpose is usually accomplished by the use of some device that provides for convenient application of the medication by the user herself. A variety of devices exist for delivery of bioactive substances such as spermatocides and various medications. Each has its place in the medical armamentarium but each has certain deficiencies for application of contraceptive or anti-microbial agents in the context of sexual activity. Conventional vaginal suppositories and ovules may not provide medication to the entire vagina because of their shape and placement by the user in the vagina. Such suppositories are generally comprised of a material that melts at body temperature to allow the medication to spread and contact the tissues. However, when the dosage form melts, the medication may drain out of the vagina rather quickly, thus minimizing its potential effectiveness and significantly reducing the extended exposure of the tissues and pathogens to the medication which is often necessary for effective treatment. Similarly, the effective duration of contraceptives applied in this way tends to be relatively brief. In addition, such delivery vehicles, even when freshly applied, do not provide any physical barrier to deposition of male ejaculate on the cervix. Such ready access of sperm to the cervix may allow them to escape the action of spermatocides that are diffused throughout the vagina. Furthermore, because cells at the cervix are uniquely sensitive to several pathogens such as Chlamydia trachomatis, the absence of a barrier deprives these cells of a significant means of protection.

[0009] In order to provide for a longer retention of medication in the vagina and assure a more continuous delivery of active ingredients to the tissue, several types of vaginal rings have been proposed. Such devices are disclosed, for example, in Duncan, U.S. Pat. No. 3,545,439; Roseman, U.S. Pat. No. 3,920,805; Schopflin, U.S. Pat. Nos. 4,012,496 and 4,012,497; Wong et al., U.S. Pat. Nos. 4,237,885 and 4,286,587; and Nash et al., U.S. Pat. No. 4,292,965. The vaginal rings are generally impregnated with a spermatocide and are designed to be retained in the vaginal vault and to release the spermatocide slowly over a period of time to maintain an effective contraceptive concentration of the active material in the vagina. However, such devices do not prevent the direct contact of ejaculate with the tissues of the cervix, and therefore do not protect those tissues from contact with pathogenic organisms which might be contained in the ejaculate. They are also of questionable efficacy in supplying the spermatocide where it is most needed.

[0010] Another approach is to use a cervical cap or a diaphragm to serve as a mechanical barrier to the sperm and to dispense medication. These devices are designed for a relatively tight fit either to the cervix or the walls of the vagina to serve as a mechanical barrier to the passage of sperm. Such devices can be effective, especially as contraceptives and when combined with spermatocides. However, because of the need to provide a sperm-resistant seal they are frequently relatively complex devices incorporating metallic springs within a rubber or synthetic resin structure to provide the required sealing force.

[0011] Another approach to providing an effective concentration of spermatocide in the vagina is to provide a sponge impregnated with a spermatocide. Such applicators are not intended to be precisely located and may permit the contact of ejaculate with the tissues of the cervix, with the undesirable consequences outlined above.

[0012] Accordingly, a need has continued to exist for a method of contraception and prophylaxis against STD's by vaginal administration of a spermatocide and/or antimicrobial material, and for a simple and effective device to protect the tissues at risk from contact with microorganisms while dispensing a spermatocidal and/or antimicrobial material.

SUMMARY OF THE INVENTION

[0013] This need has now been alleviated by the method and device of this invention, according to which one or more lectins capable of binding sperm and/or the pathogenic microorganisms responsible for STD's are administered to the vagina or site of infection prior to sexual intercourse. The lectins immobilize sperm to render them incapable of fertilization and also bind to the microorganisms to render them non-pathogenic or to the cells to prevent infection by the microorganisms.

[0014] The invention also encompasses a device for to be placed in the vault of the vagina which comprises a ring which surrounds the cervix and a membrane spanning the central aperture of the ring to prevent the direct contact of ejaculate with the cervical tissues. The device is impregnated or coated with lectins and releases them into the vaginal environment over a period of time.

[0015] Accordingly, it is an object of the invention to provide an improved method for prophylaxis against sexually transmitted diseases.

[0016] A further object is to provide a method of contraception.

[0017] A further object is to provide a method for binding and immobilizing pathogenic microorganisms in the vagina.

[0018] A further object is to provide a method for treating vaginal infections.

[0019] A further object is to provide a device for delivering lectins to the vagina over a period of time.

[0020] A further object is to provide an intravaginal device that protects the tissues of the cervix from direct contact with ejaculate.

[0021] Other objects of the invention will become apparent from the following detailed description when considered in conjunction with the drawings.

BRIEF DESCRIPTION OF THE DRAWINGS

[0022] FIG. 1 is a top plan view of a lectin-delivery device according to the invention.

[0023] FIG. 2 is a bottom view of the lectin-delivering device of FIG. 1.

[0024] FIG. 3 is a cross section of the lectin-delivering device of FIGS. 1 and 2, taken along the line 3-3.

[0025] FIG. 4 is a top plan view of another embodiment of the lectin-delivering device of this invention.

[0026] FIG. 5 is a bottom view of the lectin-delivering device of FIG. 4.

[0027] FIG. 6 is a cross section of the lectin-delivering device of FIGS. 4 and 5, taken along the line 6-6.

DETAILED DESCRIPTION OF THE INVENTION AND PREFERRED EMBODIMENTS

[0028] Lectins are carbohydrate-binding proteins of nonimmune origin that agglutinate cells or precipitate polysaccharides or glycoconjugates, i.e., proteins or lipids conjugated to oligo- or polysaccharides. They are widely distributed, and have been isolated from both plant and animal sources. Their reactions with living cells are based on their ability to bind with antibody-like specificity to particular arrangements of the sugar residues that make up oligo- or polysaccharides.

[0029] The surfaces of eucaryotic cells contain very numerous molecules of glycoproteins and glycolipids. Similarly, the cell walls and outer membranes of bacteria and the envelopes of viruses contain structural polysaccharides and/or glycoproteins. The carbohydrate moieties of these molecules which are displayed on the cell surfaces exhibit great variety in composition and structure that serves to distinguish the types of cells and to serve as a signal to other cells or materials which come into contact with the cell. For, example, variation in the carbohydrate moieties of glycoproteins and glycolipids in the membrane of red blood cells serves as the basis for the conventional blood typing classification. When lectins recognize and bind to certain carbohydrate moieties they may serve to cross-link and agglutinate the cells bearing the binding groups, a property that earns for them the alternate name of agglutinins. Furthermore, because the same sort of carbohydrate moieties often serve as attachment points for pathogens to bind to target cells and invade them, lectins may block infection of target cells by blocking the sites used by pathogens as recognition markers. The same type of specific binding occurs between sperm and egg in conception, and can be blocked by lectins. The binding ability of lectins may be very specific for certain mono- or oligosaccharides, allowing lectins to be used as a powerful tool for investigating the oligosaccharide epitopes on the surface of organisms or cells. Lectins can distinguish between blood cells of specific blood type, malignant from normal cells, and among species and genus of organisms. While glycoproteins, glycolipids, and bacterial cell walls are believed to be the main lectin-binding locations on the surface of cells, it is not excluded that carbohydrate moieties derived from other molecules or cellular structures may be displayed on the cell surface or that other lectin-binding structures may be present on cell surfaces. All such lectin-binding structures may be targets for the lectins used in the method of this invention.

[0030] Current medical uses of lectins include distinguishing erythrocytes of different blood types (blood typing). More recently, lectins have been used ex-vivo in depleting T cells of patients undergoing bone marrow transplantation.

[0031] In the context of this application the term microorganism includes any microscopic organism within the categories of algae, bacteria, fungi, parasites (helminths, protozoa), viruses, and subviral agents.

[0032] Among the microorganisms that are bound by certain lectins are infectious organisms such as bacteria, protozoa, and viruses. Lectins may be used to identify such microorganisms in vitro and are also capable of binding to them in vivo, thereby preventing them from infecting living cells. Human disease-causing organisms (and the diseases caused by them) that can be bound by lectins include Neisseria gonorrhoeae (gonorrhea); Chlamydia trachomatis (chlamydia, lymphogranuloma venereum); Treponema pallidum (syphilis); Haemophilus ducreyi (chancroid); Calymmatobacterium granulomatis (donovanosis); Mycoplasma pneumoniae, M. hominis, M. genitalium, Ureaplasma urealyticum (mycoplasmas); Shigella flexneri (shigella); Salmonella typhi, S. choleraesuis, S. enteritidis (salmonella); Campylobacter fetus, C. jejuni (campylobacter); human immunodeficiency virus HIV-1 and HIV-2 (HIV, AIDs); HTLV-1 (T-lymphotrophic virus type 1); herpes simplex virus type 1 and type 2 (HSV-1 and HSV-2); Epstein-Barr virus; cytomegalovirus; human herpesvirus 6; varicella-zoster virus; human papillomaviruses (many types) (genital warts); molluscum contagiosum (MSV); hepatitis A virus, hepatitis B virus (viral hepatitis); Trichomoniasis vaginalis (trichomoniasis); yeasts such as Candida albicans (vulvovaginal candidiasis), Phthiris pubis (crab louse), and Sarcoptes scabiei (scabies). Other diseases that are transmitted by contact with bodily fluids may also be transmissible by sexual contact and are capable of being prevented by administration of lectins according to this invention. Accordingly, the term sexually transmitted diseases (STD's) is to be interpreted in this application as including any disease that is capable of being transmitted in the course of sexual contact, whether or not the genital organs are the site of the resulting pathology.

[0033] Inasmuch as lectins are also capable of agglutinating human sperm and other components of the male ejaculate, and thereby rendering the sperm immobile, intravaginal administration of lectins can also serve as a method of contraception.

[0034] According to the invention a dose of lectins adapted to bind and agglutinate pathogenic microorganisms and/or block the recognition sites on target cells is administered to the vagina prior to sexual intercourse. For therapy of sexually transmitted diseases, the dose of lectins may also be administered at other times in a regimen of treatment. The active ingredients may also include lectins capable of binding and/or inactivating sperm or the male ejaculate to serve as a contraceptive.

[0035] Because of the specificity of lectins for certain microorganisms, it is preferred to administer a mixture of lectins chosen for their properties of agglutinating specific pathogens. It is also according to the invention to administer a mixture of sperm-agglutinating lectins and lectins capable of binding to pathogenic organisms to provide simultaneous contraception and protection against infection.

[0036] A representative listing of lectins, the abbreviations by which they are referred to, and their sources is given in Table 1.

TABLE 1
Lectins and Abbreviations
Lectin         Source
AAnA           Anguilla anguilla (eel serum)
AAurA          Aleuria aurantia (orange peel fungus)
ABA            Agaricus bisporus (mushroom)
ABrA           Amphicarpanea bracteata (hog-peanut)
AEP            Aedopodium podagraria (ground elder)
AL             Hippaestrum hybrid (amaryllis bulbs)
APA            Abrus precatorius (jequirity bean)
AS             Avena sativa (oat)
BDA            Bryonia dioica (white bryony)
BPA            Bauhinia purpurea alba (camel's foot
               tree)
CA             Cymbidium species
CA             Colchicum autumnale (meadow saffron)
CAA            Caragana arborescens (Siberian pea tree)
CCA            Cancer antennarius (California crab)
ConA           Concanavalia ensiformis (jack bean)
CPA            Cicer arietinum (chick pea)
CSA            Cytisus scoparius (Scotch broom)
DBA            Dolichos biflorus (horse gram)
DSA            Datura stramonium (jimson weed, thorn
               apple)
ECA            Erythrina crystagalli (coral tree)
ECorA          Erythrina coralldendron (coral tree)
EEA            Euonymus europaeus (spindle tree)
EHA            Eppactus hellebrine
EHA            Eranthis hyamalis
GNA            Galanthus nivalis (snowdrop bulb)
GSA-I/GSA-II   Griffonia simplicifolia
HAA            Helix aspersa (garden snail)
HHA            Hippeastrum hybrid
HPA            Helix pomatia (Roman or edible snail)
JAC (Jacalin)  Artocarpus integrifolia (jackfruit)
LAA            Laburnum alpinum
LBA            Phaseolus lunatis (also limensis) (lima
               bean)
LCA (LcH)      Lens culinaris (lentil)
LEA            Lycopersicon esculentum (tomato)
LFA            Limax flavus (garden slug)
LOA            Lathyrus oderatus (sweet pea)
LDA            Listeria ovata
LTA (LOTUS)    Lotus tetragonolobus (asparagus pea)
MAA            Maackla amurensis (maackla)
MIH            Mangifera indica (mango)
MPA            Maclura pomifera (osage orange)
NPL (NPA)      Narcissus pseudonarcissus (daffodil)
ORS            Oryza sativa (rice)
PAA            Persea americana (avocado)
PHA (PHA-L)    Phaseolis vulgaris (red kidney bean)
PNA            Arachis hypogaea (peanut)
PSA            Pisum sativum (pea)
PWA            Phytolacca americana (pokeweed)
PTAgalactose   Psophocarpus tetagonolobus (winged bean)
PTAgalNac      Psophocarpus tetagonolobus (winged bean)
RCA-I/RCA-II   Ricinus communis (castor bean)
RPA            Robinia pseudoaccacia (black locust)
SBA            Glycine max (soybean)
SJA            Sophora japonica (Japanese pagoda tree)
SNA            Sambuccus nigra (elderberry)
STA            Solanium tuberosum (potato)
TKA            Trichosanthes kinlowii (China gourd)
TL             Tulipa sp. (tulip)
TMT            Tomentine (seaweed Codium tomentosum)
UDA            Urtica dioica
UEA-I/UEA-II   Ulex europaeus (gorse or furz seeds)
URD            Urtica dioica (stinging nettle)
VAA            Viscum album (European mistletoe)
VFA            Vicia faba (fava bean)
VGA            Vicia graminea
VRA            Vigna radiata (mung bean)
VSA            Vicia sativa
VVA            Vicia villosa (hairy vetch)
WFA            Wisteria floribunda (Japanese wisteria)
WGA            Triticum vulgaris (wheat germ)
suc-WGA (sWGA) Succinyl WGA

[0037] For example, N. gonorrhoeae is agglutinated by lectins that bind to N-acetyl-D-glucosamine residues on their surfaces. Such lectins include WGA and STA, which are known to agglutinate all 193 clinical isolates of N. gonorrhoeae. WGA is effective for such agglutination at a concentration of 3.1 micrograms per milliliter. Other lectins showing some agglutination activity with respect to N. gonorrhoeae include RCA-I, RCA-II, GSA-I, and SBA.

[0038] Certain species of Chlamydia (trachomatis, psittaci, and pneumoniae) are known to be bound by the lectins ConA, DBA, UEA-1, SBA, and PNA. WGA also binds to the receptors on certain cells, thereby blocking infection by C. trachomatis and C. psittaci.

[0039] PHA binds to several isolates of H. ducreyi, suggesting that N-acetyl-D-glucosamine is present in the cell envelope polysaccharide. WGA has been found to agglutinate a variety of bacterial cells, including Escherichia coli, Micrococcus luteus, and some types of Staphylococcus aureus. WGA, specific for N-acetyl-D-glucosamine and SBA, specific for N-acetyl-D-galactosamine, are capable of agglutinating the many bacterial species which contain these sugar residues in their cell wall polysaccharides.

[0040] Various lectins are capable of binding to certain glycoproteins present in the envelope of HIV virus. For example, ConA has been found to block infection of certain cell lines against infection by HIV in vitro, and conglutinin, a lectin derived from bovine serum, has been found to bind to the HIV envelope precursor protein gp 160, thereby preventing attachment to CD-4 receptors of target cells in vitro. GNA has been found to prevent infection of T-cells by HIV in vitro. Consequently, ConA, GNA and WGA have been found to be effective at preventing infection of target cells by HIV-1 and HIV-2 in vitro. NPL and conglutinin have shown some activity as well.

[0041] HPA, ConA, BPA, and EHL have demonstrated efficacy in the prevention of infection of target cells by HSV-1 and HSV-2.

[0042] Lectins are also useful in aggregation of sperm. PHA, WGA, sWGA STA, ConA, PSA, APA, ECA, ECorA have demonstrated varying degrees of efficacy in agglutination of sperm. While the lectins discussed above and the microorganisms and/or sperm against which they are effective are representative of useful lectins according to the invention, it is to be understood that other lectins may be discovered which are active in the binding and agglutination of sperm and of the pathogens of sexually transmitted diseases, and that the use of such lectins is intended to be included within the scope of the invention.

[0043] In determining the amount of lectin to be administered for effective binding and/or agglutination of the pathogenic microorganisms of STD's, the amount of lectin that might be bound to vaginal tissues and thereby made unavailable for agglutination of pathogens must be considered. In studies on murine vaginal tissue, DBA, LAA, LBA, LCA, LTA, RCA-I, RCA-II, SJA, STA, VGA, and WFA have been found not to bind to the tissue at any stage of the estrus cycle. In contrast, ABA, MPA, PHA-E, PHA-L, Suc-ConA, and WGA bound strongly to vaginal tissues at all stages of the estrus cycle. CSA, GSA-I, GSA-II, HAA, HPA, JAC, PNA, PAA, SBA, Suc-WGA, UEA-I, VFA, and VVA exhibited intermediate degrees of binding to murine vaginal tissues. The amount of lectin to be administered for effective prophylaxis can be determined from the relative binding effect of the various lectins to the pathogen and to the vaginal tissues. The selection of particular lectins to be administered will depend on the diseases sought to be prevented or treated. It is preferred to administer a mixture of lectins, each selected for best agglutinative efficacy against a particular pathogen.

[0044] The lectins may be administered in any fluid or ointment vehicle suitable for topical administration of pharmaceutical compounds. Thus creams, ointments, foams, suppositories, liposomes, ovules and the like may be formulated in which the selected lectins are dispersed in a non-toxic vehicle suitable for topical and in particular for vaginal administration. Such vehicles include oil-in-water and water-in-oil emulsions, white petrolatum, hydrophilic petrolatum, lanolin emulsions, polyethylene glycols, cocoa butter and the like. Useful vehicles include emollient oils such as water-soluble oils, e.g., liquid polyethylene glycols, which promote complete and uniform distribution of the medicament within the vagina. Representative suitable vehicles include a lubricating jelly comprised of water, propylene glycol, hydroxyethyl cellulose, benzoic acid and sodium hydroxide, a water-soluble oil comprised of water, glycerin, propylene glycol, polyquaternium #5, methyl paraben and propyl paraben; a cream comprised of benzyl alcohol, cetearyl alcohol, cetyl esters wax, octyldodecanol, polysorbate 60, purified water, and sorbitan monostearate; and a suppository comprised of polyethylene glycol (PEG) 18, PEG-32, PEG-20 stearate, benzethonium chloride, methyl paraben and lactic acid. The lectins can also be incorporated into any conventional controlled release system for releasing them gradually or in a controlled timed release profile to the site of intended activity_Such systems are well-known to those skilled in the art and include particles having coatings that dissolve or erode at different controlled rates in a body fluid, matrices, e.g., polymers from which the lectins can diffuse, erodible matrices that release lectins to the site of intended activity, or the like.

[0045] Thus, the invention encompasses a composition having one or more lectins dispersed in a pharmaceutically acceptable non-toxic vehicle. Such a composition may be in the form of a cream, lotion, ointment, salve, foam, meltable solid, or the like.

[0046] According to the invention, the dispersion, suspension, emulsion or solution of lectins in the vehicle may be applied to the site of a lesion on the external genitalia, such as the lesions produced by herpes simplex virus type 1 or type 2, chancroid, genital warts, chancre of syphilis, and the like, to prevent the transfer of pathogens. The lectins may also be introduced into the vagina in order to prevent conception or infection by pathogens introduced during sexual intercourse. The amount of lectins to be applied will be an amount that is effective to prevent conception or infection or substantially reduce the risk thereof. The amounts needed to achieve these goals will depend on the effectiveness of the individual lectins, their affinity for the target cell and the like. The effective amounts can be determined by the skilled practitioner by routine experimentation. The lectins can be delivered to the desired site of activity either as a bolus or in the form of a controlled release composition, as is well-known in the art. Because of their ability to bind pathogenic microorganisms, thereby interfering with their mobility, attachment/adhesion, growth and reproduction, lectins are also useful in therapy of topical infections of the vagina. For those diseases wherein the pathogens grow and reproduce within the lumen of the vagina, administration of lectins, alone or in combination with other antimicrobial materials, can assist in the treatment and cure of the infections.

[0047] Because some of the conventional means of administering medications to the vagina have certain drawbacks, as discussed above, it is preferred to incorporate the lectins into a device which will remain in the vagina and dispense the lectins over a prolonged period of time in order to maintain an effective concentration of the lectins in the vagina. Such a device may also be designed to provide a barrier that will prevent the access of pathogenic organisms into the uterus and may also function as a contraceptive device.

[0048] Thus the lectins to be introduced into the vagina can be incorporated in any conventional vaginal medication-dispensing device such as suppositories, ovules, pessaries and the like, including controlled-release systems as discussed above. The lectins may also be incorporated into conventional contraceptive devices such as diaphragms, cervical caps, vaginal sponges or the like. The lectins may be incorporated into the body of such devices or coated on the surface thereof, either neat or in a vehicle, e.g., as a dusting powder, or in a binder that provides a coating from which the lectins are released over a period of time. It is not excluded that the lectins may be bound covalently to the surface of the device.

[0049] The device of the invention is generally a ring of elliptical or circular cross-section made, e.g., from a biocompatible, nontoxic thermoplastic polymer or polymeric open-cell polyurethane. Bonded to one side of the ring or molded integral with it is a web of the same material.

[0050] A device according to the invention having a ring of elliptical cross-section is illustrated in FIGS. 1-3, wherein the reference numerals indicate the same elements in each figure. A ring 102 of generally elliptical cross section constitutes the main structural member of the device and is sized to fit comfortably in the vaginal vault surrounding the cervix. To one side of the ring 102 is fastened a relatively thin web 104, preferably made of the same material as the ring. In some embodiments the web may be molded integrally with the ring.

[0051] FIGS. 4-6 illustrate another embodiment of the invention wherein a ring 202, of generally circular cross section, carries a thin web 204 spanning the central aperture on one side of the ring.

[0052] The device may be manufactured from any material that has been shown to be biocompatible with the environment of the vagina and to be capable of holding lectins within its bulk and releasing them slowly to the surrounding environment. Several materials suitable for this function are already known from the vaginal devices already in use or disclosed in the technical literature. Consequently, the skilled practitioner can easily select a suitable material from which to make the device of this invention. The lectins may also be incorporated into a thin flexible coating, placed on the ring or web or both, and designed to release the lectins therefrom over a period of time, e.g., by diffusion out of the coating or by gradual erosion and dissolution of the coating in the vaginal environment. The lectins may also be linked covalently to the surface of the device.

[0053] The device of the invention is designed to deliver one or more lectins locally in the vagina for:

[0054] 1) contraception, by binding to the glycoproteins, glycolipids and other glycoconjugates on the surface of sperm and by binding to the glycoproteins, glycolipids, and other glycoconjugates in the seminal fluid, thereby creating an ejaculate with significantly greater viscosity, and thereby preventing sperm from exiting the ejaculate;

[0055] 2) prophylaxis against various sexually transmitted diseases by binding to the glycoproteins, glycolipids, and other glycoconjugates on the surface of the bacterial agent or viral coat of the virus and the glycoproteins, glycolipids, and other glycoconjugates in the seminal fluid thereby preventing the infectious agent from reaching the target tissue;

[0056] 3) prophylaxis against various sexually transmitted diseases by binding to the glycoproteins, glycolipids and other glycoconjugate receptor sites on the vaginal stratified squamous epithelium and cervical columnar epithelium, whereby the recognition sites for attack by pathogens are blocked or concealed; and

[0057] 4) treatment of topical infections of the vagina by interfering with the growth and reproduction of the pathogenic microorganism, thereby hindering their ability to infect healthy cells.

[0058] The device of the invention also operates by providing a physical barrier to the direct deposition of ejaculate on the cervix. This design assures that the concentration of protective lectins in the cervical region will not be diluted and overwhelmed by the ejaculate. Rather, the sperm and the pathogens present in the ejaculate can only reach the cervical region gradually by diffusion and transport around the outside of the peripheral ring of the device. This slow transport of the sperm and pathogens from the ejaculate to the cervical region assures that the lectins will have an opportunity to bind to all appropriate constituents of the ejaculate. The presence of the lectins, which will coagulate and inhibit the transport of sperm and pathogens, makes it unnecessary to have a device that fits tightly either around the cervix or against the wall of the vagina.

[0059] Accordingly, the device of the invention has several advantages over the vaginal medication and contraceptive devices currently available:

[0060] 1) It is easily inserted and comfortable to use.

[0061] 2) Because of its position in the top of the vaginal canal, it ensures that the lectins are carried down through the vagina.

[0062] 3) Since it is placed next to the cervix it can also deliver lectins targeted to the cervix

[0063] 4) Gradual release of lectins provides a more consistent delivery over time, thus ensuring more efficient treatment.

EXAMPLE 1

[0064] This example illustrates the utility of various lectins in binding to certain microorganisms and to seminal plasma, sperm, human serum and cervical mucus.

[0065] The efficacy of binding of various lectins to human sperm and seminal plasma and cervical mucus, an indicator of the effectiveness of such materials as vaginally-applied contraceptives, was investigated in vitro by the following procedures. Similarly the efficacy of lectin binding to Neisseria gonorrhoeae, the pathogen responsible for gonorrhoea, was investigated by the following in vitro procedures. Such binding efficacy is an indication of the capability of such lectins to bind the pathogen and prevent infection when used intravaginally as a prophylactic material.

[0066] Growth of bacteria: A cervical isolate of Chlamydia trachomatis serovar G ATCC VR-878 was grown in 175 cm2 McCoy cell monolayers in the presence of 2 μg of cycloheximide per ml. The culture medium was 90% Eagle's minimum essential medium-10% fetal calf serum-20 mM HEPES (pH 7.3) supplemented with 50 μg of gentamycin sulfate per ml. Elementary bodies were purified by differential centrifugation followed by density gradient centrifugation in Percoll as described by Newhall et al. (Newhall, W. J., Baheiger, B. and Jones, R. B. 1982, Analysis of the human serological response to the proteins of Chlamydia trachomatis, Infection Immunity 38: 1181-1189). The purified elementary bodies were washed twice in 10 mM HEPES-145 mM NaCl (pH 7.4) and resuspended in bicarbonate buffer (100 mM NaHCO3 containing 0.01% NaN3, pH 9.5). The density of elementary bodies was adjusted to a McFarland No. 2 standard using the same buffer. Neisseria gonorrhoeae ATCC 19424 were grown on chocolate agar plates for 48-72 hrs at 37° C. in a CO2 incubator (5% CO2 and 80% humidity) and were harvested by scraping bacteria from the agar surface and resuspending the cells in sterile phosphate buffered saline. The cells were washed three times by centrifugation at 5000×g and resuspended in bicarbonate buffer, the density of which was adjusted to a McFarland No. 2 standard (optical density as measured by a spectrometer—0.4 at 650 nm). The cells were stored on ice prior to immediately testing in the lectin binding assay. Lactobacillus jensenii ATCC 25258 was grown 48-72 hrs at 37° C. in a shaking incubator in MRS broth at pH 5.5 containing 2% glucose. After incubation, cells were centrifuged at 5000×g for 10 min and washed twice in phosphate buffered saline, and the density was adjusted to a McFarland No. 2 standard with bicarbonate buffer. Haemophilus ducreyi was grown on chocolate agar plates for 72 hrs in a CO2 incubator (10% CO2 and 80% humidity) t 31° C. Bacteria were harvested by scraping bacteria from the agar surface and resuspending the cells in sterile phosphate buffered saline. The cells were washed three times by centrifugation at 5000×g, resuspended in bicarbonate buffer and the cell density adjusted to a McFarland No.2 standard. The cells were stored on ice prior to immediately testing in the pectin binding assay.

[0067] Lectin Binding Assay: Biotinylated lectins were reconstituted in phosphate buffered saline (10 mM sodium phosphate-150 mM NaCl, pH 7.2) and stored in a freezer at −70° C. until used. Microtiter plates washed with 95% ethanol and dried were coated with bacteria. (Chlamydia trachomatis or Neisseria gonorrhoeae or Haemophilus ducreyi or Lactobacillus Jensenii) by adding 200 μl of a bacterial suspension (in bicarbonate buffer) to each well and incubating overnight at room temperature. Wells coated with bacteria were washed three times in either sodium acetate buffered saline, pH 4.0, containing 0.1% Tween detergent (ABST) or phosphate buffered saline containing 0.1% Tween (PBST). Lectins defrosted at room temperature were diluted in each buffer, and 100 μl of various lectins was added to bacteria-coated wells at a final concentration of 50 μg/ml. After incubation in a humid chamber at room temperature for 2 hours, wells were washed three times with either ABST or PBST followed by the addition to each well of 100 μl of alkaline phosphatase streptavidin (10 μg/ml). After incubation for 1 hour at room temperature, wells were washed three times with ABST or PBST and 100 μl of freshly prepared p-nitrophenylphosphate (1 mg/ml) in 0.1 M Tris buffer-0.15 M NaCl was added and color development was quantified with a spectrophotometer at 405 nm.

[0068] Cervical Mucus: A sample of cervical mucus was obtained from a healthy donor and the gel phase separated by centrifugation. The pellet was washed three times by centrifugation and the mucin stabilized and alkylated before dialysis against a low ionic strength, pH 8.0 buffer. The cervical mucus was bound to flat-bottomed plates by incubating in bicarbonate coating buffer at 4° C. overnight. The plates were washed to remove unbound ligand. Biotinylated lectins were serially diluted across the plates in the wash buffer and the plates incubated at room temperature for 2 hrs. Unbound lectin was removed by washing, and the bound lectins were tagged by incubating with streptavidin-alkaline phosphatase at room temperature for 1 hr. Unbound streptavidin-alkaline phosphatase was removed by washing and the assay completed by adding freshly prepared p-nitrophenylphosphate (1 mg/ml) in 0.1 M Tris buffer-0.15 M NaCl) and monitoring the rate of color production.

[0069] Seminal Plasma and Sperm: A sample of ejaculate was donated by a healthy donor and the seminal plasma (supernatant) removed by centrifugation and frozen at −20° C. The binding assay was performed in the same way as for cervical mucus.

[0070] The sperm pellet resulting from centrifugation of the ejaculate was washed twice and total sperm count determined using a hemocytometer. Sperm were added to plates, left to settle at room temperature for 2 hrs and fixed using glutaraldehyde. The plates were then washed and unbound sites blocked with protein solution and stored at +4° C. until use. The remainder of the binding assay was performed in the same way as for cervical mucus and seminal plasma.

[0071] Serum: A sample of blood was collected from a healthy donor, the serum separated by centrifugation and stored at −20° C. The binding assay was performed in the same way as for cervical mucus and seminal fluid.

[0072] Analysis of data: Sigma Plot was used for graphing and curve fitting of binding plots. Velocity of the color-forming reaction versus concentration of lectin added was plotted. Binding curves were fitted to the hyperbolic equation f(x)=ax/(b+x) where “x” is the concentration of lectin, “f(x)” is the rate of reaction measured by change in optical density (OD) of the reaction solution per unit time, “a” is the asymptotic value of maximum reaction velocity measured as change in optical density per minute (represented in the following tables as mOD/min) and “b” is the concentration of lectin where half of maximum binding occurs (represented in the following tables as [Lectin]1/2 max). The binding “quotient” is defined as a/b.

[0073] The data for lectin binding to sperm, seminal plasma, cervical mucus, human serum, Neisseria gonorrhoeae, and Lactobacillus jensenii are summarized in the following tables wherein WB signifies weak binding, NB signifies no binding, and N/A signifies not available.

TABLE 2
SUMMARY OF BINDING DATA
				QUOTIENT
			Seminal	Cervical	Human
	Lectin	Sperm	Plasma	Mucus	Serum
	ABA	WB	0.44	WB	WB
	AL	NB	NB	NB	NB
	BPA	0.60	0.86	20.76	WB
	CAA	0.46	1.04	7.82	WB
	ConA	2.59	2.68	1.11	3.29
	CPA	WB	WB	WB	WB
	CSA	WB	0.30	7.30	WB
	DBA	WB	WB	WB	WB
	DSA	1.09	WB	WB	WB
	ECA	WB	WB	WB	WB
	EEA	NB	NB	0.39	NB
	GNA	0.36	0.58	0.24	WB
	GSA-I/GSA-II	WB	WB	WB	WB
	HAA	NB	WB	WB	WB
	Jacalin	3.43	11.63	21.55	8.93
	LAA	NB	0.57	WB	WB
	LBA	WB	WB	WB	WB
	LcH	7.26	2.58	8.64	1.60
	LES	WB	WB	WB	WB
	LOTUS	NB	0.94	4.13
	MAA	NB	WB	WB	NB
	MPA	2.29	3.17	13.8	1.18
	NPA	NB	NB	NB	NB
	PWA	WB	NB	NB	NB
	PHA-L	WB	WB	WB	NB
	PNA	WB	WB	7.25	NB
	PSA	3.44	2.70	14.5	1.12
	PTAgalactose	NB	WB	1.31	WB
	PTAgalNacnb	NB	NB	1.39	WB
	RPA	1.28	0.84	0.45	WB
	SBA	NB	WB	WB	NB
	SJA	NB	WB	WB	NB
	STA	NB	WB	WB	NB
	sWGA	1.32	7.50	WB	WB
	TKA	WB	0.87	WB	WB
	UEA-1	WB	WB	14.72	WB
	VPA	WB	2.78	5.21	2.02
	VRA	WB	3.35	WB	WB
	VVA	N/A	0.81	WB	WB
	WFA	2.48	1.96	26.24	WB
	WGA	19.38	4.87	12.77	1.13
	Notes
	1. N/A - not available
	2. NB - no binding
	3. WB - weak binding

[0074]

TABLE 3
LECTIN BINDING TO SPERM
		Max	[Lectin]1/2 Max
	Lectin	(mOD/min)	(μg/ml)	Quotient
	WGA	155	8	19.38
	LcH	196	27	7.26
	PSA	141	41	3.44
	Jacalin	103	30	3.43
	ConA	57	22	2.59
	WFA	67	27	2.48
	MPA	48	21	2.29
	sWGA	41	31	1.32
	RPA	120	94	1.28
	DSA	63	58	1.09
	BPA	67	112	0.60
	CAA	33	71	0.46
	GNA	27	74	0.36

[0075]

TABLE 4
LECTIN BINDING TO SEMINAL PLASMA
		Max	[Lectin]1/2 Max
	Lectin	(mOD/min)	(μg/ml)	Quotient
	Jacalin	93	8	11.63
	sWGA	45	6	7.50
	WGA	112	23	4.87
	VRA	208	62	3.35
	MPA	57	18	3.17
	VFA	125	45	2.7
	PSA	100	37	2.70
	ConA	51	19	2.68
	LcH	147	57	2.58
	WFA	49	25	1.96
	CAA	51	49	1.04
	LOTUS	32	34	0.94
	BPA	64	74	0.86
	RPA	56	64	0.88
	VVA	25	31	0.81
	GNA	38	65	0.58
	TKA	39	45	0.87
	LAA	37	65	0.57
	ADA			0.44
	CSA	25	82	0.30

[0076]

TABLE 5
LECTIN BINDING TO CERVICAL MUCUS
		Max	[Lectin]1/2 Max
	Lectin	(mOD/min)	(μg/ml)	Quotient
	WFA	656	25	26.24
	Jacalin	237	11	21.55
	BPA	353	17	20.76
	UEA-1	265	18	14.72
	PSA	58	4	14.50
	MPA	138	10	13.80
	WGA	562	44	12.77
	LcH	121	14	8.64
	CAA	352	45	7.82
	CSA	445	61	7.30
	PNA	174	24	7.25
	VFA	203	39	5.21
	LOTUS	194	47	4.13
	PTAgalNac	110	79	1.39
	PTAgalactose	113	86	1.31
	ConA	41	37	1.11
	RPA	25	56	0.45
	EEA	27	70	0.39
	GNA	13	55	0.24

[0077]

TABLE 6
LECTIN BINDING TO HUMAN SERUM
		Max	[Lectin]1/2 Max
	Lectin	(mOD/min)	(μg/ml)	Quotient
	Jacalin	134	15	8.93
	ConA	79	24	3.29
	VFA	107	53	2.02
	LcH	123	77	1.60
	MPA	40	34	1.18
	WGA	160	142	1.13
	PSA	84	75	1.12

[0078]

TABLE 7
LECTIN BINDING TO NEISSERIA GONORRHOEAE
pH 4
		Max	[Lectin]1/2 Max
	Lectin	(mOD/min)	(μg/ml)	Quotient
	BPA	1190	82	14.51
	CPA	80	33	2.42
	CSA	560	7	80.00
	GNA	294	18	16.33
	LAA	176	42	4.19
	LBA	275	14	19.64
	LCH	213	176	1.21
	LEA	106	7	14.29
	MAA	235	56	4.20
	MPA	159	5	31.80
	NPA	299	38	7.87
	PSA	55	13	4.23
	RPA	233	10	23.30
	SBA	414	8	51.75
	STA	194	24	7.57
	sWGA	49	0.50	90.00
	TKA	178	55	3.24
	VVA	411	3	137.00
	WFA	331	3	110.33
	WGA	125	0.78	160.26

[0079]

TABLE 8
LECTIN BINDING TO LACTOBACILLUS JENSENII
		Max	[Lectin]1/2 Max
	Lectin	(mOD/min)	(μg/ml)	Quotient
	ABA	216	2	108.00
	BPA	557	57	9.77
	GNA	405	12	33.75
	Jacalin	148	7	21.14
	LBA	334	15	22.27
	RPA	177	55	3.22
	SBA	523	63	8.30
	WFA	464	23	20.17
	STA	140	19	7.37
	LEA	45	82	0.55
	DSA	26	80	0.33
	MPA	2047	328	6.24
	ConA	301	7	43.00
	sWGA	96	64	1.50
	LAA	136	17	8.00
	CSA	624	387	1.61
	NPA	425	36	11.81
	VVA	260	33	7.88

[0080] In the above tables the affinity of the lectin for a particular substrate is inversely proportional to the maximum velocity of the color-forming reaction. Consequently, those lectins having a smaller b value ([lectin]1/2 max) bind more firmly to the substrate. A high binding efficacy (low mOD/min) is preferable for binding to sperm or seminal plasma for contraceptive purposes or to a pathogen, such as Neisseria gonorrhoeae, whose infections activity is to be inhibited. However, it must be recognized that some microorganisms of the vaginal flora, e.g., Lactobacillus jensenii, are desirable and may even provide some protection against pathogenic organisms. Accordingly, if possible, it is desirable to select a lectin for contraception and/or prophylaxis against sexually transmitted diseases that combines great binding affinity for the constituents of the male ejaculate or for a pathogenic microorganism, but has a lesser, preferably minimal, binding affinity for beneficial vaginal flora. A skilled practitioner may select the most efficacious lectins by consulting the data provided in the tables of this example.

EXAMPLE 2

[0081] This example illustrates the effectiveness of lectins in inhibiting the infective activity of Chlamydia trachomatis.

[0082] Chlamydia trachomatis serovar G was cultured as described in Example 1, lyophilized lectins were reconstituted in phosphate buffered saline (PBS) to a concentration of 1 mg/ml and frozen at −20° C. The lectins were prepared for testing in the Chlamydia trachomatis inactivation assay by diluting them in Minimum Essential Medium (MEM) with 10 mM HEPES and 50 μg/ml gentamycin sulfate to appropriate concentrations. Chlamydia trachomatis serovar G elementary bodies were added to the diluted lectins and the mixture was incubated for 1.5 hours at 37° C. After incubation, the Chlamydia-lectin mixture was added to monolayers of McCoy cells in 15×45 mm shell vials and centrifuged at 3500×g for 60 minutes at 37° C. Following centrifugation, the medium in the vials was removed and 1 ml of fresh Chlamydia overlay medium (with cycloheximide) was added to each vial. The vials were incubated for 40-43 hours and the cells were then fixed and stained for Chlamydia trachomatis using Syva Microtrak™ Chlamydia trachomatis culture confirmation reagent.

[0083] Samples of the infected cell culture were then examined under the fluorescence microscope and evaluated for the effect of the lectin on the infectivity of the microorganism. Table 9 shows the number of Chlamydia trachomatis inclusions per 160×microscopic field on a 12 mm circular glass coverslip as a percentage of a positive control sample which was not exposed to any lectins. WGA (118%) and ConA (121%) show enhanced infectivity of Chlamydia trachomatis serovar G in having more inclusions per 160×field than the positive control which had not been exposed to any lectins. In contrast, exposure to Jacalin shows significantly reduced infectivity of Chlamydia trachomatis serovar G as evidenced by the 65% reduction in the number of inclusions per 160×field (35% of the positive control value).

	TABLE 9
	Lectin	Concentration	Infectivity
	ABA	150	59
	TKA	150	80
	WGA	50	118
	DSA	50	75
	WFA	150	48
	VFA	150	61
	ConA	150	121
	Jacalin	150	35
	MPA	150	55

[0084] Table 10 shows the results of additional experiments for determining the anti-Chlamydia activity of selected lectins. The data in the table show that at concentrations of 150 μg/ml, the lectins designated HAA, ABA, and RPA significantly reduced infection of McCoy cells by C. trachomatis. However, of these three, only the lectin designated RPA was cytotoxic to McCoy cells. The lectins WGA and ConA potentiated chlamydial infectivity compared to control samples devoid of lectins.

TABLE 10
Anti-Chlamydia Activity of Lectins
	Concentration	Infectivity (a)
Lectin	(μg/ml)	Exp. 1	Exp. 2	Exp. 3	Exp. 4
HAA	150	40.4	44.0	42.0	42.1
ABA	150	48.8	62.0	62.3	57.7
RPA	150	59.6	60.0	60.0	59.9
WFA	150	73.8	72.9	95.9	80.9
NPA	150	81.4	99.0	69.3	83.2
GNA	150	82.0	94.2	83.4	86.5
sWGA	100	95.8	75.8	93.6	88.4
LAA	150	86.7	92.3	86.5	88.5
LBA	150	88.2	110.0	74.5	90.9
MAA	150	94.4	101.0	82.5	92.6
BPA	150	93.5	109.0	101.0	101.0
CSA	150	94.9	124.0	118.0	112.0
LEA	150	110.0	140.0	102.0	117.0
DSA	50	124.0	135.0	96.1	118.0
WGA	50	109.0	154.0	144.0	136.0
ConA	150	123.0	168.0	164.0	149.0

EXAMPLE 3

[0085] This example illustrates the effectiveness of lectins in blocking the infectivity of human immunodeficiency viruses Type 1 and 2 (HIV-1/HIV-2).

[0086] A number of lectins were evaluated for possible inhibitory effects against HIV-1 and HIV-2 replication in primary infected human T-lymphocyte CEM cells. The effect of lectins on the infectivity of HIV-1 and HIV-2 toward human lymphocytes was investigated in vitro by a standard technique (Balzarini et al. 1991, Antimicrobial Agents and Chemotherapy, March 1991, pages 410-416) wherein the toxicity of the lectins toward the infected cells was determined (human T-lymphocytes CEM/0) and also the ability of the lectins to block the fusion of infected cells (HUT-78/HIV-1(IIIB)) with other cells (MOLT/4 clone 8). The results of these tests are set forth in Tables 11 and 12 below. The results are expressed in terms of the concentration of lectins required to reduce by 50% the number of viable cells in the virus-infected cell cultures (EC50) and in the control cell cultures (mock-infected) (CC50), respectively. That is, CC50 is the cytotoxic concentration without virus and corresponds to lectin concentrations required to reduce by 50% the number of viable cells in the virus-infected culture.

TABLE 11
Anti-Virus Activity of Lectins
		EC50 (μg/ml)a
Lectin	HIV-1	HIV-2	CC50b (μg/ml)
GNA	0.80 ± 0.1	1.35 ± 0.6	>100
NPA	0.8 ± 0.2	0.9 ± 0.2	>200
ConA	111.5 ± 0.79	1.4 ± 0.77	20 ± 0.71
EEA	>0.16	>0.16	0.5 ± 0.4
MPA	>0.8	>0.8	8.9 ± 3.0
LCH	11 ± 8.2	>100	15 ± 2.9
HAA	15 ± 7.8	11.5	14 ± 5.9
WGA	≧16 ± 6.0	≧15 ± 7.8	13 ± 2.5
PSA	16 ± 6.4	82 ± 32	21 ± 5.7
DSA	>20	>20	1.5
JAC	>20	>20	22 ± 7.4
PHA-L	23 ± 19	>100	17 ± 8.5
PNA	>20	>20	88 ± 11
VFA	34 ± 25	≧100	97 ± 22
ABA	>100	>100	73 ± 15
CAA	>100	>100	≧140
CPA	>100	>100	>200
CSA	>100	>100	>200
ECA	≧100	≧100	14 ± 2.5
GSA-I	>100	>100	>200
GSA-II	>100	>100	±90
LAA	>100	>100	>200
LBA	>100	>100	>200
LEA	>100	>100	>200
Lotus	>100	>100	≧90
PAA	≧100	≧58	>200
PTA-gal	>100	>100	>200
PTA-galNAc	>100	>100	>200
SJA	>100	>100	>200
sWGA	>100	>100	>200
SBA	100	>100	NDc
TKA	>100	>100	98
UEA-I	>100	>100	>200
VVA	>100	>100	>200
WEA	>100	>100	>200
aConcentration required to inhibit HIV-1 and HIV-2 induced cytopathogenicity in human T-lymphocyte CEM cells. Data are the means ± s.d. of at least three independent experiments.
bConcentration required to inhibit CEM cell viability by 50%.
cND means not determined

[0087] The above data indicate that only a few lectins proved inhibitory to HIV-1 and HIV-2 replication in primary infected CEM cultures under the conditions of this experiment. At concentrations ranging from 0.80 to 1.5 μg/ml, the lectins designated GNA, NPA and ConA inhibited virus-induced cytopathogenicity in CEM cells by 50%; however, the lectin designated ConA also was found to by cytotoxic to CEM cells at about 20 μg/ml.

[0088] It should also be noted that in practice in administering lectins for contraceptive, prophylactic, and/or therapeutic use, it is not always preferred to use the lectin that binds most strongly to the target microorganism. For example, it is preferable to use lectins that will not stimulate a mitogenic response in the host.

TABLE 12
Inhibitory Effect of Lectins on Giant Cell Formation Between
HUT-78/HIV-1 (IIIB) and MOLT/4 clone 8 cells
	EC50 (μg/ml)
	Compound	Individual Values	Average
	ABA	>100->100	>100
	CAA	>100->100	>100
	ConA	1.7-9	5.4 ≧ 5.2
	CPA	>100->100	>100
	CSA	>100->100	>100
	ECA	>100->100	>100
	EEA	>4->4	>4
	GSA-I	>100->100	>100
	GSA-II	>100->100	>100
	HAA	>100->100	>100
	JAC	>100->100	>100
	LAA	>100->100	>100
	LBA	>100->100	>100
	LCH	45-45	45
	LEA	>100->100	>100
	Lotus	>100->100	>100
	MPA	>100->100	>100
	PAA	>100->100	>100
	PHA-L	44-12-44	33 ± 18
	PNA	>100->100	>100
	PSA	45-58-58	54 ± 7.5
	PTAgal	>100->100	>100
	PTAgalNac	>100->100	>100
	SJA	>100->100	>100
	sWGA	>100->100	>100
	TKA	>100->100	>100
	UEA-I	>100->100	>100
	UFA	>100->100	>100
	VVA	>100->100	>100
	WFA	>100->100	>100
	WGA	20->4	≧20
	* Cluster formation of the cells after 1 day incubation with the compound

[0089] The invention having now been fully described, it should be understood that it may be embodied in other specific forms or variations without departing from its spirit or essential characteristics. Accordingly, the embodiments described above are to be considered in all respects as illustrative and not restrictive, the scope of the invention being indicated by the appended claims rather than by the foregoing description, and all changes which come within the meaning and range of equivalency of the claims are intended to be embraced therein

Claims

1. A method of treating sexually transmitted infections comprising administering to the site of the infection an amount of a composition containing at least one lectin capable of binding to a pathogenic microorganism or to carbohydrate moieties expressed on the surface of epithelial cells at the site of the infection, said lectin being effective to diminish the infective capability of the microorganism, said lectin being dispersed in a biocompatible non-toxic vehicle.

2. The method of claim 1 wherein a plurality of lectins is administered.

3. The method of claim 1 wherein said disease is selected from the group consisting of gonorrhea, chlamydial infections, lymphogranuloma venereum, syphilis, chancroid, donovanosis, Mycoplasma hominis infections, Mycoplasma genitalium infections, Ureaplasma urealyticum infections, HIV-1 and HIV-2 infections, HTLV-1 infections, herpes simplex virus type 1 and type 2 infections, Epstein-Barr virus infections, infections with human papilloma viruses, molluscum contagiosum, cytomegalovirus infections, viral hepatitis, trichomoniasis, and candidiasis.

4. The method of claim 3 wherein a plurality of lectin is adminstered.

5. The method of claim 1 wherein said lectin is selected from the group consisting of BPA, CPA, CSA, GNA, LAA, LBA, LCH, LEA, MAA, MPA, NPA, PSA, RPA, SBA, STA, sWGA, TKA, VVA, WFA, and WGA.

6. The method of claim 5 wherein a plurality of lectins is administered.

7. The method of claim 1 wherein said sexually transmitted disease is infection with Chlamydia trachomatis and said lectin is selected from the group consisting of ABA, TKA, DSA, WFA, VFA, Jacalin, MPA, HAA, WGA, and GNA.

8. The method of claim 7 wherein a plurality of lectins is administered.

9. The method of claim 1 wherein said sexually transmitted disease is infection with HIV-1 or HIV-2 and said lectin is selected from the group consisting of ConA, EEA, GNA, MPA, and HAA.

10. The method of claim 9 wherein a plurality of lectins is administered.

11. The method of claim 1 wherein said sexually transmitted disease is gonorrhea and said lectin is selected from the group consisting of BPA, CPA, CSA, GNA, LAA, LBA, LCH, LEA, NPA, MAA, MPA, NPA, PSA, RPA, SBA, STA, sWGA, TKA, VVA, WFA, and WGA.

12. The method of claim 11 wherein a plurality of lectins is administered.

13. The method of claim 1 wherein said site of infection is the female or male urogenital tract.

14. A composition for administering lectins to the vagina comprising at least one lectin dispersed in a pharmacologically acceptable non-toxic vehicle.

15. The composition of claim 14 containing a plurality of lectins.

16. The composition of claim 14 wherein said lectin is selected from the group consisting of WGA, LcH, PSA, Jacalin, ConA, AS, WFA, MPA, sWGA, RPA, DSA, BPA, CAA, GNA, VRA, VFA, LOTUS, NPA, VVA, TKA, LAA, ABA, CSA, UEA-1, PNA, PTAgalNac, PTAgalactose, EEA, ORS, STA, PAA, LOA, and LEA.

17. The composition of claim 16 containing a plurality of lectins.

18. A device for administering lectins to the vagina comprising a solid support adapted to be inserted into the vagina, said support being impregnated with or coated with at least one lectin.

19. The device of claim 18 wherein a plurality of lectins are impregnated therein or coated thereon.

20. The device of claim 18 wherein said lectin is selected from the group consisting of WGA, LcH, PSA, Jacalin, ConA, AS, WFA, MPA, sWGA, RPA, DSA, BPA, CAA, GNA, VRA, VFA, LOTUS, NPA, VVA, TKA, LAA, ABA, CSA, UEA-1, PNA, PTAgalNac, PTAgalactose, EEA, ORS, STA, PAA, LOA, and LEA.

21. The device of claim 20 wherein a plurality of lectins are impregnated therein or coated thereon.