Antimicrobial peptides as microbicidal contraceptives: prophecies for prophylactics – a mini review

REFERENCES

• Joint United Nations programme on HIV/AIDS. AIDS Epidemic Update: December 1999. Geneva: United Nations, 1999
   Google Scholar
• Gerbase AC, Rowley JT, Heymann DHL, Berkley SFB, Piot P. Global prevalence and the incidence estimated of selected curable STDs. Sex Transm Inf 1998;74:12–16
   PubMedGoogle Scholar
• Uckun FM, D’Cruz OJ. Prophylactic contraceptives for HIV/AIDS. Hum Reprod Update 1999;5:506–14
   PubMed Web of Science ®Google Scholar
• Weber J, Nunn A, Connor O, et al. Chemical condoms for the prevention of HIV infection: evaluation of novel agents against SHIV89.6pd in vitro and in vivo. AIDS 2001;15:1563–8
   Google Scholar
• Hill R, Ryan J, Stone A, Fransen L. Vaginal microbicides for the prevention of HIV/AIDS: assessment of the potential market. Int J Pharm Med 2000; 14: 271–8
   Google Scholar
• Rosenberg Z, Van Damme L, Mauck C. Recommendations for the clinical development of topical microbicides: an update. AIDS 2001;15:857–68
   PubMed Web of Science ®Google Scholar
• Greenhead P, Hayes P, Watts P, Laing K, Griffin G, Shattock R. Parameters of human immunodeficiency virus infection of human cervical tissue and inhibition by vaginal virucides. J Virol 2000;74:5577–86
   PubMed Web of Science ®Google Scholar
• Stone A. Microbicides: The UNAIDS-sponsored trial of nonoxynol-9 gel. IPPF Med Bull 2000;34:3–4
   Google Scholar
• Stafford M, Ward H, Flanagan A, et al. Safety study of nonoxynol-9 as a vaginal microbicide: evidence of adverse effects. J Acquir Imm Def Syndrome 1998;17:327–31
   Web of Science ®Google Scholar
• Medzhitov R, Janeway CJ. Advances in immunology: innate immunity. N Engl J Med 2000;343:338–44
   PubMed Web of Science ®Google Scholar
• Lehrer RI, Ganz T. Antimicrobial peptides in mammalian and insect host defense. Curr Opin Immun 1999;11:23–7
   PubMed Web of Science ®Google Scholar
• Colilla FJ, Rocher A, Mendez E. Gamma-purothionins: amino acid sequence of two poly peptides of a new family of thionins from wheat endosperm. FEBS Letters 1990;270:191–4
   PubMed Web of Science ®Google Scholar
• Vizioli J, Salzet M. Antimicrobial peptides: New weapons to control parasitic infections? Trends Parasitol 2002;18:475–6
   PubMed Web of Science ®Google Scholar
• Bulet P, Hetru C, Dimarcq J, Hoffmann D. Antimicrobial peptides from insects: structure and function. Dev Comp Immun 1999;23:329–44
   PubMed Web of Science ®Google Scholar
• Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotney MJ. Purification, primary structures of antimicrobial peptide from bovine neutrophils. J Biol Chem 1993;268:6641–48
   PubMed Web of Science ®Google Scholar
• Schnapp D, Reid CJ, Harris A. Localization and expression of human a-defensin-1 in the pancreas and kidney. J Pathol 1998;186:99–103
   PubMed Web of Science ®Google Scholar
• Barra D, Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol 1995;13:205–10
   PubMed Web of Science ®Google Scholar
• Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2000;415:389–95
   Web of Science ®Google Scholar
• Hultmark D. Drosophila immunity: paths and patterns. Curr Opin Immunol 2003;15:12–19
   PubMed Web of Science ®Google Scholar
• Nakamura T, Furunaka H, Miyata T, et al. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus): Isolation and chemical structure. J Biol Chem 1988;263:16709–13
   PubMed Web of Science ®Google Scholar
• Sitaram N, Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity. Biochim Biophys Acta 1999;1462:29–54
   PubMed Web of Science ®Google Scholar
• Oren Z, Shai Y. Mode of action of linear amphipathic a helical antimicrobial peptides. Biopolymers 1998;47:451–63
   PubMed Web of Science ®Google Scholar
• Cudic M, Otvos L Jr. Intracellular targets of antibacterial peptides, Curr Drug Targets 2002;3:101–6
   Google Scholar
• Shai Y. Mechanism of the binding, insertional destabilization of phospholipid bilayer membranes by helical antimicrobial and cell non-selective membrane lytic peptides. Biochim Biophys Acta 1999;1462:55–70
   PubMed Web of Science ®Google Scholar
• White SH, Wimley WC, Selsted ME. Structure, function and membrane integration of defensins. Curr Opin Struct Biol 1995;5:521–7
   PubMed Web of Science ®Google Scholar
• Otvos L Jr. Antibacterial peptides isolated from insects. J Pept Sci 2000;6:497–511
   PubMed Web of Science ®Google Scholar
• Garcia-Olmedo F, Molina A, Alamillo JM, RodriguezPalenzuela P. Plant defense peptides. Biopolymers 1998;47:479–91
   PubMed Web of Science ®Google Scholar
• Schroder JM, Harder J. Human b defensin-2. Int J Biochem Cell Biol 1999;31:645–51
   PubMed Web of Science ®Google Scholar
• Lehrer RI, Ganz T. Defensins of vertebrate animals. Curr Opin Immunol 2002;14:96–102
   PubMed Web of Science ®Google Scholar
• Jones DE, Bevins CL. Paneth cells of human small intestine express an antimicrobial peptide gene. J Biol Chem 1992;267:23216–25
   PubMed Web of Science ®Google Scholar
• Schutte BC, Mitros JP, Bartlett JA, et al. Discovery of five conserved b defensin gene clusters using a computational search strategy. Proc Natl Acad Sci USA 2002;99:2129–33
   PubMed Web of Science ®Google Scholar
• Tang YQ, Yuan J, Osapay G, et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated a defensins. Science 1999;286:498–502
   PubMed Web of Science ®Google Scholar
• Daher KA, Selsted ME, Lehrer RI. Direct inactivation of viruses by human granulocyte defensins. J Virol 1986;60:1068–74
   PubMed Web of Science ®Google Scholar
• Lehrer RI, Daher K, Ganz T, Selsted ME. Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes. J Virol 1985;54:467–72
   PubMed Web of Science ®Google Scholar
• Van Strijp JA, Miltenberg LA, Vander Tol ME, Van Kessel KP, Fluit AC, Verhoef J. Degradation of herpes simplex virions by human polymorphonuclear leukocytes and monocytes. J Gen Virol 1990;71:1205–9
   PubMed Web of Science ®Google Scholar
• Sinha S, Cheshenko N, Lehrer RI, Herold BC. NP-1, a rabbit a defensin prevents the entry and intracellular spread of herpes simplex virus type 2. Antimicrob Agents Chemother. 2003;47:494–500
   PubMed Web of Science ®Google Scholar
• Zhang L, Yu Y, He T, et al. Contribution of human adefensin 1,2 and 3 to the anti HIV-1 activity of CD8 antiviral factor. Science 2002;298:995–1000
   PubMed Web of Science ®Google Scholar
• Chang TL, Francois F, Mosoian A, Klotman ME. CAFmediated human immunodeficiency virus (HIV) type 1 transcriptional inhibition is distinct from a-defensin-1 HIV inhibition. J Virol 2003;77:6777–84
   PubMed Web of Science ®Google Scholar
• Borenstein LA, Ganz T, Sell S, Lehrer RI, Miller JN. Contribution of rabbit leukocyte defensins to the host response in experimental syphilis. Infect Immun 1991;59:1368–77
   PubMed Web of Science ®Google Scholar
• Borenstein LA, Selsted ME, Lehrer RI, Miller JN. Antimicrobial activity of rabbit leukocyte defensins against Treponema pallidum subsp. pallidum. Infect Immun 1991;59:1359–67
   PubMed Web of Science ®Google Scholar
• Yasin B, Harwig SL, Lehrer RI, Wagar EA. Susceptibility of Chlamydia trachomatis to protegrins and defensins. Infect Immun 1996;64:709–13
   PubMed Web of Science ®Google Scholar
• Lehrer RI, Lichtenstein AK, Ganz T. Defensin: antimicrobial and cytotoxic peptides of mammalian cells. Annu Rev Immunol 1993;11:105–28
   PubMed Web of Science ®Google Scholar
• Fahrner RL, Dieckmann T, Harwig SSL, Lehrer RI, Feigon J. Solution structure of protegrin 1, a broad spectrum antimicrobial peptide from porcine leukocytes. Chem Biol 1996;3:543–50
   PubMed Web of Science ®Google Scholar
• Harwig SSL, Swiderek KM, Lee TD, Lehrer RI. Determination of disulfide bridges in PG-2, an antimicrobial peptide from porcine leukocytes. J Peptide Sci 1995;3:207–15
   Google Scholar
• Kokryakov VN, Harwig SSL, Panyutich EA, et al. Protegrins, leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett 1993;327:231–36
   PubMed Web of Science ®Google Scholar
• Lehrer RI, Panyutich EA, Oren A, et al. Protegrins: mechanisms of bactericidal activity against gram negative bacteria. J Invest Med 1990;43:288–94
   Google Scholar
• Qu X, Harwig SL, Oren A, Shafer WM, Lehrer RI. Susceptibilty of Neisseria gonorrhoeae to protegrins. Infect Immun 1996;65:636–9
   Google Scholar
• Qu X, Harwig SL, Shafer WM, Lehrer RI. Protegrin structure and activity against Neiserria gonorrhoeae. Infect Immun 1997;65:636–39
   PubMed Web of Science ®Google Scholar
• Tamamura H, Marakami T, Horiuchi S, et al. Synthesis of protegrin-related peptides and their antibacterial and anti-human immunodeficiency virus activity. Chem Pharm Bull 1995;43:853–8
   PubMed Web of Science ®Google Scholar
• Gennaro R, Zanetti M. Structural functions and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 2000;55:31–49
   PubMed Web of Science ®Google Scholar
• Zanetti M, Gennaro R, Romeo D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Letters 1995;374:1–5
   PubMed Web of Science ®Google Scholar
• Zanetti M, Litteri L, Gennaro R, Hortsmann H, Romeo D. Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules. J Cell Biol 1990;111:1363–71
   PubMed Web of Science ®Google Scholar
• Sorenson OE, Follin P, Johnson AH, et al. Human cathelicidin hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001;97:3951–9
   PubMed Web of Science ®Google Scholar
• Travis SM, Anderson NN, Forysth WB, et al. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect Immun 2000;68:2748–55
   PubMed Web of Science ®Google Scholar
• Sambri V, Marangoni A, Giacani L, et al. Comparative in vitro activity of five cathelicidin-derived synthetic peptides against Leptospira, Borrelia and Treponema pallidum. J Antimicrob Chemother 2002;50:895–902
   Google Scholar
• Hardy PH Jr, Levin J. Lack of endotoxin in Borrelia hispanica and Treponema pallidum. <i>Proc Soc Expt Biol Med 1983;174:47–52
   Google Scholar
• Takayama K, Rothenberg RJ, Barbour AG. Absence of lipopolysaccharide in the Lyme disease spirochete Borrelia burgdorferi. Infect Immun 1987;55:2311–13
   PubMed Web of Science ®Google Scholar
• Zasloff M. Magainins, a class of antimicrobial peptides from xenopus skin. Isolation, characterization of two active forms and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 1987;84:5449–56
   PubMed Web of Science ®Google Scholar
• Purnasai K, Reddy NP, Babu M. Investigations on wound healing by using amphibian skin. Ind J Exp Biol 1995;33:673–6
   PubMedGoogle Scholar
• Zasloff M, Martin B, Chen HC. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc Natl Acad Sci USA 1988;85:910–13
   PubMed Web of Science ®Google Scholar
• Reddy KVR, Shahani SK, Meherji PK. Spermicidal activity of magainins: in vitro and in vivo studies. Contraception 1996;53:205–10
   PubMed Web of Science ®Google Scholar
• Reddy KVR, Majramkar DD. Evaluation of the antifertility effect of magainin-a in rabbits in vitro and in vivo studies. Fertil Steril 2000;73:353–8
   PubMed Web of Science ®Google Scholar
• Reddy KVR, Aranha C. Studies on safety aspects of contraceptive magainin-A in rabbits. Ind J Exp Biol 2000;38:1217–21
   PubMedGoogle Scholar
• Aranha C, Majramkar DD, Reddy KVR. Preclinical evaluation of magainin-A as contraceptive antimicrobial agent. Fertil Steril 2004;81:1357–65
   PubMed Web of Science ®Google Scholar
• Hwang PM, Vogel HJ. Structure–function relationships of antimicrobial peptides. Biochem Cell Biol 1998;76:235–46
   PubMed Web of Science ®Google Scholar
• Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J Membr Biol 1997;156:197–211
   PubMed Web of Science ®Google Scholar
• Moore AJ, Beazley WD, Bibby MC, Devine DA. Antimicrobial activity of cecropins. J Antimicrob Chemother 1996;37:1077–89
   PubMed Web of Science ®Google Scholar
• Ballweber LM, Jaynes JE, Stamm WE, Lampe MF. In vitro microbicidal activitites of cecropin peptides D2A21 and D4E1 and gel formulations containing 0.1% to 2% D2A21 against Chlamydia trachomatis. Antimicrob Agents Chemother 2002;46:34–41
   Google Scholar
• Miyata T, Tokunaga F, Yoneya T, et al. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II and polyphemusins I and II. Chemical structures and biological activity. J Biochem 1989;106:663–8
   PubMed Web of Science ®Google Scholar
• Nakashima H, Masuda M, Murakami T, et al. Antihuman immunodeficiency virus activity of a novel synthetic peptide, T22 ([Tyr-5, 12, Lys-7] polyphemusin II): a possible inhibitor of virus-cell fusion. Antimicrob Agents Chemother 1992;36:1249–55
   PubMed Web of Science ®Google Scholar
• Murakami T, Nakajima T, Koyanagi Y, et al. A small molecule CXCR4 inhibitor that blocks T cell line-tropic HIV-1 infection. J Exp Med 1997;186:1389–93
   PubMed Web of Science ®Google Scholar
• Dempsey CE. The actions of melittin on membranes. Biochim Biophys Acta 1990;1031:143–61
   PubMed Web of Science ®Google Scholar
• Wade D, Andreu D, Mitchell SA, et al. Antibacterial peptides designed as analogs or hybrids of cecropins and melittin. Int J Pept Prot Res 1992;40:429–36
   PubMedGoogle Scholar
• Esser AF, Bartholomew RM, Jensen FC, MullerEberhardt HJ. Disassembly of viral membranes by complement independent channel formation. Proc Natl Acad Sci USA 1979;76:5843–7
   PubMed Web of Science ®Google Scholar
• Wachinger M, Kleinschmidt A, Winder D, et al. Antimicrobial peptides melittin and cecropin inhibit replication of human immunodeficiency virus 1 by suppressing viral gene expression. J Gen Virol, 1998;79:731–40
   PubMed Web of Science ®Google Scholar
• Wachinger M, Saermark T, Erfle V. Influence of amphipathic peptides on the HIV-1 production in persistently infected T-lymphoma cells. FEBS Letters. 1992;309:235–41
   PubMed Web of Science ®Google Scholar
• Breukink E, Kruijff B De. The lantibiotic nisin, a special case or not? Biochim Biophys Acta 1999;1462:223–34
   PubMed Web of Science ®Google Scholar
• Mulders JW, Boerrigter IJ, Rollema HS, Seizen RJ, De Vos W. Identification and characterization of the lantibiotic nisin Z. Eur J Biochem 2001;1991;581–4
   Google Scholar
• Delves-Broughton A. Nisin and its uses as a food preservative. Food Technol 1990;44:100–12
   Web of Science ®Google Scholar
• Clara A, Gupta SM, Reddy KVR. Spermicidal activity of Nisin: in vitro and in vitro studies. Contraception 2004;69:333–42
   PubMed Web of Science ®Google Scholar
• Reddy KVR, Aranha C, Gupta SM, Yedery RD. Evaluation of antimicrobial peptide nisin as a safe vaginal contraceptive agent in rabbits: in vitro and in vivo studies. Reproduction 2004;128:126–37
   Google Scholar
• Cole AM, Hong T, Boo LM, et al. Retrocyclin: a primate peptide that protect cells from infection by Tand M-tropic strains of HIV-1. Proc Natl Acad Sci USA, 2002;99:1813–18
   PubMed Web of Science ®Google Scholar
• Wexner SD. Sexually transmitted diseases of the colon, rectum, and anus. The challenge of the nineties. Diseases of the Colon and Rectum 1990;33:1048–62
   PubMed Web of Science ®Google Scholar
• Pye G, Evans DF, Ledingham S, Hardcastle JD. Gastrointestinal intraluminal pH in normal subjects and those with colorectal adenoma or carcinoma. Gut 1990;31:1355–7
   PubMed Web of Science ®Google Scholar