Defensin HNP-2 is a peptide with antimicrobial properties that is secreted by human polymorphonuclear leukocytes (PMNs).1 It induces 26.2 and 43.5% lysis of mammalian cells at concentrations of 25 and 100 μg/ml, respectively.2 It also completely inhibits secretion of the exotoxin superantigen TSS toxin-1 (TSST-1) from S. aureus at a concentration of 5 ng/ml and inhibits infection of McCoy cells by C. trachomatis elementary bodies (EBs).3,4 Defensin HNP-2 binds to recombinant HIV-1 envelope glycoprotein gp120 and human CD4 (Kds = 8 and 15.8 nM, respectively).5 It also induces permeabilization of large unilamellar vesicles (LUVs) formed from 1-palmitoyl-2-oleoyl-sn-glycero-3-PG .6
1.Lehrer, R.I.Primate defensinsNat. Rev. Microbiol.2(9)727-738(2004) 2.Lichtenstein, A., Ganz, T., Selsted, M.E., et al.In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytesBlood68(6)1407-1410(1986) 3.Merriman, J.A., Nemeth, K.A., and Schlievert, P.M.Novel antimicrobial peptides that inhibit gram positive bacterial exotoxin synthesisPLoS One9(4)(2014) 4.Yasin, B., Harwig, S.S.L., Lehrer, R.I., et al.Susceptibility of Chlamydia trachomatis to protegrins and defensinsInfect. Immun.64(3)709-713(1996) 5.Wang, W., Owen, S.M., Rudolph, D.L., et al.Activity of ɑ- and θ-defensins against primary isolates of HIV-1J. Immunol.173(1)515-520(2004) 6.Wimley, W.C., Selsted, M.E., and White, S.H.Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric poresProtein Sci.3(9)1362-1373(1994)