Defensins

Literature References: A class of low molecular weight cationic peptides which have in vitro microbiocidal activity against various bacteria, fungi, and viruses, originally isolated from mammalian neutrophils. Possess similar arginine-rich, cysteine-rich structures of 29-35 amino acids with a conserved core of 8-11 residues. Characterized by six cysteines comprising 3 disulfide linkages. Abbreviated NP (neutrophil peptide) where NP is used for rabbit, HNP for human, GPNP for guinea pig etc.; defensins represent a major protein component of granulocytes. Initial identification studies: H. I. Zeya, J. K. Spitznagel, Science 142, 1085 (1961); eidem, J. Bacteriol. 91, 750 (1966). Isoln, antimicrobial activities and amino acid sequence of six NPs: M. E. Selsted et al., Infect. Immun. 45, 150 (1984); M. E. Selsted et al., J. Biol. Chem. 260, 4579 (1985); of three HNPs: T. Ganz et al., J. Clin. Invest. 76, 1427 (1985); M. E. Selsted et al., ibid. 1436. Crystal structure of HNP-3: C. P. Hill et al., Science 251, 1481 (1991). Direct inactivation of enveloped viruses: K. A. Daher et al., J. Virol. 60, 1068 (1986). In vitro cytolysis of tumor cells: A. Lichtenstein et al., Blood 68, 1407 (1986). Mechanism of cytolysis: eidem, J. Immunol. 140, 2686 (1988). Identification and isoln of insect defensins from haemolymph of dipteran: J. A. Hoffmann, D. Hoffmann, Res. Immunol. 141, 910 (1990). Structure determn of insect forms: P. Lepage et al., Eur. J. Biochem. 196, 735 (1991). Review of insect forms: J. A. Hoffmann, C. Hetru, Immunol. Today 13, 411-415 (1992). Review: B. L. Kagan et al., Toxicology 87, 131-149 (1994); including insect forms: T. Ganz, R. I. Lehrer, Pharmacol. Ther. 66, 191-205 (1995).