Inactivation of herpes simplex virus by protein components of bovine neutrophil granules.

From an acid extract of granules of bovine neutrophils we isolated fractions of cationic proteins, exhibiting significant anti-herpesvirus activity at concentrations which were devoid of cytotoxicity and of activity against a picornavirus (rhinovirus). The mechanism of action seems to involve a direct neutralization of the virions. Two antiviral peptides with an approximate MW 7500 were purified to homogeneity by reversed phase high-performance liquid chromatography. Proline and arginine accounted for about 43% and 26-27% of their amino acid residues. One of these peptides (IIIa2 beta) had an MIC of 2 microM.