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.
Zerial
A
A
Rhône Poulenc Santé, Centre de Recherches de Vitry, Vitry-sur-Seine, France.
Skerlavaj
B
B
Gennaro
R
R
Romeo
D
D
D000818:Animals; D000998:Antiviral Agents / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D001798:Blood Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D002417:Cattle; D002460:Cell Line; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003594:Cytoplasmic Granules / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D009504:Neutrophils / Q000032:analysis*; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology; D018139:Simplexvirus / Q000187:drug effects* / Q000502:physiology
D000998:Antiviral Agents; D001798:Blood Proteins; D010455:Peptides