INACTIVATION OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 BY THE AMINE OXIDASE-PEROXIDASE SYSTEM

Human immunodeficiency virus type 1 (HIV-1) is rapidly inactivated by exposure to a naturally occurring antimicrobial system consisting of p eroxidase, H2O2 and a halide. Among the potential sources of H2O2 is t he amine oxidase system in which mono-, di-, and polyamines are oxidat ively deaminated with the formation of H2O2. The polyamine spermine is present at exceptionally high concentrations in semen. We report here that spermine, spermidine, and, to a lesser degree, the synthetic pol yamine 15-deoxyspergualin are viricidal to HIV-1 when combined with am ine oxidase and myeloperoxidase. Antiviral activity required each comp onent of the spermine-amine oxidase-peroxidase system and was inhibite d by azide (a peroxidase inhibitor) and by catalase but not by superox ide dismutase. Heat treatment of catalase largely abolished its inhibi tory effect. These findings implicate H2O2 formed by the amine oxidase system in the antiviral effect and raise the possibility that the pol yamine-amine oxidase-peroxidase system influences the survival of HIV- 1 in semen and in the vaginal canal.