Inactivation of human immunodeficiency virus type 1 by the amine oxidase-peroxidase system
Autor: | F Kazazi, S J Klebanoff |
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Rok vydání: | 1995 |
Předmět: |
Male
Microbiology (medical) Amine oxidase Hot Temperature Spermine HIV Infections In Vitro Techniques Virus Replication Antiviral Agents Cell Line Superoxide dismutase chemistry.chemical_compound Semen Polyamines Humans Oxidoreductases Acting on CH-NH Group Donors biology Amine oxidase (copper-containing) Hydrogen Peroxide Catalase Molecular biology Spermidine Peroxidases chemistry Biochemistry Vagina HIV-1 biology.protein Female Amine Oxidase (Copper-Containing) Polyamine Research Article Peroxidase |
Zdroj: | Journal of Clinical Microbiology. 33:2054-2057 |
ISSN: | 1098-660X 0095-1137 |
Popis: | Human immunodeficiency virus type 1 (HIV-1) is rapidly inactivated by exposure to a naturally occurring antimicrobial system consisting of peroxidase, H2O2, and a halide. Among the potential sources of H2O2 is the amine oxidase system in which mono-, di-, and polyamines are oxidatively 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 polyamine 15-deoxyspergualin are viricidal to HIV-1 when combined with amine oxidase and myeloperoxidase. Antiviral activity required each component of the spermine-amine oxidase-peroxidase system and was inhibited by azide (a peroxidase inhibitor) and by catalase but not by superoxide dismutase. Heat treatment of catalase largely abolished its inhibitory effect. These findings implicate H2O2 formed by the amine oxidase system in the antiviral effect and raise the possibility that the polyamine-amine oxidase-peroxidase system influences the survival of HIV-1 in semen and in the vaginal canal. |
Databáze: | OpenAIRE |
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