Lysis of human immunodeficiency virus type 1 by a specific secreted human phospholipase A2.

Vaccine Research Center, NIAID, National Institutes of Health, Room 4502, Bldg. 40, MSC-3005, 40 Convent Dr., Bethesda, MD 20892-3005, USA.
Journal of Virology (Impact Factor: 4.65). 03/2007; 81(3):1444-50. DOI: 10.1128/JVI.01790-06
Source: PubMed

ABSTRACT Phospholipase A2 (PLA2) proteins affect cellular activation, signal transduction, and possibly innate immunity. A specific secretory PLA2, sPLA2-X, is shown here to neutralize human immunodeficiency virus type 1 (HIV-1) through degradation of the viral membrane. Catalytic function was required for antiviral activity, and the target cells of infection were unaffected. sPLA2-X potently reduced gene transfer of HIV-1 Env-pseudotyped lentivirus vectors and inhibited the replication of both CCR5- and CXCR4-tropic HIV-1 in human CD4+ T cells. Virions resistant to damage by antibody and complement were sensitive to lysis by sPLA2-X, suggesting a novel mechanism of antiviral surveillance independent of the acquired immune system.

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Available from: Mark K Louder, Aug 24, 2015
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    • "Finally, group X sPLA2 (PLA2G10) protein could neutralize several enveloped lentiviruses, including HIV-1, through the phospholipid hydrolysis of the viral membranes [13]. As these in vitro studies suggest, PLA2 enzymes may influence HIV infection. "
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