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


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.

SUBMITTER: Kim JO 

PROVIDER: S-EPMC1797512 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature

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

Kim Jae-Ouk JO   Chakrabarti Bimal K BK   Guha-Niyogi Anuradha A   Louder Mark K MK   Mascola John R JR   Ganesh Lakshmanan L   Nabel Gary J GJ  

Journal of virology 20061108 3


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  ...[more]

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