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

Jae Ouk Kim, Bimal K. Chakrabarti, Anuradha Guha-Niyogi, Mark K. Louder, John R. Mascola, Lakshmanan Ganesh, Gary J. Nabel

Research output: Contribution to journalArticle

Abstract

Phospholipase A2 (PLA2) proteins affect cellular activation, signal transdnction, 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.

Original languageEnglish (US)
Pages (from-to)1444-1450
Number of pages7
JournalJournal of Virology
Volume81
Issue number3
DOIs
StatePublished - Feb 2007
Externally publishedYes

ASJC Scopus subject areas

  • Immunology

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    Kim, J. O., Chakrabarti, B. K., Guha-Niyogi, A., Louder, M. K., Mascola, J. R., Ganesh, L., & Nabel, G. J. (2007). Lysis of human immunodeficiency virus type 1 by a specific secreted human phospholipase A2. Journal of Virology, 81(3), 1444-1450. https://doi.org/10.1128/JVI.01790-06