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 language | English (US) |
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Pages (from-to) | 1444-1450 |
Number of pages | 7 |
Journal | Journal of Virology |
Volume | 81 |
Issue number | 3 |
DOIs | |
State | Published - Feb 2007 |
Externally published | Yes |
ASJC Scopus subject areas
- Immunology