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

J Virol. 2007 Feb;81(3):1444-50. doi: 10.1128/JVI.01790-06. Epub 2006 Nov 8.

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.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Acquired Immunodeficiency Syndrome / immunology
  • Acquired Immunodeficiency Syndrome / virology
  • Cell Line
  • HIV Infections / virology*
  • HIV-1 / metabolism*
  • HIV-1 / physiology
  • Humans
  • Phospholipases A / metabolism*
  • Phospholipases A2
  • Receptors, CXCR4 / metabolism
  • Virion / metabolism*
  • Virion / physiology

Substances

  • Receptors, CXCR4
  • Phospholipases A
  • Phospholipases A2