Open AccessLysis of Human Immunodeficiency Virus Type 1 by a Specific Secreted Human Phospholipase A2
Author(s) -
Jae Ouk Kim,
Bimal K. Chakrabarti,
Anuradha Guha-Niyogi,
Mark K. Louder,
John R. Mascola,
Ganesh Lakshmanan,
Gary J. Nabel
Publication year - 2007
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01790-06
Subject(s) - biology , virology , lysis , human immunodeficiency virus (hiv) , human disease , secretion , microbiology and biotechnology , biochemistry , gene
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.