Lysis of human immunodeficiency virus type 1 by a specific secreted human phospholipase A2.
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.
Kim
Jae-Ouk
JO
Vaccine Research Center, NIAID, National Institutes of Health, Room 4502, Bldg. 40, MSC-3005, 40 Convent Dr., Bethesda, MD 20892-3005, USA.
Chakrabarti
Bimal K
BK
Guha-Niyogi
Anuradha
A
Louder
Mark K
MK
Mascola
John R
JR
Ganesh
Lakshmanan
L
Nabel
Gary J
GJ
D000163:Acquired Immunodeficiency Syndrome / Q000276:immunology / Q000821:virology; D002460:Cell Line; D015658:HIV Infections / Q000821:virology*; D015497:HIV-1 / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D019718:Receptors, CXCR4 / Q000378:metabolism; D014771:Virion / Q000378:metabolism* / Q000502:physiology
D019718:Receptors, CXCR4; D010741:Phospholipases A; D054467:Phospholipases A2