The Nucleoside Triphosphate Diphosphohydrolase-1/CD39 Is Incorporated into Human Immunodeficiency Type 1 Particles, Where It Remains Biologically Active

Human immunodeficiency virus type 1 (HIV-1) carries a variety of host proteins in addition to virus-encoded structural proteins, both in its envelope and inside the viral particle. Previous studies have reported that the HIV-1 life-cycle is affected by such virus-associated host cell surface protein...

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Bibliographic Details
Published in:Journal of molecular biology 2007-08, Vol.371 (1), p.269-282
Main Authors: Barat, Corinne, Martin, Geneviève, Beaudoin, Adrien R., Sévigny, Jean, Tremblay, Michel J.
Format: Article
Language:English
Subjects:
Adenosine Diphosphate - metabolism
Animals
Antigens, CD - chemistry
Antigens, CD - genetics
Antigens, CD - metabolism
Apyrase - chemistry
Apyrase - genetics
Apyrase - metabolism
ATPase
CD39
Cell Line
cell surface molecules
HIV-1
HIV-1 - metabolism
HIV-1 - ultrastructure
Human immunodeficiency virus 1
Humans
Platelet Aggregation - physiology
thromboregulation
Virion - metabolism
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Summary:Human immunodeficiency virus type 1 (HIV-1) carries a variety of host proteins in addition to virus-encoded structural proteins, both in its envelope and inside the viral particle. Previous studies have reported that the HIV-1 life-cycle is affected by such virus-associated host cell surface proteins. The nucleoside triphosphate diphosphohydrolase-1 (NTPDase1), also known as CD39, is a plasma membrane-bound ectoenzyme that hydrolyzes extracellular ATP and ADP to AMP. It has been shown that CD39 inhibits platelet function, and is thus a critical thromboregulatory molecule. We demonstrate here that host-derived CD39 is acquired by both laboratory-adapted and clinical variants of HIV-1 produced in cellular reservoirs of the virus. Moreover, purified CD39-bearing virions, but not isogenic viruses lacking CD39, display strong ATPase and ADPase activities. It is of particular interest that virions bearing this cellular enzyme can inhibit ADP-induced platelet aggregation, an effect blocked by an NTPDase inhibitor. On the basis of published and the present data on the functionality of human cellular proteins embedded within HIV-1, it can be proposed that these proteins might contribute to some of the immunologic deficiencies seen in infected individuals.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2007.05.012