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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2001-5-23
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pubmed:abstractText |
The virus infectivity factor (Vif) protein facilitates the replication of human immunodeficiency virus type 1 (HIV-1) in primary lymphocytes and macrophages. Its action is strongly dependent on the cellular environment, and it has been proposed that the Vif protein counteracts cellular activities that would otherwise limit HIV-1 replication. Using a glutathione S-transferase pull-down assay, we identified that Vif binds specifically to the Src homology 3 domain of Hck, a tyrosine kinase from the Src family. The interaction between Vif and the full-length Hck was further assessed by co-precipitation assays in vitro and in human cells. The Vif protein repressed the kinase activity of Hck and was not itself a substrate for Hck phosphorylation. Within one single replication cycle of HIV-1, Hck was able to inhibit the production and the infectivity of vif-deleted virus but not that of wild-type virus. Accordingly, HIV-1 vif- replication was delayed in Jurkat T cell clones stably expressing Hck. Our data demonstrate that Hck controls negatively HIV-1 replication and that this inhibition is suppressed by the expression of Vif. Hck, which is present in monocyte-macrophage cells, represents the first identified cellular inhibitor of HIV-1 replication overcome by Vif.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16885-93
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11278465-Amino Acid Sequence,
pubmed-meshheading:11278465-Cell Line,
pubmed-meshheading:11278465-Cloning, Molecular,
pubmed-meshheading:11278465-Consensus Sequence,
pubmed-meshheading:11278465-Gene Products, vif,
pubmed-meshheading:11278465-Genes, vif,
pubmed-meshheading:11278465-HIV-1,
pubmed-meshheading:11278465-HeLa Cells,
pubmed-meshheading:11278465-Humans,
pubmed-meshheading:11278465-Jurkat Cells,
pubmed-meshheading:11278465-Kidney,
pubmed-meshheading:11278465-Kinetics,
pubmed-meshheading:11278465-Molecular Sequence Data,
pubmed-meshheading:11278465-Protein-Tyrosine Kinases,
pubmed-meshheading:11278465-Proto-Oncogene Proteins,
pubmed-meshheading:11278465-Proto-Oncogene Proteins c-hck,
pubmed-meshheading:11278465-Proto-Oncogenes,
pubmed-meshheading:11278465-Recombinant Proteins,
pubmed-meshheading:11278465-Sequence Alignment,
pubmed-meshheading:11278465-Sequence Homology, Amino Acid,
pubmed-meshheading:11278465-U937 Cells,
pubmed-meshheading:11278465-Virus Replication,
pubmed-meshheading:11278465-src Homology Domains,
pubmed-meshheading:11278465-vif Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2001
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pubmed:articleTitle |
The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein.
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pubmed:affiliation |
INSERM Unit 372, Université de la Méditerranée, 163 Avenue de Luminy, 13276 Marseilles Cedex 09, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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