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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-10-2
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pubmed:abstractText |
Human immunodeficiency virus (HIV) Nef functions are thought to be mediated via interactions with cellular proteins. Utilizing zone velocity sedimentation in glycerol gradients we found that recombinant HIV-1 Nef non-covalently associates with actin forming a high-molecular-mass complex of 150-300 kDa. This Nef/actin complex was present in human B and T lymphocytes but not in insect cells and was dependent on the N-terminal myristoylation of Nef, whereas the SH3-binding proline motif of Nef was not involved. Despite being myristoylated, HIV-2 Nef did not associate with actin. This might reflect differences in the subcellular localization of Nef since cell-fractionation experiments revealed that HIV-1 Nef was virtually exclusively localized in the cytoskeletal (detergent-insoluble) fraction whereas HIV-2 Nef had significantly reduced affinity for the cytoskeleton. Colocalization experiments in HIV-1-infected CD4+ fibroblasts revealed that Nef/actin complexes may also exist in HIV-infected cells. This novel interaction of HIV-1 Nef with actin provides insight into the association of Nef with cellular structures and reveals general differences in the interactions of the Nef proteins from HIV-1 and HIV-2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, nef,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nef Gene Products, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
247
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
843-51
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9288906-Actins,
pubmed-meshheading:9288906-Animals,
pubmed-meshheading:9288906-Cell Line,
pubmed-meshheading:9288906-Gene Products, nef,
pubmed-meshheading:9288906-HIV-1,
pubmed-meshheading:9288906-HIV-2,
pubmed-meshheading:9288906-Molecular Weight,
pubmed-meshheading:9288906-Myristic Acid,
pubmed-meshheading:9288906-Myristic Acids,
pubmed-meshheading:9288906-Protein Binding,
pubmed-meshheading:9288906-Recombinant Proteins,
pubmed-meshheading:9288906-Spodoptera,
pubmed-meshheading:9288906-Subcellular Fractions,
pubmed-meshheading:9288906-T-Lymphocytes,
pubmed-meshheading:9288906-nef Gene Products, Human Immunodeficiency Virus
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pubmed:year |
1997
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pubmed:articleTitle |
Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization.
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pubmed:affiliation |
Universitätskliniken des Saarlandes, Institut für Med. Mikrobiologie und Hygiene, Abt. Virologie, Homburg/Saar, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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