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rdf:type |
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lifeskim:mentions |
umls-concept:C0014662,
umls-concept:C0017279,
umls-concept:C0178539,
umls-concept:C0205087,
umls-concept:C0282629,
umls-concept:C0599697,
umls-concept:C0919496,
umls-concept:C0968902,
umls-concept:C1180347,
umls-concept:C1514562,
umls-concept:C1705552,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
12
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pubmed:dateCreated |
1998-11-30
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pubmed:abstractText |
We have identified an interaction between the equine infectious anemia virus (EIAV) late assembly domain and the cellular AP-2 clathrin-associated adapter protein complex. A YXXL motif within the EIAV Gag late assembly domain was previously characterized as a sequence critical for release of assembling virions. We now show that this YXXL sequence interacts in vitro with the AP-50 subunit of the AP-2 complex, while the functionally interchangeable late assembly domains carried by the Rous sarcoma virus p2b protein and human immunodeficiency virus type 1 p6 protein, which utilize PPPY and PTAPP L domains, respectively, do not bind AP-50 in vitro. In addition, EIAV late domain mutants containing mutations that have previously been shown to abrogate budding also exhibit marked decreases in AP-50 binding efficiencies. A role for AP-2 complex in viral assembly is supported by immunofluorescence analysis of EIAV-infected equine dermal cells demonstrating specific colocalization of the alpha adaptin subunit of AP-2 with the EIAV p9 protein at sites of virus budding on the plasma membrane. These data provide strong evidence that EIAV utilizes the cellular AP-2 complex to accomplish virion assembly and release.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-1423600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-170408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-2014240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-2564002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-2867098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-3029406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-6178843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7474093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7569928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7593326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7636963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7636991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7648278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7782338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-7846762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-8083996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-8280459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-8599109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-8657277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-8764091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-9261374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-9400603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-9557699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9811764-9624176
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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 |
Dec
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10218-21
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9811764-Amino Acid Sequence,
pubmed-meshheading:9811764-Animals,
pubmed-meshheading:9811764-COS Cells,
pubmed-meshheading:9811764-DNA-Binding Proteins,
pubmed-meshheading:9811764-Gene Products, gag,
pubmed-meshheading:9811764-Humans,
pubmed-meshheading:9811764-Infectious Anemia Virus, Equine,
pubmed-meshheading:9811764-Macromolecular Substances,
pubmed-meshheading:9811764-Mutagenesis, Site-Directed,
pubmed-meshheading:9811764-Protein Conformation,
pubmed-meshheading:9811764-Recombinant Fusion Proteins,
pubmed-meshheading:9811764-Transcription Factor AP-2,
pubmed-meshheading:9811764-Transcription Factors
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pubmed:year |
1998
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pubmed:articleTitle |
Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly.
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pubmed:affiliation |
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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