Linked Life Data

16215227

Source:http://linkedlifedata.com/resource/pubmed/id/16215227

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
2005-12-5
pubmed:abstractText
The proline-rich L domains of human immunodeficiency virus 1 (HIV-1) and other retroviruses interact with late endocytic proteins during virion assembly and budding. In contrast, the YPDL L domain of equine infectious anemia virus (EIAV) is apparently unique in its reported ability to interact both with the mu2 subunit of the AP-2 adaptor protein complex and with ALG-2-interacting protein 1 (AIP1/Alix) protein factors involved in early and late endosome formation, respectively. To define further the mechanisms by which EIAV adapts vesicle trafficking machinery to facilitate virion production, we have examined the specificity of EIAV p9 binding to endocytic factors and the effects on virion production of alterations in early and late endocytic protein expression. The results of these studies demonstrated that (i) an approximately 300-residue region of AIP1/Alix-(409-715) was sufficient for binding to the EIAV YPDL motif; (ii) overexpression of AIP1/Alix or AP-2 mu2 subunit specifically inhibited YPDL-mediated EIAV budding; (iii) virion budding from a replication-competent EIAV variant with its L domain replaced by the HIV PTAP sequence was inhibited by wild type or mutant mu2 to a level similar to that observed when a dominant-negative mutant of Tsg101 was expressed; and (iv) overexpression or siRNA silencing of AIP1/Alix and AP-2 revealed additive suppression of YPDL-mediated EIAV budding. Taken together, these results indicated that both early and late endocytic proteins facilitate EIAV production mediated by either YPDL or PTAP L domains, suggesting a comprehensive involvement of endocytic factors in retroviral assembly and budding that can be accessed by distinct L domain specificities.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
40474-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:16215227-Adaptor Protein Complex 2, pubmed-meshheading:16215227-Animals, pubmed-meshheading:16215227-COS Cells, pubmed-meshheading:16215227-Carrier Proteins, pubmed-meshheading:16215227-Cercopithecus aethiops, pubmed-meshheading:16215227-DNA, Viral, pubmed-meshheading:16215227-Endocytosis, pubmed-meshheading:16215227-Gene Silencing, pubmed-meshheading:16215227-Glutathione Transferase, pubmed-meshheading:16215227-HeLa Cells, pubmed-meshheading:16215227-Humans, pubmed-meshheading:16215227-Infectious Anemia Virus, Equine, pubmed-meshheading:16215227-Mutagenesis, pubmed-meshheading:16215227-Protein Subunits, pubmed-meshheading:16215227-Proteins, pubmed-meshheading:16215227-Proviruses, pubmed-meshheading:16215227-RNA, Small Interfering, pubmed-meshheading:16215227-Recombinant Fusion Proteins, pubmed-meshheading:16215227-Saccharomyces cerevisiae, pubmed-meshheading:16215227-Transfection, pubmed-meshheading:16215227-Two-Hybrid System Techniques, pubmed-meshheading:16215227-Viral Proteins
pubmed:year
2005
pubmed:articleTitle
Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding.
pubmed:affiliation
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural