Document Detail


Binding of HIV-1 to its receptor induces tyrosine phosphorylation of several CD4-associated proteins, including the phosphatidylinositol 3-kinase.
MedLine Citation:
PMID:  9123823     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell surface CD4 molecules are known to be important in several physiological responses of T lymphocytes. The use of human immunodeficiency virus (HIV) particles or purified gp120 molecules as CD4 cross-linking agents has been shown to result in a cascade of intracellular biochemical events. In addition, we and other have provided evidence suggesting that virus-mediated CD4 multimerization can lead to modulation of HIV-1 long terminal repeat-dependent activity and virus production. We were thus interested in measuring the effect of HIV-1 particles on intracellular tyrosine-phosphorylation levels, mostly of CD4-associated proteins. Using the T cell line CEM-T4, we observed that HIV-1 induces an increase in tyrosine phosphorylation of four major proteins physically complexed to the CD4 molecule. Immunoblot analysis permitted the identification of two of these proteins, p56lck and phosphatidylinositol 3-kinase (PI 3-kinase) p85 alpha. No concomitant variation in the level of these two CD4-associated proteins was observed after HIV-1-induced CD4 cross-linking. To our knowledge, this is the first report linking HIV-1-mediated CD4 multimerization to an increase in tyrosine phosphorylation of the PI 3-kinase complex. The four CD4-associated molecules described in this report are most likely implicated in virus-induced CD4-linked signaling events.
Authors:
G Briand; B Barbeau; M Tremblay
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Virology     Volume:  228     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  1997 Feb 
Date Detail:
Created Date:  1997-04-21     Completed Date:  1997-04-21     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  171-9     Citation Subset:  IM; X    
Affiliation:
Centre de Recherche en Infectiologie, Centre Hospitalier Universitaire de Québec, Canada.
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase
Animals
Antigens, CD4 / metabolism
CD4-Positive T-Lymphocytes / cytology
HIV-1 / metabolism*
Humans
Jurkat Cells
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
Mice
Phosphorylation
Phosphotransferases (Alcohol Group Acceptor) / metabolism*
Receptors, HIV / metabolism*
Tumor Cells, Cultured
Tyrosine / metabolism*
src-Family Kinases / metabolism*
Chemical
Reg. No./Substance:
0/Antigens, CD4; 0/Receptors, HIV; 55520-40-6/Tyrosine; EC 2.7.1.-/Phosphotransferases (Alcohol Group Acceptor); EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.10.2/Lymphocyte Specific Protein Tyrosine Kinase p56(lck); EC 2.7.10.2/src-Family Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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