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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2008-12-18
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pubmed:abstractText |
The human immunodeficiency virus 1 (HIV-1) envelope regulates the initial attachment of viral particles to target cells through its association with CD4 and either CXCR4 or CCR5. Although F-actin is required for CD4 and CXCR4 redistribution, little is known about the molecular mechanisms underlying this fundamental process in HIV infection. Using CD4(+) CXCR4(+) permissive human leukemic CEM T cells and primary lymphocytes, we have investigated whether HIV-1 Env might promote viral entry and infection by activating ERM (ezrin-radixin-moesin) proteins to regulate F-actin reorganization and CD4/CXCR4 co-clustering. The interaction of the X4-tropic protein HIV-1 gp120 with CD4 augments ezrin and moesin phosphorylation in human permissive T cells, thereby regulating ezrin-moesin activation. Moreover, the association and clustering of CD4-CXCR4 induced by HIV-1 gp120 requires moesin-mediated anchoring of actin in the plasma membrane. Suppression of moesin expression with dominant-negative N-moesin or specific moesin silencing impedes reorganization of F-actin and HIV-1 entry and infection mediated by the HIV-1 envelope protein complex. Therefore, we propose that activated moesin promotes F-actin redistribution and CD4-CXCR4 clustering and is also required for efficient X4-tropic HIV-1 infection in permissive lymphocytes.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CXCR4,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ezrin,
http://linkedlifedata.com/resource/pubmed/chemical/gp120 protein, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/moesin,
http://linkedlifedata.com/resource/pubmed/chemical/radixin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
122
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
103-13
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pubmed:meshHeading |
pubmed-meshheading:19066282-Actins,
pubmed-meshheading:19066282-Animals,
pubmed-meshheading:19066282-Antigens, CD4,
pubmed-meshheading:19066282-Cell Line,
pubmed-meshheading:19066282-Cytoskeletal Proteins,
pubmed-meshheading:19066282-HIV Envelope Protein gp120,
pubmed-meshheading:19066282-HIV Infections,
pubmed-meshheading:19066282-HIV-1,
pubmed-meshheading:19066282-Humans,
pubmed-meshheading:19066282-Lymphocytes,
pubmed-meshheading:19066282-Membrane Proteins,
pubmed-meshheading:19066282-Microfilament Proteins,
pubmed-meshheading:19066282-Receptors, CXCR4,
pubmed-meshheading:19066282-Recombinant Fusion Proteins,
pubmed-meshheading:19066282-Virus Internalization
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pubmed:year |
2009
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pubmed:articleTitle |
Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes.
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pubmed:affiliation |
Servicio de Inmunología, Hospital Universitario de La Princesa, 28006 Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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