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rdf:type |
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lifeskim:mentions |
umls-concept:C0017278,
umls-concept:C0019704,
umls-concept:C0026724,
umls-concept:C0039194,
umls-concept:C0205100,
umls-concept:C0597357,
umls-concept:C0648695,
umls-concept:C0699819,
umls-concept:C1145667,
umls-concept:C1422036,
umls-concept:C1710082
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pubmed:issue |
3
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pubmed:dateCreated |
2008-2-20
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pubmed:abstractText |
Infection with human immunodeficiency virus 1 (HIV-1) results in the dissemination of virus to gut-associated lymphoid tissue. Subsequently, HIV-1 mediates massive depletion of gut CD4+ T cells, which contributes to HIV-1-induced immune dysfunction. The migration of lymphocytes to gut-associated lymphoid tissue is mediated by integrin alpha4beta7. We demonstrate here that the HIV-1 envelope protein gp120 bound to an activated form of alpha4beta7. This interaction was mediated by a tripeptide in the V2 loop of gp120, a peptide motif that mimics structures presented by the natural ligands of alpha4beta7. On CD4+ T cells, engagement of alpha4beta7 by gp120 resulted in rapid activation of LFA-1, the central integrin involved in the establishment of virological synapses, which facilitate efficient cell-to-cell spreading of HIV-1.
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pubmed:grant |
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pubmed:commentsCorrections |
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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 |
Mar
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pubmed:issn |
1529-2916
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pubmed:author |
pubmed-author:ArthosJamesJ,
pubmed-author:CensoplanoNinaN,
pubmed-author:ChungEvaE,
pubmed-author:CicalaClaudiaC,
pubmed-author:ConradThomas PTP,
pubmed-author:CruzCatherine CCC,
pubmed-author:FauciAnthony SAS,
pubmed-author:GoodeDiana JDJ,
pubmed-author:GopaulRavindraR,
pubmed-author:KottililShyamS,
pubmed-author:LempickiRichard ARA,
pubmed-author:MacleodKatilynK,
pubmed-author:MartinelliElenaE,
pubmed-author:McLaughlinSherryS,
pubmed-author:McNallyJonathanJ,
pubmed-author:PascuccioMassimilianoM,
pubmed-author:ReitanoKristin NKN,
pubmed-author:Van RykDonaldD,
pubmed-author:VeenstraTimothy DTD,
pubmed-author:WeiDanlanD,
pubmed-author:XiaoZhenZ
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pubmed:issnType |
Electronic
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
301-9
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pubmed:meshHeading |
pubmed-meshheading:18264102-CD4-Positive T-Lymphocytes,
pubmed-meshheading:18264102-Cell Movement,
pubmed-meshheading:18264102-Cells, Cultured,
pubmed-meshheading:18264102-Fibroblasts,
pubmed-meshheading:18264102-Flow Cytometry,
pubmed-meshheading:18264102-HIV Envelope Protein gp120,
pubmed-meshheading:18264102-HIV Infections,
pubmed-meshheading:18264102-HIV-1,
pubmed-meshheading:18264102-Humans,
pubmed-meshheading:18264102-Integrins,
pubmed-meshheading:18264102-Intestinal Mucosa,
pubmed-meshheading:18264102-Killer Cells, Natural,
pubmed-meshheading:18264102-Ligands,
pubmed-meshheading:18264102-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:18264102-Protein Binding,
pubmed-meshheading:18264102-Signal Transduction
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pubmed:year |
2008
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pubmed:articleTitle |
HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells.
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pubmed:affiliation |
Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. jarthos@niaid.nih.gov
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural,
Research Support, N.I.H., Intramural
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