期刊
NATURE IMMUNOLOGY
卷 9, 期 3, 页码 301-309出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ni1566
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- Intramural NIH HHS Funding Source: Medline
- NIAID NIH HHS [AI047734, AI058894] Funding Source: Medline
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 alpha(4)beta(7). We demonstrate here that the HIV-1 envelope protein gp120 bound to an activated form of alpha(4)beta(7). 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 alpha(4)beta(7). On CD4(+) T cells, engagement of alpha(4)beta(7) 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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