Abstract |
HIV-1 envelope glycoprotein is reported to interact with α4β7, an integrin mediating the homing of lymphocytes to gut-associated lymphoid tissue, but the significance of α4β7 in HIV-1 infection remains controversial. Here, using HIV-1 strain BaL, the gp120 of which was previously shown to be capable of interacting with α4β7, we demonstrated that α4β7 can mediate the binding of whole HIV-1 virions to α4β7-expressing transfectants. We further constructed a cell line stably expressing α4β7 and confirmed the α4β7-mediated HIV-1 binding. In primary lymphocytes with activated α4β7 expression, we also observed significant virus binding which can be inhibited by an anti-α4β7 antibody. Moreover, we investigated the impact of antagonizing α4β7 on HIV-1 infection of primary CD4(+) T cells. In α4β7-activated CD4(+) T cells, both anti-α4β7 antibodies and introduction of short-hairpin RNAs specifically targeting α4β7 resulted in a decreased HIV-1 infection. Our findings indicate that α4β7 may serve as an attachment factor at least for some HIV-1 strains. The established approach provides a promising means for the investigation of other viral strains to understand the potential roles of α4β7 in HIV-1 infection.
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Authors | Chang Li, Wei Jin, Tao Du, Biao Wu, Yalan Liu, Robin J Shattock, Qinxue Hu |
Journal | Virologica Sinica
(Virol Sin)
Vol. 29
Issue 6
Pg. 381-92
(Dec 2014)
ISSN: 1995-820X [Electronic] Netherlands |
PMID | 25527342
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Integrins
- Receptors, Virus
- integrin alpha4beta7
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Topics |
- CD4-Positive T-Lymphocytes
(metabolism, virology)
- Cells, Cultured
- HIV Infections
(genetics, metabolism, virology)
- HIV-1
(genetics, physiology)
- Humans
- Integrins
(genetics, metabolism)
- Protein Binding
- Receptors, Virus
(genetics, metabolism)
- Virion
(genetics, physiology)
- Virus Attachment
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