Binding of HIV-1 virions to α4β 7 expressing cells and impact of antagonizing α4β 7 on HIV-1 infection of primary CD4 + T cells
2014
Li, Chang | Jin, Wei | Du, Tao | Wu, Biao | Liu, Yalan | Shattock, Robin J. | Hu, Qinxue
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 α₄β₇in 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 α₄β₇can mediate the binding of whole HIV-1 virions to α₄β₇-expressing transfectants. We further constructed a cell line stably expressing α₄β₇and confirmed the α₄β₇-mediated HIV-1 binding. In primary lymphocytes with activated α₄β₇expression, we also observed significant virus binding which can be inhibited by an anti-α₄β₇antibody. Moreover, we investigated the impact of antagonizing α₄β₇on HIV-1 infection of primary CD4⁺T cells. In α₄β₇-activated CD4⁺T cells, both anti-α₄β₇antibodies and introduction of short-hairpin RNAs specifically targeting α₄β₇resulted in a decreased HIV-1 infection. Our findings indicate that α₄β₇may 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 α₄β₇in HIV-1 infection.
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