Abstract
HIV-1 is capable of mimicking the ligand of integrin α(4)β(7) by displaying a tripeptide mimotope on the V2 region. Through this mimicry HIV can bind the α(4)β(7) integrin and get carried through the lymphocyte proliferation signaling pathway, cell-to-cell adhesion and can migrate to gut-associated lymphoid tissues. The same tripeptide motif was suggested to be the epicenter of neutralization in laboratory strains of HIV-1. In this study, we compared the α(4)β(7) binding sites of two HIV-1 subtypes prevalent in China and found that the tripeptide binding domain of α(4)β(7) was more diverse in subtype B' strains than in CRF07_BC.
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