Abstract
The human immunodeficiency virus type 1 (HIV-1) 92UG046 Env protein, obtained from aCD4-independent HIV-1 primary isolate (Zerhouni et al., 2004), has the ability to initiate an infection in HeLa cells expressing CD4 when carrying the full-length (FL) Env, but uses CD8 molecules for receptor-mediated entry when carrying atruncated Env (CT84). To determine whether aspecific length or structure in the cytoplasmic tail (CT) is responsible for this alteration of tropism, we compared aseries of Env constructs with different CT truncations and the presence or absence of an amphipathic alpha- helical sequence. We found that truncated constructs containing the alpha-helical LLP-2 structure in their CT domains conferred aswitch from CD4 to CD8 tropism. The results support the conclusion that the structure of the CT domain can play an important role in determining receptor specificity.
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