Abstract
Fusion between cell and viral membranes constitutes a key step of the human immunodeficiency virus (HIV) infectious cycle. To this end, the fusogenic gp41 transmembrane Env subunit makes use of a collapsible ectodomain structure (the hairpin or six-helix bundle) that opens and closes and two membrane-transferring regions, the fusion peptide (FP) and the membrane-proximal external region (MPER), which ensure coupling of hairpin closure to apposition and fusion of cell and viral membranes. The isolation of natural products, short peptides and neutralizing IgG-s, that interact with FP and MPER, respectively, and block the viral infection, suggests that these conserved regions might represent alternative targets for clinical intervention. FP and MPER-derived peptides have been shown to be membrane-active. Here, it is discussed the potential use of these specimens in the development of HIV fusion inhibitors and immunogens.
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