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Inhibition of HIV-1 by Fusion Inhibitors

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The envelope glycoprotein complex (Env) is responsible for entry of the human immunodeficiency virus type 1 (HIV-1) into cells by mediating attachment to target cells and subsequent membrane fusion. Env consists of three gp120 subunits that mediate receptor and co-receptor attachment and three gp41 subunits responsible for membrane fusion. Several steps of the entry process can serve as drug targets. Receptor antagonists prevent attachment of gp120 to the receptor or co-receptor and conformational changes within gp41 required for membrane fusion can be inhibited by fusion inhibitors. Enfuvirtide (T20, Fuzeon) is a peptide based on the gp41 sequence and is the only approved fusion inhibitor. It prevents membrane fusion by competitively binding to gp41 and blocking the formation of the post-fusion structure. New generations of T20-like peptides have been developed with improved potency and stability. Besides T20 and derivatives, other fusion inhibitors have been developed that target different domains of gp41. Here we discuss the development of fusion inhibitors, their mode of action and their potential for incorporation in future drug regimens.

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Keywords: BMS-378806; Cyclic depsipeptides; DNA strand elongation; Enfuvirtide; Fusion Inhibitors; Fuzeon; Gag-Pol precursor; HIV; HIV-1; HXB2 isolate; Highly Active Antiretroviral Therapy (HAART); Maraviroc; N126K; PRO542; S138A; Saquinavir; Siliquaria spongia mirabilis; T20; TORO phase III study; VIRIP; abacavir; acquired immunodeficiency syndrome; antiviral peptide; coronaviridae; didanosine; enfuvirtide; envelope glycoprotein complex; fusion inhibitors; gp120; gp41; guanine; human immunodeficiency virus type 1; immunoglobulin; indinavir; integrase; non-nucleoside RT inhibitors; nucleoside analogue; resistance; reverse transcriptase (RT); ritonavir; stavudine; thymidine; vicriviroc; viral Gag; virus entry; zidovudine

Document Type: Research Article

Publication date: November 1, 2010

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