Laboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam, Academic Medical Center, University of Amsterdam, The Netherlands.
Curr Opin Virol. 2012 Feb;2(1):50-9. doi: 10.1016/j.coviro.2012.01.002. Epub 2012 Jan 28.
Entry of human immunodeficiency virus type 1 (HIV-1) into cells is mediated by attachment of the envelope glycoproteins, gp120 and gp41, to the CD4 receptor and a chemokine receptor (CCR5 or CXCR4) and subsequent fusion of viral and cellular membranes. Several steps of the entry process can be targeted by drugs. Receptor antagonists prevent virus attachment and fusion inhibitors block conformational changes that are required for membrane fusion. The T20 peptide (Enfuvirtide, Fuzeon), which is homologous to part of the gp41-encoded fusion machinery, is the only clinically approved fusion inhibitor, but over the last decade new generations of T20-like peptides have been developed with improved potency and stability, as well as fusion inhibitors that target alternative gp41 domains. Here, we will review the field of HIV-1 fusion inhibitors.
人类免疫缺陷病毒 1 型（HIV-1）进入细胞是由包膜糖蛋白 gp120 和 gp41 与 CD4 受体和趋化因子受体（CCR5 或 CXCR4）结合，随后病毒和细胞膜融合介导的。进入过程的几个步骤可以用药物靶向。受体拮抗剂阻止病毒附着，融合抑制剂阻断膜融合所需的构象变化。T20 肽（恩夫韦肽，Fuzeon）与 gp41 编码融合机制的一部分同源，是唯一临床批准的融合抑制剂，但在过去十年中，已经开发出了具有更高效力和稳定性的新一代 T20 样肽，以及针对替代 gp41 结构域的融合抑制剂。在这里，我们将回顾 HIV-1 融合抑制剂领域。
