Peisajovich Sergio G, Shai Yechiel
Dept of Biological Chemistry, Weizmann Institute of Science, 76100, The Harold S. and Harriet B. Professorial Chair in Cancer Research., Rehovot, Israel.
Trends Biochem Sci. 2002 Apr;27(4):183-90. doi: 10.1016/s0968-0004(01)02050-3.
Infection by enveloped viruses requires fusion between the viral and cellular membranes, a process mediated by specific viral envelope glycoproteins. Information from studies with whole viruses, as well as protein dissection, has suggested that the fusion glycoprotein (F) from Paramyxoviridae, a family that includes major human pathogens, has two hydrophobic segments, termed fusion peptides. These peptides are directly responsible for the membrane fusion event. The recently determined three-dimensional structure of the pre-fusion conformation of the F protein supported these predictions and enabled the formulation of: (1) a detailed model for the initial interaction between F and the target membrane, (2) a new model for Paramyxovirus-induced membrane fusion that can be extended to other viral families, and (3) a novel strategy for developing better inhibitors of paramyxovirus infection.
包膜病毒的感染需要病毒膜与细胞膜融合,这一过程由特定的病毒包膜糖蛋白介导。对完整病毒以及蛋白质剖析的研究信息表明,副粘病毒科(该科包含主要的人类病原体)的融合糖蛋白(F)有两个疏水片段,称为融合肽。这些肽直接负责膜融合事件。最近确定的F蛋白预融合构象的三维结构支持了这些预测,并促成了以下几点:(1)F与靶膜初始相互作用的详细模型;(2)可扩展到其他病毒科的副粘病毒诱导膜融合的新模型;(3)开发更好的副粘病毒感染抑制剂的新策略。