Peisajovich Sergio G, Shai Yechiel
Department of Biological Chemistry, The Weizmann Institute of Science, 76100, Rehovot, Israel.
Biochim Biophys Acta. 2003 Jul 11;1614(1):122-9. doi: 10.1016/s0005-2736(03)00170-6.
In recent years, the simple picture of a viral fusion protein interacting with the cell and/or viral membranes by means of only two localized segments (i.e. the fusion peptide and the transmembrane domain) has given way to a more complex picture in which multiple regions from the viral proteins interact with membranes. Indeed, possible roles in membrane binding and/or destabilization have been postulated for the N-terminal heptad repeats, pre-transmembrane segments, and other internal regions of fusion proteins from distant viruses (such as orthomyxo-, retro-, paramyxo-, or flaviviruses). This review focuses on the experimental evidence and functional models postulated so far about the role of these regions in the process of virus-induced membrane fusion.
近年来，病毒融合蛋白仅通过两个局部片段（即融合肽和跨膜结构域）与细胞和/或病毒膜相互作用的简单图景，已被更为复杂的图景所取代，在这一复杂图景中，病毒蛋白的多个区域与膜相互作用。事实上，对于来自远亲病毒（如正粘病毒、逆转录病毒、副粘病毒或黄病毒）的融合蛋白，其N端七肽重复序列、跨膜前片段及其他内部区域在膜结合和/或膜不稳定方面的可能作用已被提出。本综述聚焦于目前关于这些区域在病毒诱导的膜融合过程中作用的实验证据及功能模型。
