Viral fusion proteins: multiple regions contribute to membrane fusion

被引:83
作者
Peisajovich, SG [1 ]
Shai, Y [1 ]
机构
[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2003年 / 1614卷 / 01期
关键词
viral entry; fusion peptide; protein dissection;
D O I
10.1016/S0005-2736(03)00170-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:122 / 129
页数:8
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