Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin

被引:2173
作者
Skehel, JJ
Wiley, DC
机构
[1] Natl Inst Med Res, London NW7 1AA, England
[2] Harvard Univ, Howard Hughes Med Inst, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
关键词
antigenic variation; sialic acid; viral glycoprotein; glycoprotein conformations; binding-site evolution;
D O I
10.1146/annurev.biochem.69.1.531
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
Hemagglutinin (HA) is the receptor-binding and membrane fusion glycoprotein of influenza virus and the target for infectivity-neutralizing antibodies. The structures of three conformations of the ectodomain of the 1968 Hong Kong influenza virus HA have been determined by X-ray crystallography: the single-chain precursor, HA0; the metastable neutral-pH conformation found on virus, and the fusion pH-induced conformation. These structures provide a framework for designing and interpreting the results of experiments on the activity of HA in receptor binding, the generation of emerging and reemerging epidemics, and membrane fusion during viral entry.
引用
收藏
页码:531 / 569
页数:39
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