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The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
被引:24
|作者:
Velkov, Tony
[1
]
机构:
[1] Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
基金:
澳大利亚国家健康与医学研究理事会;
关键词:
influenza B;
hemagglutinin;
receptor specificity;
NS1;
PROTEIN;
EVOLUTIONARY PATTERN;
GLYCOSYLATION SITE;
STRUCTURAL BASIS;
A VIRUSES;
RECOGNITION;
GANGLIOSIDES;
GROWTH;
CONSERVATION;
SUBSTITUTION;
D O I:
10.1002/jmr.2293
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:
The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl-glycans, usually linked to galactose in either 2,6 or 2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg-adapted variants. Overall, the review serves as an up-to-date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA. Copyright (c) 2013 John Wiley & Sons, Ltd.
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页码:439 / 449
页数:11
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