Influenza virus-glycan interactions

被引：39

作者：

Air, Gillian M. ^{[1
]}

机构：

[1] Univ Oklahoma, Hlth Sci Ctr, Dept Biochem & Mol Biol, Oklahoma City, OK 73104 USA

来源：

CURRENT OPINION IN VIROLOGY | 2014年 / 7卷

关键词：

RECEPTOR-BINDING SPECIFICITY; NEURAMINIDASE; TRANSMISSION; FERRETS; H7N9; SUBSTITUTION; MICROARRAYS; VARIANTS; ARRAY;

D O I：

10.1016/j.coviro.2014.06.004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

It has been known for many years that influenza viruses bind by their hemagglutinin surface glycoprotein to sialic acid (N-acetylneuraminic acid) on the surface of the host cell, and that avian viruses most commonly bind to sialic acid linked alpha 2-3 to galactose while most human viruses bind to sialic acid in the alpha 2-6 configuration. Over the past few years there has been a large increase in data on this binding due to technological advances in glycan binding assays, reverse genetic systems for influenza and in X-ray crystallography. The results show some surprising changes in binding specificity that do not appear to affect the ability of the virus to infect host cells.

引用

页码：128 / 133

页数：6

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