Influenza virus-glycan interactions.

Influenza virus-glycan interactions.
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DOI:
10.1016/j.coviro.2014.06.004
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发表时间:
2014-08
影响因子:
5.9
通讯作者:
Air, Gillian M.
Air, Gillian M.
中科院分区:
医学2区
文献类型:
--
作者:
Air, Gillian M.

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多年来,已知流感病毒通过其血凝素表面糖蛋白与宿主细胞表面的唾液酸(N-乙酰神经氨酸)结合,而禽流感病毒最常与唾液酸结合,α2-3与半乳糖相连,而大多数人类病毒以α2-6构型与唾液酸结合。在过去的几年里,由于在多糖结合分析、流感反向遗传系统和X射线结晶学方面的技术进步,关于这种结合的数据有了很大的增加。结果显示,在结合特异性方面出现了一些令人惊讶的变化,但似乎并不影响病毒感染宿主细胞的能力。
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 α2–3 to galactose while most human viruses bind to sialic acid in the α2–6 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.
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