Glycan array analysis of influenza H1N1 binding and release.
Glycan array analysis of influenza H1N1 binding and release.
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DOI：
10.3233/cbm-130376
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发表时间：
2014-01-01
期刊：
影响因子：
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通讯作者：
Air GM
中科院分区：
文献类型：
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作者：
Gulati S;Lasanajak Y;Smith DF;Cummings RD;Air GM
流感病毒通过附着在宿主细胞表面的唾液酸受体来启动感染。一段时间以来，人们已经认识到禽流感病毒通常与以α2-3构型连接到下一个糖的末端唾液酸结合，而人类病毒则显示出偏好α2-6连接的唾液酸。随着合成化学和合成相当复杂的聚糖的化学酶方法的发展，很明显，结合特异性超出了唾液酸，这引起了人们对开发聚糖试剂的极大兴趣，这些试剂可用作特定流感病毒的诊断工具，或识别易受某些流感病毒感染的细胞。在这里，我们描述了使用功能糖组学联盟聚糖阵列来研究流感血凝素和神经氨酸酶切割的结合特异性，以季节性和大流行性 H1N1 流感病毒为例，并将结果与使用其他阵列方法发布的数据进行比较。
Influenza viruses initiate infection by attaching to sialic acid receptors on the surface of host cells. It has been recognized for some time that avian influenza viruses usually bind to terminal sialic acid that is linked in the α2-3 configuration to the next sugar while human viruses show preference for α2-6 linked sialic acid. With developments in synthetic chemistry and chemo-enzymatic methods of synthesizing quite complex glycans, it has become clear that the binding specificity extends beyond the sialic acid, and this has led to considerable interest in developing glycan reagents that could be used either as a diagnostic tool for particular influenza viruses, or to identify cells that are susceptible to infection by certain influenza viruses. Here we describe the use of the Consortium for Functional Glycomics Glycan Array to investigate binding specificity of influenza hemagglutinin and cleavage by neuraminidase, using seasonal and pandemic H1N1 influenza viruses as examples, and compare the results with published data using other array methods.