Hemagglutinin Receptor Specificity and Structural Analyses of Respiratory Droplet-Transmissible H5N1 Viruses
Hemagglutinin Receptor Specificity and Structural Analyses of Respiratory Droplet-Transmissible H5N1 Viruses
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DOI：
10.1128/jvi.02690-13
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发表时间：
2014-01-01
影响因子：
5.4
通讯作者：
Paulson, James C.
中科院分区：
文献类型：
--
作者：
de Vries, Robert P.;Zhu, Xueyong;Paulson, James C.
两种雪貂适应的H5 N1病毒能够通过呼吸道飞沫传播，已报告在血凝素受体结合位点和茎域发生突变。聚糖微阵列分析显示，两种病毒都表现出与“人型”α 2-6唾液酸糖苷结合的强烈转变，但在精细特异性方面存在显著差异。晶体结构分析进一步表明，茎突变不会引起受体结合口袋的明显扰动，与其对血凝素稳定性的影响一致，而不影响受体特异性。
Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to "human-type" alpha 2-6 sialosides but with notable differences in fine specificity. Crystal structure analysis further shows that the stalk mutation causes no obvious perturbation of the receptor-binding pocket, consistent with its impact on hemagglutinin stability without affecting receptor specificity.