Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
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DOI：
10.1126/science.1124513
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发表时间：
2006-04-21
期刊：
影响因子：
56.9
通讯作者：
Wilson, IA
中科院分区：
文献类型：
--
作者：
Stevens, J;Blixt, O;Wilson, IA
血凝素(HA)的分辨率为2.9埃，来自高致病性的越南H5N1流感病毒，与1918年和其他人的H1HH更相关，而不是与1997年的鸭H5 HA有关。对这种Viet04 HA的葡聚糖微阵列分析显示，禽α2-3唾液酸受体具有结合偏好。引入可以转换H1血清型的突变只会增强或降低对禽类受体的亲和力。然而，能够转换禽类H2和H3的突变具有人类受体特异性，当插入到Viet04 H5 HA框架上时，允许与天然的人α2-6糖结合，这表明这种H5N1病毒在人类群体中站稳脚跟的路径。
The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAS than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian alpha 2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAS to human alpha 2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAS to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human alpha 2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.