Lin Tianwei, Wang Gengyan, Li Anzhang, Zhang Qian, Wu Caiming, Zhang Rongfu, Cai Qixu, Song Wenjun, Yuen Kwok-Yung
School of Life Sciences, Xiamen University, Xiamen, PR China.
Virology. 2009 Sep 15;392(1):73-81. doi: 10.1016/j.virol.2009.06.028. Epub 2009 Jul 22.
The interaction between hemagglutinin (HA) and receptors is a kernel in the study of evolution and host adaptation of H1N1 influenza A viruses. The notion that the avian HA is associated with preferential specificity for receptors with Siaalpha2,3Gal glycosidic linkage over those with Siaalpha2,6Gal linkage is not all consistent with the available data on H1N1 viruses. By x-ray crystallography, the HA structure of an avian H1N1 influenza A virus, as well as its complexes with the receptor analogs, was determined. The structures revealed no preferential binding of avian receptor analogs over that of the human analog, suggesting that the HA/receptor binding might not be as stringent as is commonly believed in determining the host receptor preference for some subtypes of influenza viruses, such as the H1N1 viruses. The structure also showed difference in glycosylation despite the preservation of related sequences, which may partly contribute to the difference between structures of human and avian origin.
血凝素（HA）与受体之间的相互作用是甲型H1N1流感病毒进化及宿主适应性研究的核心内容。禽源HA对具有Siaα2,3Gal糖苷键的受体的偏好性高于具有Siaα2,6Gal糖苷键的受体这一观点，并不完全与关于H1N1病毒的现有数据相符。通过X射线晶体学，确定了一株禽源甲型H1N1流感病毒的HA结构及其与受体类似物的复合物结构。这些结构显示，禽源受体类似物的结合并不比人源受体类似物更具偏好性，这表明在决定某些流感病毒亚型（如H1N1病毒）的宿主受体偏好方面，HA/受体结合可能不像通常认为的那样严格。该结构还显示，尽管相关序列得以保留，但糖基化存在差异，这可能部分导致了人源和禽源结构之间的差异。
