13-09-2013
An avian-origin human-infecting influenza (H7N9) virus has recently been identified in China. Here, we have
evaluated the viral hemagglutinin (HA) receptor binding properties from two human H7N9 isolates,
A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature Q226) and A/Anhui/1/2013 (AH-H7N9)
(containing the mammalian-signature L226). We found that SH-H7N9 HA preferentially binds the avian receptor
analog, whereas the AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9
mutant HA (L226Q) has dual receptor binding property, indicating that other amino acid substitutions contribute
to the receptor binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with
either avian or human receptor analogs show how the AH-H7N9 can bind human receptors, yet also retain the
avian receptor binding property. The research was conducted at the SSRF beamline 17U1.
Structural comparative analyses of the interactions of the AH-H7N9 HA, SH-H7N9 HA and AH-H7N9 mutant HA with either avian or human receptor analogs
Links: Yi Shi, Wei Zhang, Fei Wang, Jianxun Qi, Ying Wu, Hao Song, Feng Gao, Yuhai Bi, Yanfang Zhang, Zheng Fan, Chengfeng Qin, Honglei Sun, Jinhua Liu, Joel Haywood, Wenjun Liu, Weimin Gong, Dayan Wang, Yuelong Shu, Yu Wang, Jinghua Yan, George F. Gao, Science Express DOI: 10.1126/science.1242917
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