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Science DOI: 10.1126/science.1242917
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Structures and Receptor Binding of Hemagglutinins from Human-Infecting H7N9 Influenza Viruses
Yi Shi1,2,*,
Wei Zhang2,3,*,
Fei Wang2,4,*,
Jianxun Qi2,*,
Ying Wu2,*,
Hao Song2,3,
Feng Gao5,
Yuhai Bi2,
Yanfang Zhang6,
Zheng Fan7,
Chengfeng Qin8,
Honglei Sun4,
Jinhua Liu4,
Joel Haywood2,
Wenjun Liu2,
Weimin Gong5,
Dayan Wang9,
Yuelong Shu9,
Yu Wang10,
Jinghua Yan2,
George F. Gao1,2,3,4,6,9,10,?
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.
Report
Structures and Receptor Binding of Hemagglutinins from Human-Infecting H7N9 Influenza Viruses
Yi Shi1,2,*,
Wei Zhang2,3,*,
Fei Wang2,4,*,
Jianxun Qi2,*,
Ying Wu2,*,
Hao Song2,3,
Feng Gao5,
Yuhai Bi2,
Yanfang Zhang6,
Zheng Fan7,
Chengfeng Qin8,
Honglei Sun4,
Jinhua Liu4,
Joel Haywood2,
Wenjun Liu2,
Weimin Gong5,
Dayan Wang9,
Yuelong Shu9,
Yu Wang10,
Jinghua Yan2,
George F. Gao1,2,3,4,6,9,10,?
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.
