An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level

被引:121
作者
Zhang, Wei [1 ,3 ]
Shi, Yi [1 ,2 ]
Lu, Xishan [4 ]
Shu, Yuelong [5 ]
Qi, Jianxun [1 ]
Gao, George F. [1 ,2 ,3 ,4 ,5 ]
机构
[1] Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Beijing Inst Life Sci, Res Network Immun & Hlth RNIH, Beijing 100101, Peoples R China
[3] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[4] China Agr Univ, Coll Vet Med, Beijing 100193, Peoples R China
[5] Chinese Ctr Dis Control & Prevent China CDC, Natl Inst Viral Dis Control & Prevent, Beijing 102206, Peoples R China
基金
中国国家自然科学基金;
关键词
A VIRUSES; RECEPTOR-BINDING; SWINE-ORIGIN;
D O I
10.1126/science.1236787
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Recent studies have identified several mutations in the hemagglutinin (HA) protein that allow the highly pathogenic avian H5N1 influenza A virus to transmit between mammals by airborne route. Here, we determined the complex structures of wild-type and mutant HAs derived from an Indonesia H5N1 virus bound to either avian or human receptor sialic acid analogs. A cis/trans conformational change in the glycosidic linkage of the receptor analog was observed, which explains how the H5N1 virus alters its receptor-binding preference. Furthermore, the mutant HA possessed low affinities for both avian and human receptors. Our findings provide a structural and biophysical basis for the H5N1 adaptation to acquire human, but maintain avian, receptor-binding properties.
引用
收藏
页码:1463 / 1467
页数:5
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