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Published Online May 2 2013
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Science DOI: 10.1126/science.1236787
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An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level
Wei Zhang1,3,*,
Yi Shi1,2,*,
Xishan Lu4,
Yuelong Shu5,
Jianxun Qi1,
George F. Gao1,2,3,4,5,?
+ Author Affiliations
1CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
2Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China.
3University of Chinese Academy of Sciences, Beijing 100049, China.
4College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
5National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China.
↵?Corresponding author. E-mail: gaof@im.ac.cn (G.F.G.)
↵* These authors contributed equally to this work.
Abstract
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.
< Science Express Index
Read Full Text to Comment (0)
Science DOI: 10.1126/science.1236787
Report
An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level
Wei Zhang1,3,*,
Yi Shi1,2,*,
Xishan Lu4,
Yuelong Shu5,
Jianxun Qi1,
George F. Gao1,2,3,4,5,?
+ Author Affiliations
1CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
2Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China.
3University of Chinese Academy of Sciences, Beijing 100049, China.
4College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
5National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China.
↵?Corresponding author. E-mail: gaof@im.ac.cn (G.F.G.)
↵* These authors contributed equally to this work.
Abstract
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.
