期刊
EMBO JOURNAL
卷 34, 期 12, 页码 1661-1673出版社
WILEY
DOI: 10.15252/embj.201590960
关键词
crystal structure; H6N1; hemagglutinin; receptor binding
资金
- China Ministry of Science and Technology National 973 Project [2011CB504703]
- National Natural Science Foundation of China (NSFC) [31402196]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB08020100]
- Intramural Special Grant for Influenza Virus Research from the Chinese Academy of Sciences [KJZD-EW-L09]
- China National Grand S&T Special Project [2014ZX10004002]
- NSFC Innovative Research Group [81321063]
- Excellent Young Scientist Program of the Chinese Academy of Sciences
The receptor-binding specificity of influenza A viruses is a major determinant for the host tropism of the virus, which enables inter-species transmission. In 2013, the first human case of infection with avian influenza A (H6N1) virus was reported in Taiwan. To gather evidence concerning the epidemic potential of H6 subtype viruses, we performed comprehensive analysis of receptor-binding properties of Taiwan-isolated H6 HAs from 1972 to 2013. We propose that the receptor-binding properties of Taiwan-isolated H6 HAs have undergone three major stages: initially avian receptor-binding preference, secondarily obtaining human receptor-binding capacity, and recently human receptor-binding preference, which has been confirmed by receptor-binding assessment of three representative virus isolates. Mutagenesis work revealed that E190V and G228S substitutions are important to acquire the human receptor-binding capacity, and the P186L substitution could reduce the binding to avian receptor. Further structural analysis revealed how the P186L substitution in the receptor-binding site of HA determines the receptor-binding preference change. We conclude that the human-infecting H6N1 evolved into a human receptor preference.
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