Enabling the 'host jump': structural determinants of receptor-binding specificity in influenza A viruses

被引:220
作者
Shi, Yi [1 ,2 ]
Wu, Ying [2 ]
Zhang, Wei [2 ]
Qi, Jianxun [2 ]
Gao, George F. [1 ,2 ,3 ]
机构
[1] Chinese Acad Sci, Beijing Inst Life Sci, Res Network Immun & Hlth, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China
[3] Chinese Ctr Dis Control & Prevent China CDC, Off Director Gen, Beijing 102206, Peoples R China
基金
中国国家自然科学基金;
关键词
HEMAGGLUTININ MEMBRANE GLYCOPROTEIN; PANDEMIC INFLUENZA; H7N9; VIRUS; AIRBORNE TRANSMISSION; HUMAN INFECTIONS; CONFORMATIONAL-ANALYSIS; H3N2; VIRUSES; HUMAN-BEINGS; EVOLUTION; IDENTIFICATION;
D O I
10.1038/nrmicro3362
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The recent emergence of the H7N9 avian influenza A virus and its ability to infect humans emphasize the epidemic and pandemic potential of these viruses. Interspecies transmission is the result of many factors, which ultimately lead to a change in the host tropism of the virus. One of the key factors involved is a shift in the receptor-binding specificity of the virus, which is mostly determined by mutations in the viral haemagglutinin (HA). In this Review, we discuss recent crystallographic studies that provide molecular insights into HA-host receptor interactions that have enabled several influenza A virus subtypes to 'jump' from avian to human hosts.
引用
收藏
页码:822 / 831
页数:10
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