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Nat Rev Microbiol. 2014 Dec;12(12):822-31. doi: 10.1038/nrmicro3362. Epub 2014 Nov 10.

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

Author information

1
1] Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences (CAS), Beijing 100101, China. [2] CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
2
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
3
1] Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences (CAS), Beijing 100101, China. [2] CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China. [3] Office of Director-General, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China.

Abstract

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.

PMID:
25383601
DOI:
10.1038/nrmicro3362
[Indexed for MEDLINE]

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