Structural basis for preferential avian receptor binding by the human-infecting H10N8 avian influenza virus

Min Wang, Wei Zhang, Jianxun Qi, Fei Wang, Jianfang Zhou, Yuhai Bi, Ying Wu, Honglei Sun, Jinhua Liu, Chaobin Huang, Xiangdong Li, Jinghua Yan, Yuelong Shu, Yi Shi and George F. Gao ()
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Min Wang: College of Veterinary Medicine, China Agricultural University
Wei Zhang: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
Jianxun Qi: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
Fei Wang: College of Veterinary Medicine, China Agricultural University
Jianfang Zhou: National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC)
Yuhai Bi: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
Ying Wu: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
Honglei Sun: College of Veterinary Medicine, China Agricultural University
Jinhua Liu: College of Veterinary Medicine, China Agricultural University
Chaobin Huang: State Key Laboratory of Agro-biotechnology, China Agricultural University
Xiangdong Li: State Key Laboratory of Agro-biotechnology, China Agricultural University
Jinghua Yan: College of Veterinary Medicine, China Agricultural University
Yuelong Shu: National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC)
Yi Shi: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
George F. Gao: College of Veterinary Medicine, China Agricultural University

Nature Communications, 2015, vol. 6, issue 1, 1-7

Abstract: Abstract Since December 2013, at least three cases of human infections with H10N8 avian influenza virus have been reported in China, two of them being fatal. To investigate the epidemic potential of H10N8 viruses, we examined the receptor binding property of the first human isolate, A/Jiangxi-Donghu/346/2013 (JD-H10N8), and determined the structures of its haemagglutinin (HA) in complex with both avian and human receptor analogues. Our results suggest that JD-H10N8 preferentially binds the avian receptor and that residue R137—localized within the receptor-binding site of HA—plays a key role in this preferential binding. Compared with the H7N9 avian influenza viruses, JD-H10N8 did not exhibit the enhanced binding to human receptors observed with the prevalent H7N9 virus isolate Anhui-1, but resembled the receptor binding activity of the early-outbreak H7N9 isolate (Shanghai-1). We conclude that the H10N8 virus is a typical avian influenza virus.

Date: 2015
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DOI: 10.1038/ncomms6600

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