OmniVira

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

Min Wang1 Wei Zhang2 Jianxun Qi2 Fei Wang1 Jianfang Zhou3 Yuhai Bi2 Ying Wu2 Honglei Sun4 Jinhua Liu4 Chaobin Huang5 Xiangdong Li5 Jinghua Yan4 Yuelong Shu3 Yi Shi6 George F Gao7
Affiliations 7 institutions
  1. 1] College of Veterinary Medicine, China Agricultural University, Beijing 100193, 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. National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China.
  4. College of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
  5. State Key Laboratory of Agro-biotechnology, China Agricultural University, Beijing 100193, China.
  6. 1] CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China [2] Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China.
  7. 1] College of Veterinary Medicine, China Agricultural University, Beijing 100193, China [2] CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China [3] National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China [4] Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China [5] Office of Director-General, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China.
PMID25574798 DOI10.1038/ncomms6600 Year2015 Journal Nature communications Nat Commun Languageeng Statusepublish

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.

Supporting text Virus Host Location
Animals 1949 China 229 Crystallography, X-Ray 32 Ducks 81 Hemagglutinin Glycoproteins, Influenza Virus 180 Humans 1441 Influenza A Virus, H10N8 Subtype 4 Influenza A Virus, H7N9 Subtype 87 Influenza in Birds 341 Influenza, Human 286 Intestines 7 Molecular Sequence Data 160 Protein Binding 193 Protein Structure, Secondary 11 Protein Structure, Tertiary 29 Receptors, Virus 205 Recombinant Proteins 17 Surface Plasmon Resonance 4 Trachea 16

Evidence records

2 total
Functional Mechanism
2 records · 2 evidence types
Evidence type Receptor Usage
1 records
OVE1913 Receptor Usage
Key finding

The human isolate JD-H10N8 preferentially binds the avian receptor analogue, indicating avian-type receptor usage despite human isolation.

Virus
Influenza A virus H10N8
Host
birds Aves Experimental system human Homo sapiens Experimental system
Location
Not specified
Supporting text

Our results suggest that JD-H10N8 preferentially binds the avian receptor.

Method
receptor-binding assay | X-ray crystallography of HA–receptor complex
Receptors
avian receptor analogue
Evidence type Molecular Adaptation
1 records
OVE1915 Molecular Adaptation
Key finding

Residue R137 in the HA receptor-binding site of the H10N8 influenza virus mediates preferential binding to the avian-type receptor.

Virus
Influenza A virus H10N8
Host
Not specified
Location
Not specified
Supporting text

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.

Genes or proteins
HA
Receptors
avian receptor
Mutations
R137
Mechanism types
receptor binding | receptor usage | host-range expansion