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Literature detail

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.
PMID 25574798 2015 Nat Commun eng epublish
PubMed DOI Browse context

Article

Publication summary

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.

Animals China Crystallography, X-Ray Ducks Hemagglutinin Glycoproteins, Influenza Virus Humans Influenza A Virus, H10N8 Subtype Influenza A Virus, H7N9 Subtype Influenza in Birds Influenza, Human Intestines Molecular Sequence Data Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Receptors, Virus Recombinant Proteins Surface Plasmon Resonance

Structured evidence records

Evidence records

4 total
Receptor Usage 2 records
Receptor Usage Extraction confidence 1.00
Key finding

The HA of H10N8 influenza virus preferentially binds avian receptor analogues, with residue R137 determining this specificity.

Virus
IAV H10N8
Location
Not specified
Supporting text

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.

Method
structural analysis; X-ray crystallography
Receptors
avian receptor
Receptor Usage Extraction confidence 1.00
Key finding

H10N8 showed weaker binding to human receptors than the H7N9 Anhui-1 isolate, indicating limited adaptation to human-type receptors.

Virus
IAV H10N8
Location
Not specified
Supporting text

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).

Method
structural comparison
Receptors
human receptor
Molecular Adaptation 1 records
Molecular Adaptation Extraction confidence 0.90
Key finding

Residue R137 in the haemagglutinin (HA) of H10N8 influenza virus determines its preferential binding to avian-type receptors, showing limited adaptation toward human receptors.

Virus
IAV 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; human receptor
Mutations
R137
Mechanism types
receptor_binding
Spillover Event 1 records
Spillover Event Extraction confidence 0.85
Key finding

H10N8 avian influenza virus caused human infections in China, indicating direct avian-to-human spillover.

Virus
IAV H10N8
Location
China China
Supporting text

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.

Study design
case report
Transmission direction
animal-to-human
Geographic raw
China
Country inferred
China