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Literature detail

Structural analysis of the hemagglutinin from the recent 2013 H7N9 influenza virus.

Hua Yang1 Paul J Carney Jessie C Chang Julie M Villanueva James Stevens
Affiliations 1 institutions
  1. Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.
PMID 24027325 2013 J Virol eng ppublish
PubMed DOI Browse context

Article

Publication summary

In March 2013, the Chinese Center for Disease Control and Prevention reported human infections with an H7N9 influenza virus, and by 20 July 2013, the numbers of laboratory-confirmed cases had climbed to 134, including 43 fatalities and 127 hospitalizations. The newly emerging H7N9 viruses constitute an obvious public health concern because of the apparent severity of this outbreak. Here we focus on the hemagglutinins (HAs) of these viruses and assess their receptor binding phenotype in relation to previous HAs studied. Glycan microarray and kinetic analyses of recombinant A(H7N9) HAs were performed to compare the receptor binding profile of wild-type receptor binding site variants at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized, and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs, suggesting that these viruses require further adaptation in order to adapt fully to humans.

Amino Acid Sequence Amino Acid Substitution Binding Sites Crystallization Crystallography, X-Ray Hemagglutinin Glycoproteins, Influenza Virus Humans Influenza A Virus, H7N9 Subtype Influenza, Human Molecular Sequence Data Mutation Polysaccharides Protein Binding Protein Conformation Recombinant Proteins Sequence Homology, Amino Acid

Structured evidence records

Evidence records

2 total
Molecular Adaptation 1 records
Molecular Adaptation Extraction confidence 0.95
Key finding

H7N9 hemagglutinin variants at position 217 show weak binding to human-type receptors, indicating partial molecular adaptation toward the human host.

Virus
IAV H7N9
Host
Not specified
Location
Not specified
Supporting text

Glycan microarray and kinetic analyses of recombinant A(H7N9) HAs were performed to compare the receptor binding profile of wild-type receptor binding site variants at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized, and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs, suggesting that these viruses require further adaptation in order to adapt fully to humans.

Genes or proteins
hemagglutinin; HA
Receptors
avian receptor; human receptor
Mutations
position 217
Mechanism types
receptor_binding; host_range_adaptation
Receptor Usage 1 records
Receptor Usage Extraction confidence 0.98
Key finding

Recombinant H7N9 hemagglutinin displays weak human-type receptor binding compared with avian-type preference, influenced by residue 217 in the receptor binding site.

Virus
IAV H7N9
Location
Not specified
Supporting text

Glycan microarray and kinetic analyses of recombinant A(H7N9) HAs were performed to compare the receptor binding profile of wild-type receptor binding site variants at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Results highlight a weak human receptor preference of the H7N9 HAs.

Method
glycan microarray; kinetic analysis; mutational study; structural characterization
Receptors
human-type receptor