OmniVira

Literature detail

Avian and human receptor binding by hemagglutinins of influenza A viruses.

R J Russell1 D J Stevens L F Haire S J Gamblin J J Skehel
Affiliations 1 institutions
  1. MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA.
PMID 16575525 2006 Glycoconj J eng ppublish
PubMed DOI Browse context

Article

Publication summary

An understanding of the structural determinants and molecular mechanisms involved in influenza A virus binding to human cell receptors is central to the identification of viruses that pose a pandemic threat. To date, only a limited number of viruses are known to have infected humans even sporadically, and this has recently included the virulent H5 and H7 avian viruses. We compare here the 3-dimensional structures of H5 and H7 hemagglutinins (HA) complexed with avian and human receptor analogues, to highlight regions within the receptor binding domains of these HAs that might prevent strong binding to the human receptor.

Carbohydrate Sequence Crystallography, X-Ray Hemagglutinin Glycoproteins, Influenza Virus Humans Influenza A Virus, H5N1 Subtype Influenza A Virus, H7N7 Subtype Molecular Sequence Data Protein Conformation Receptors, Virus hemagglutinin, avian influenza A virus

Structured evidence records

Evidence records

4 total
Molecular Adaptation 2 records
Molecular Adaptation Extraction confidence 0.90
Key finding

Structural analysis of H5 and H7 influenza A virus hemagglutinins identified receptor-binding domain features that influence avian versus human receptor binding and thus cross-species adaptation potential.

Virus
IAV H5N1
Host
Not specified
Location
Not specified
Supporting text

We compare here the 3-dimensional structures of H5 and H7 hemagglutinins (HA) complexed with avian and human receptor analogues, to highlight regions within the receptor binding domains of these HAs that might prevent strong binding to the human receptor.

Genes or proteins
hemagglutinin
Receptors
avian receptor; human receptor
Mechanism types
receptor_binding
Molecular Adaptation Extraction confidence 0.90
Key finding

Structural comparison of H7 influenza A virus hemagglutinin with receptor analogues shows molecular determinants that restrict efficient human receptor binding, indicating partial adaptation barriers.

Virus
IAV H7N7
Host
Not specified
Location
Not specified
Supporting text

We compare here the 3-dimensional structures of H5 and H7 hemagglutinins (HA) complexed with avian and human receptor analogues, to highlight regions within the receptor binding domains of these HAs that might prevent strong binding to the human receptor.

Genes or proteins
hemagglutinin
Receptors
avian receptor; human receptor
Mechanism types
receptor_binding
Receptor Usage 2 records
Receptor Usage Extraction confidence 0.98
Key finding

H5 and H7 influenza A virus hemagglutinins display structural differences in their receptor-binding domains that limit strong binding to human cell receptor analogues.

Virus
IAV H5N1
Location
Not specified
Supporting text

We compare here the 3-dimensional structures of H5 and H7 hemagglutinins (HA) complexed with avian and human receptor analogues, to highlight regions within the receptor binding domains of these HAs that might prevent strong binding to the human receptor.

Method
structural analysis; X-ray crystallography
Receptors
human receptor
Receptor Usage Extraction confidence 0.98
Key finding

H5 and H7 influenza A virus hemagglutinins bind avian receptor analogues, with structural comparisons indicating avian-type receptor compatibility.

Virus
IAV H7N7
Host
Aves
Location
Not specified
Supporting text

We compare here the 3-dimensional structures of H5 and H7 hemagglutinins (HA) complexed with avian and human receptor analogues.

Method
structural analysis; X-ray crystallography
Receptors
avian receptor