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Literature detail

Amino Acid Substitutions That Affect Receptor Binding and Stability of the Hemagglutinin of Influenza A/H7N9 Virus.

Eefje J A Schrauwen1 Mathilde Richard2 David F Burke3 Guus F Rimmelzwaan1 Sander Herfst1 Ron A M Fouchier1
Affiliations 3 institutions
  1. Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam, The Netherlands.
  2. Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam, The Netherlands [email protected].
  3. Department of Zoology, University of Cambridge, Cambridge, United Kingdom.
PMID 26792744 2016 J Virol eng epublish
PubMed DOI Browse context

Article

Publication summary

Receptor-binding preference and stability of hemagglutinin have been implicated as crucial determinants of airborne transmission of influenza viruses. Here, amino acid substitutions previously identified to affect these traits were tested in the context of an A/H7N9 virus. Some combinations of substitutions, most notably G219S and K58I, resulted in relatively high affinity for α2,6-linked sialic acid receptor and acid and temperature stability. Thus, the hemagglutinin of the A/H7N9 virus may adopt traits associated with airborne transmission.

Amino Acid Substitution Virus Attachment Cell Line Hemagglutinin Glycoproteins, Influenza Virus Humans Influenza A Virus, H7N9 Subtype Mutant Proteins Sialic Acids Temperature

Structured evidence records

Evidence records

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

The G219S and K58I mutations in the hemagglutinin of influenza A/H7N9 virus increase receptor binding to α2,6-linked sialic acid and enhance protein stability, indicating molecular adaptation toward airborne transmission.

Virus
IAV H7N9
Host
Not specified
Location
Not specified
Supporting text

Some combinations of substitutions, most notably G219S and K58I, resulted in relatively high affinity for α2,6-linked sialic acid receptor and acid and temperature stability.

Genes or proteins
hemagglutinin
Receptors
α2,6-linked sialic acid receptor
Mutations
G219S; K58I
Mechanism types
receptor_binding; protein_stability; transmission_fitness
Receptor Usage 1 records
Receptor Usage Extraction confidence 0.95
Key finding

Amino acid substitutions G219S and K58I in Influenza A/H7N9 hemagglutinin increased binding affinity for the α2,6-linked sialic acid receptor, indicating altered receptor usage relevant to airborne transmission.

Virus
IAV H7N9
Host
Not specified
Location
Not specified
Supporting text

Some combinations of substitutions, most notably G219S and K58I, resulted in relatively high affinity for α2,6-linked sialic acid receptor and acid and temperature stability.

Receptors
α2,6-linked sialic acid receptor