Preferential recognition of avian-like receptors in human influenza A H7N9 viruses.
basic_science · Level V
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- Record sourced from PubMed, PMID 24311689.
- Also identified by DOI 10.1126/science.1243761 and PMC identifier 3954636.
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Abstract
The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu(226), a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to humanlike α2-6-linked receptors and strong preference for a subset of avian-like α2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.
Medical subject headings
- Hemagglutinin Glycoproteins, Influenza Virus
- Influenza A Virus, H7N9 Subtype
- Polysaccharides
- Receptors, Virus