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J Gen Virol. 2013 Nov;94(Pt 11):2417-23. doi: 10.1099/vir.0.056184-0. Epub 2013 Aug 15.

H7N9 influenza viruses interact preferentially with α2,3-linked sialic acids and bind weakly to α2,6-linked sialic acids.

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  • 1Department of Microbiology, Icahn School of Medicine at Mount Sinai, 1468 Madison Avenue New York, NY 10029, USA.

Abstract

The recent human outbreak of H7N9 avian influenza A virus has caused worldwide concerns. Receptor binding specificity is critical for viral pathogenicity, and still not thoroughly studied for this emerging virus. Here, we evaluated the receptor specificity of the haemagglutinin (HA) of two human H7N9 isolates (A/Shanghai/1/13 and A/Anhui/1/13) through a solid-phase binding assay and a flow cytometry-based assay. In addition, we compared it with those from several HAs from human and avian influenza viruses. We observed that the HAs from the novel H7 isolates strongly interacted with α2,3-linked sialic acids. Importantly, they also showed low levels of binding to α2,6-linked sialic acids, but significantly higher than other avian H7s.

PMID:
23950563
[PubMed - indexed for MEDLINE]
PMCID:
PMC3809111
[Available on 2014/11/1]
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