Literature detail

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

Irene Ramos¹ Florian Krammer¹ Rong Hai¹ Domingo Aguilera¹ Dabeiba Bernal-Rubio¹ John Steel² Adolfo García-Sastre^3,4,1 Ana Fernandez-Sesma^3,1

Affiliations 4 institutions

Department of Microbiology, Icahn School of Medicine at Mount Sinai, 1468 Madison Avenue New York, NY 10029, USA.
Department of Microbiology and Immunology, Emory University School of Medicine, GA 30322, USA.
Division of Infectious Diseases, Department of Medicine, Icahn School of Medicine at Mount Sinai, 1468 Madison Avenue New York, NY 10029, USA.
Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, 1468 Madison Avenue New York, NY 10029, USA.

PMID 23950563 2013 J Gen Virol eng ppublish

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Article

Publication summary

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.

Host-Pathogen Interactions Viral Tropism Animals Birds China Hemagglutinin Glycoproteins, Influenza Virus Humans Influenza A Virus, H7N9 Subtype Influenza in Birds Influenza, Human Receptors, Virus Sialic Acids

Structured evidence records

Evidence records

2 total

Receptor Usage 2 records

Receptor Usage Extraction confidence 1.00

Key finding

H7N9 influenza virus hemagglutinin binds preferentially to α2,3-linked sialic acid receptors and less strongly to α2,6-linked sialic acids.

Virus

Host

Location

Supporting text

We observed that the HAs from the novel H7 isolates strongly interacted with α2,3-linked sialic acids and also showed low levels of binding to α2,6-linked sialic acids.

Method: solid-phase binding assay; flow cytometry-based assay
Receptors: α2,3-linked sialic acid

Receptor Usage Extraction confidence 1.00

Key finding

H7N9 influenza virus hemagglutinin binds weakly to α2,6-linked sialic acid receptors compared with α2,3-linked sialic acids.

Virus

Host

Location

Supporting text

We observed that the HAs from the novel H7 isolates strongly interacted with α2,3-linked sialic acids and also showed low levels of binding to α2,6-linked sialic acids.

Method: solid-phase binding assay; flow cytometry-based assay
Receptors: α2,6-linked sialic acid

Citation context

References

36 references

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Evidence overview

Evidence 2

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Publication metadata

Journal: The Journal of general virology
Volume / Issue / Pages: 94 / Pt 11 / 2417-2423
ISSN: 1465-2099
Journal country: England
DOI: 10.1099/vir.0.056184-0