tetano
Editor, Senior Moderator
J Gen Virol. 2013 Aug 15. [Epub ahead of print]
H7N9 influenza viruses interact preferentially with α2,3-linked sialic acids and bind weakly to α2,6-linked sialic acids.
Ramos I, Krammer F, Hai R, Aguilera D, Bernal-Rubio D, Steel J, Garcia-Sastre A, Fernandez-Sesma A.
Source
Icahn School of Medicine at Mount Sinai;
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 hemagglutinin (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.
KEYWORDS:
H7N9, Influenza A virus, avian influenza, receptor binding, sialic acid
PMID:
23950563
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23950563
H7N9 influenza viruses interact preferentially with α2,3-linked sialic acids and bind weakly to α2,6-linked sialic acids.
Ramos I, Krammer F, Hai R, Aguilera D, Bernal-Rubio D, Steel J, Garcia-Sastre A, Fernandez-Sesma A.
Source
Icahn School of Medicine at Mount Sinai;
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 hemagglutinin (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.
KEYWORDS:
H7N9, Influenza A virus, avian influenza, receptor binding, sialic acid
PMID:
23950563
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23950563