RAMOS I, Krammer F, Hai R, Aguilera D, et al. H7N9 influenza viruses interact preferentially with α2,3-linked sialic acids and bind weakly to α2,6-linked sialic acids.. J Gen Virol. 2013 Aug 15
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
See Also:
Latest articles in those days:
- Phylogenetic Analysis of Highly Pathogenic Avian Influenza H7 Viruses in Australia and New Zealand Suggests Local Viral Evolution 15 hours ago
- AI-Powered Identification of Human Cell Surface Protein Interactors of the Hemagglutinin Glycoprotein of High-Pandemic-Risk H5N1 Influenza Virus 15 hours ago
- Seasonal Influenza Vaccination Uptake and Intentions Among Nursing Students in Hong Kong 15 hours ago
- Intranasal Mosaic H1N1 Live Attenuated Influenza Vaccine Elicits Broad Cross-Reactive Immunity and Protection Against Group 1 and 2 Influenza A Viruses 15 hours ago
- Changing Landscape of Pediatric Influenza in Northern Mexico: A Comparative Clinical and Virological Study 15 hours ago
[Go Top] [Close Window]


