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:
- Emergence of a genetically distinct cluster of influenza A(H3N2) viruses within subclade J.2.2 associated with hospitalization during the 2024-2025 season in Auvergne-Rh?ne-Alpes, France 8 hours ago
- Interaction between DEAD-box RNA helicase 10 and influenza PB1 polymerase selectively regulates influenza A virus replication 8 hours ago
- Genetic Diversity of Clade 2.3.4.4b H5Nx High Pathogenicity Avian Influenza Viruses Detected in Korea During the 2025-2026 Winter Season and Pathogenicity of H5N1 and H5N9 Viruses 8 hours ago
- Update and optimization of a multiplex RT-qPCR assay to overcome diagnostic failure in emerging influenza A(H3N2) subclades J.2 and K (Peru, 2024-2026) 8 hours ago
- Antigenic and structural analysis of the influenza hemagglutinin lateral patch 8 hours ago
[Go Top] [Close Window]


