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.
J Gen Virol. 2013 Nov;94(Pt 11):2417-2423. doi: 10.1099/vir.0.056184-0. Epub 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 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.
最近的人感染 H7N9 禽流感病毒已经引起了全球的关注。受体结合特异性对于病毒的致病性至关重要，但对于这种新兴病毒的研究还不够彻底。在这里，我们通过固相结合试验和基于流式细胞术的试验评估了两种人感染 H7N9 分离株（A/上海/1/13 和 A/安徽/1/13）血凝素（HA）的受体特异性。此外，我们还将其与来自几种人源和禽流感病毒的 HA 进行了比较。我们观察到，新型 H7 分离株的 HA 与α2,3-连接的唾液酸强烈相互作用。重要的是，它们也表现出与α2,6-连接的唾液酸的低结合水平，但明显高于其他禽源 H7。
