The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs

详细信息    查看全文

• 作者：Min Gu ; Qunhui Li ; Ruyi Gao ; Dongchang He ; Yunpeng Xu ; Haixu Xu…
• 刊名：Veterinary Research
• 出版年：2018
• 出版时间：January 2018
• 年：0
• 卷：48
• 期：1
• 全文大小：1564KB
• 刊物主题：Veterinary Medicine/Veterinary Science; Virology; Microbiology; Immunology;
• 出版者：BioMed Central
• ISSN：1297-9716
• 卷排序：48

文摘

We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to α-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both α-2,3 (avian-type) and α-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.