The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus ... View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-02-06

AUTHORS

Min Gu, Qunhui Li, Ruyi Gao, Dongchang He, Yunpeng Xu, Haixu Xu, Lijun Xu, Xiaoquan Wang, Jiao Hu, Xiaowen Liu, Shunlin Hu, Daxin Peng, Xinan Jiao, Xiufan Liu

ABSTRACT

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. More... »

PAGES

7

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/s13567-017-0410-0

DOI

http://dx.doi.org/10.1186/s13567-017-0410-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1083687378

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28166830


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