Title |
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
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Published in |
Veterinary Research, February 2017
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DOI | 10.1186/s13567-017-0410-0 |
Pubmed ID | |
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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 19 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Bachelor | 3 | 16% |
Student > Ph. D. Student | 3 | 16% |
Researcher | 3 | 16% |
Professor | 2 | 11% |
Other | 1 | 5% |
Other | 1 | 5% |
Unknown | 6 | 32% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 5 | 26% |
Biochemistry, Genetics and Molecular Biology | 3 | 16% |
Veterinary Science and Veterinary Medicine | 2 | 11% |
Immunology and Microbiology | 1 | 5% |
Unknown | 8 | 42% |