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

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 a...

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Autores principales: Gu, Min, Li, Qunhui, Gao, Ruyi, He, Dongchang, Xu, Yunpeng, Xu, Haixu, Xu, Lijun, Wang, Xiaoquan, Hu, Jiao, Liu, Xiaowen, Hu, Shunlin, Peng, Daxin, Jiao, Xinan, Liu, Xiufan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Short Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5294818/
https://www.ncbi.nlm.nih.gov/pubmed/28166830
http://dx.doi.org/10.1186/s13567-017-0410-0
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author Gu, Min
Li, Qunhui
Gao, Ruyi
He, Dongchang
Xu, Yunpeng
Xu, Haixu
Xu, Lijun
Wang, Xiaoquan
Hu, Jiao
Liu, Xiaowen
Hu, Shunlin
Peng, Daxin
Jiao, Xinan
Liu, Xiufan
author_facet Gu, Min
Li, Qunhui
Gao, Ruyi
He, Dongchang
Xu, Yunpeng
Xu, Haixu
Xu, Lijun
Wang, Xiaoquan
Hu, Jiao
Liu, Xiaowen
Hu, Shunlin
Peng, Daxin
Jiao, Xinan
Liu, Xiufan
author_sort Gu, Min
collection PubMed
description 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-017-0410-0) contains supplementary material, which is available to authorized users.
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spelling pubmed-52948182017-02-09 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 Gu, Min Li, Qunhui Gao, Ruyi He, Dongchang Xu, Yunpeng Xu, Haixu Xu, Lijun Wang, Xiaoquan Hu, Jiao Liu, Xiaowen Hu, Shunlin Peng, Daxin Jiao, Xinan Liu, Xiufan Vet Res Short Report 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-017-0410-0) contains supplementary material, which is available to authorized users. BioMed Central 2017-02-06 2017 /pmc/articles/PMC5294818/ /pubmed/28166830 http://dx.doi.org/10.1186/s13567-017-0410-0 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Short Report
Gu, Min
Li, Qunhui
Gao, Ruyi
He, Dongchang
Xu, Yunpeng
Xu, Haixu
Xu, Lijun
Wang, Xiaoquan
Hu, Jiao
Liu, Xiaowen
Hu, Shunlin
Peng, Daxin
Jiao, Xinan
Liu, Xiufan
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
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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort t160a hemagglutinin substitution affects not only receptor binding property but also transmissibility of h5n1 clade 2.3.4 avian influenza virus in guinea pigs
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5294818/
https://www.ncbi.nlm.nih.gov/pubmed/28166830
http://dx.doi.org/10.1186/s13567-017-0410-0
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