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Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus

Since the first reported cases of ducks infected with a previously unknown flavivirus in eastern China in April 2010, the virus, provisionally designated Duck Tembusu Virus (DTMUV), has spread widely in domestic ducks in China and caused significant economic losses to poultry industry. In this study...

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Autores principales: Yu, Kexiang, Sheng, Zhi-Zhang, Huang, Bing, Ma, Xiuli, Li, Yufeng, Yuan, Xiaoyuan, Qin, Zhuoming, Wang, Dan, Chakravarty, Suvobrata, Li, Feng, Song, Minxun, Sun, Huaichang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3750017/
https://www.ncbi.nlm.nih.gov/pubmed/23990944
http://dx.doi.org/10.1371/journal.pone.0071319
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author Yu, Kexiang
Sheng, Zhi-Zhang
Huang, Bing
Ma, Xiuli
Li, Yufeng
Yuan, Xiaoyuan
Qin, Zhuoming
Wang, Dan
Chakravarty, Suvobrata
Li, Feng
Song, Minxun
Sun, Huaichang
author_facet Yu, Kexiang
Sheng, Zhi-Zhang
Huang, Bing
Ma, Xiuli
Li, Yufeng
Yuan, Xiaoyuan
Qin, Zhuoming
Wang, Dan
Chakravarty, Suvobrata
Li, Feng
Song, Minxun
Sun, Huaichang
author_sort Yu, Kexiang
collection PubMed
description Since the first reported cases of ducks infected with a previously unknown flavivirus in eastern China in April 2010, the virus, provisionally designated Duck Tembusu Virus (DTMUV), has spread widely in domestic ducks in China and caused significant economic losses to poultry industry. In this study, we examined in detail structural, antigenic, and evolutionary properties of envelope (E) proteins of six DTMUV isolates spanning 2010–2012, each being isolated from individual farms with different geographical locations where disease outbreaks were documented. Structural analysis showed that E proteins of DTMUV and its closely related flavivirus (Japanese Encephalitis Virus) shared a conserved array of predicted functional domains and motifs. Among the six DTMUV strains, mutations were observed only at thirteen amino acid positions across three separate domains of the E protein. Interestingly, these genetic polymorphisms resulted in no detectable change in viral neutralization properties as demonstrated in a serum neutralization assay. Furthermore, phylogenetic analysis of the nucleotide sequences of the E proteins showed that viruses evolved into two distinct genotypes, termed as DTMUV.I and DTMUV.II, with II emerging as the dominant genotype. New findings described here shall give insights into the antigenicity and evolution of this new pathogen and provide guidance for further functional studies of the E protein for which no effective vaccine has yet been developed.
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spelling pubmed-37500172013-08-29 Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus Yu, Kexiang Sheng, Zhi-Zhang Huang, Bing Ma, Xiuli Li, Yufeng Yuan, Xiaoyuan Qin, Zhuoming Wang, Dan Chakravarty, Suvobrata Li, Feng Song, Minxun Sun, Huaichang PLoS One Research Article Since the first reported cases of ducks infected with a previously unknown flavivirus in eastern China in April 2010, the virus, provisionally designated Duck Tembusu Virus (DTMUV), has spread widely in domestic ducks in China and caused significant economic losses to poultry industry. In this study, we examined in detail structural, antigenic, and evolutionary properties of envelope (E) proteins of six DTMUV isolates spanning 2010–2012, each being isolated from individual farms with different geographical locations where disease outbreaks were documented. Structural analysis showed that E proteins of DTMUV and its closely related flavivirus (Japanese Encephalitis Virus) shared a conserved array of predicted functional domains and motifs. Among the six DTMUV strains, mutations were observed only at thirteen amino acid positions across three separate domains of the E protein. Interestingly, these genetic polymorphisms resulted in no detectable change in viral neutralization properties as demonstrated in a serum neutralization assay. Furthermore, phylogenetic analysis of the nucleotide sequences of the E proteins showed that viruses evolved into two distinct genotypes, termed as DTMUV.I and DTMUV.II, with II emerging as the dominant genotype. New findings described here shall give insights into the antigenicity and evolution of this new pathogen and provide guidance for further functional studies of the E protein for which no effective vaccine has yet been developed. Public Library of Science 2013-08-22 /pmc/articles/PMC3750017/ /pubmed/23990944 http://dx.doi.org/10.1371/journal.pone.0071319 Text en © 2013 Yu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Yu, Kexiang
Sheng, Zhi-Zhang
Huang, Bing
Ma, Xiuli
Li, Yufeng
Yuan, Xiaoyuan
Qin, Zhuoming
Wang, Dan
Chakravarty, Suvobrata
Li, Feng
Song, Minxun
Sun, Huaichang
Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus
title Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus
title_full Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus
title_fullStr Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus
title_full_unstemmed Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus
title_short Structural, Antigenic, and Evolutionary Characterizations of the Envelope Protein of Newly Emerging Duck Tembusu Virus
title_sort structural, antigenic, and evolutionary characterizations of the envelope protein of newly emerging duck tembusu virus
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3750017/
https://www.ncbi.nlm.nih.gov/pubmed/23990944
http://dx.doi.org/10.1371/journal.pone.0071319
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