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Structural, antigenic, and evolutionary characterizations of the envelope protein of newly emerging Duck Tembusu Virus.

Yu K, Sheng ZZ, Huang B, Ma X, Li Y, Yuan X, Qin Z, Wang D, Chakravarty S, Li F, Song M, Sun H - PLoS ONE (2013)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China ; Institute of Poultry Science, Shandong Academy of Agricultural Sciences, Jinan, China.

ABSTRACT
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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Related in: MedlinePlus

Modeled structure and domain architecture of envelope protein of FX-2012 strain.A) Cartoon scheme view of envelope protein structure. Sites containing amino acid changes were colored red and all these changes were listed in gray boxes. The side-chains of glycosylated residues were colored cyan. For illustration purpose, a β-D-Manp-(1-4)-β-D-GlcpNAc (colored magenta) was added to the glycosylation sites. B). Domain diagram of envelope protein. Domain boundaries were labeled (black) on top of the diagram. The two glycosylation sites were labeled magenta. Domain boundaries were predicted based on domain architecture of Japanese encephalitis virus. Domain colors: orange, domain I; green, domain II; blue, domain III.
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pone-0071319-g002: Modeled structure and domain architecture of envelope protein of FX-2012 strain.A) Cartoon scheme view of envelope protein structure. Sites containing amino acid changes were colored red and all these changes were listed in gray boxes. The side-chains of glycosylated residues were colored cyan. For illustration purpose, a β-D-Manp-(1-4)-β-D-GlcpNAc (colored magenta) was added to the glycosylation sites. B). Domain diagram of envelope protein. Domain boundaries were labeled (black) on top of the diagram. The two glycosylation sites were labeled magenta. Domain boundaries were predicted based on domain architecture of Japanese encephalitis virus. Domain colors: orange, domain I; green, domain II; blue, domain III.

Mentions: Multiple sequence alignment demonstrated that six E proteins shared approximately 98% identity (data not shown) and only thirteen positions of the E protein were shown to exhibit genetic polymorphisms (Figs. 2 and 3). To map structurally these mutations in E proteins of six viruses, we took advantage of the recently resolved crystal structure of the E protein of a Japanese Encephalitis virus (JEV) [10], a mosquito-borne zoonotic flavivirus, which has about 65% sequence identity with DTMUV E protein. The relatively high protein identity should allow us to establish a reliable model of DTMUV E protein that can be used to predict its important structural features.


Structural, antigenic, and evolutionary characterizations of the envelope protein of newly emerging Duck Tembusu Virus.

Yu K, Sheng ZZ, Huang B, Ma X, Li Y, Yuan X, Qin Z, Wang D, Chakravarty S, Li F, Song M, Sun H - PLoS ONE (2013)

Modeled structure and domain architecture of envelope protein of FX-2012 strain.A) Cartoon scheme view of envelope protein structure. Sites containing amino acid changes were colored red and all these changes were listed in gray boxes. The side-chains of glycosylated residues were colored cyan. For illustration purpose, a β-D-Manp-(1-4)-β-D-GlcpNAc (colored magenta) was added to the glycosylation sites. B). Domain diagram of envelope protein. Domain boundaries were labeled (black) on top of the diagram. The two glycosylation sites were labeled magenta. Domain boundaries were predicted based on domain architecture of Japanese encephalitis virus. Domain colors: orange, domain I; green, domain II; blue, domain III.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3750017&req=5

pone-0071319-g002: Modeled structure and domain architecture of envelope protein of FX-2012 strain.A) Cartoon scheme view of envelope protein structure. Sites containing amino acid changes were colored red and all these changes were listed in gray boxes. The side-chains of glycosylated residues were colored cyan. For illustration purpose, a β-D-Manp-(1-4)-β-D-GlcpNAc (colored magenta) was added to the glycosylation sites. B). Domain diagram of envelope protein. Domain boundaries were labeled (black) on top of the diagram. The two glycosylation sites were labeled magenta. Domain boundaries were predicted based on domain architecture of Japanese encephalitis virus. Domain colors: orange, domain I; green, domain II; blue, domain III.
Mentions: Multiple sequence alignment demonstrated that six E proteins shared approximately 98% identity (data not shown) and only thirteen positions of the E protein were shown to exhibit genetic polymorphisms (Figs. 2 and 3). To map structurally these mutations in E proteins of six viruses, we took advantage of the recently resolved crystal structure of the E protein of a Japanese Encephalitis virus (JEV) [10], a mosquito-borne zoonotic flavivirus, which has about 65% sequence identity with DTMUV E protein. The relatively high protein identity should allow us to establish a reliable model of DTMUV E protein that can be used to predict its important structural features.

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China ; Institute of Poultry Science, Shandong Academy of Agricultural Sciences, Jinan, China.

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus