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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

Serum neutralization properties of six DTMUV isolates.Antisera generated from ducks inoculated with BZ-10 and FX-12, respectively, were selected to test the effects of E protein mutations on neutralization sensitivity of each of six viruses as described in Materials and Methods. Each experiment was run in duplicate and repeated twice. The serum neutralizing titers were determined by the minimal serum dilution that inhibited chicken embryo death. The titers were the mean values of two independent experiments.
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pone-0071319-g004: Serum neutralization properties of six DTMUV isolates.Antisera generated from ducks inoculated with BZ-10 and FX-12, respectively, were selected to test the effects of E protein mutations on neutralization sensitivity of each of six viruses as described in Materials and Methods. Each experiment was run in duplicate and repeated twice. The serum neutralizing titers were determined by the minimal serum dilution that inhibited chicken embryo death. The titers were the mean values of two independent experiments.

Mentions: Antisera generated against BZ-10 an FX-12 neutralized corresponding viruses with high titers 1∶1259 and 1∶1422, respectively. As summarized in Fig. 4, other four viruses were also effectively neutralized by these two antisera with antibody titters ranging from 1∶1024 to 1∶1422, indicating that there was no discernible difference in neutralizing activity among six examined viruses. Thus, results of our experiments suggested that the observed genetic polymorphisms over the past two years in the E protein had no effects on neutralizing properties of these DTMUV strains.


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)

Serum neutralization properties of six DTMUV isolates.Antisera generated from ducks inoculated with BZ-10 and FX-12, respectively, were selected to test the effects of E protein mutations on neutralization sensitivity of each of six viruses as described in Materials and Methods. Each experiment was run in duplicate and repeated twice. The serum neutralizing titers were determined by the minimal serum dilution that inhibited chicken embryo death. The titers were the mean values of two independent experiments.
© Copyright Policy
Related In: Results  -  Collection

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

pone-0071319-g004: Serum neutralization properties of six DTMUV isolates.Antisera generated from ducks inoculated with BZ-10 and FX-12, respectively, were selected to test the effects of E protein mutations on neutralization sensitivity of each of six viruses as described in Materials and Methods. Each experiment was run in duplicate and repeated twice. The serum neutralizing titers were determined by the minimal serum dilution that inhibited chicken embryo death. The titers were the mean values of two independent experiments.
Mentions: Antisera generated against BZ-10 an FX-12 neutralized corresponding viruses with high titers 1∶1259 and 1∶1422, respectively. As summarized in Fig. 4, other four viruses were also effectively neutralized by these two antisera with antibody titters ranging from 1∶1024 to 1∶1422, indicating that there was no discernible difference in neutralizing activity among six examined viruses. Thus, results of our experiments suggested that the observed genetic polymorphisms over the past two years in the E protein had no effects on neutralizing properties of these DTMUV strains.

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