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Identification of a New Broadly Cross-reactive Epitope within Domain III of the Duck Tembusu Virus E Protein.


ABSTRACT: In 2010, a pathogenic flavivirus termed duck Tembusu virus (DTMUV) caused widespread outbreak of egg-drop syndrome in domesticated ducks in China. Although the glycoprotein E of DTMUV is an important structural component of the virus, the B-cell epitopes of this protein remains uncharacterized. Using phage display and mutagenesis, we identified a minimal B-cell epitope, 374EXE/DPPFG380, that mediates binding to a nonneutralizing monoclonal antibody. DTMUV-positive duck serum reacted with the epitope, and amino acid substitutions revealed the specific amino acids that are essential for antibody binding. Dot-blot assays of various flavivirus-positive sera indicated that EXE/DPPFG is a cross-reactive epitope in most flaviviruses, including Zika, West Nile, Yellow fever, dengue, and Japanese encephalitis viruses. These findings indicate that the epitope sequence is conserved among many strains of mosquito-borne flavivirus. Protein structure modeling revealed that the epitope is located in domain III of the DTMUV E protein. Together, these results provide new insights on the broad cross-reactivity of a B-cell binding site of the E protein of flaviviruses, which can be exploited as a diagnostic or therapeutic target for identifying, studying, or treating DTMUV and other flavivirus infections.

SUBMITTER: Li C 

PROVIDER: S-EPMC5099753 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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Identification of a New Broadly Cross-reactive Epitope within Domain III of the Duck Tembusu Virus E Protein.

Li Chenxi C   Bai Xiaofei X   Meng Runze R   Shaozhou Wulin W   Zhang Qingshan Q   Hua Ronghong R   Liu Jyung-Hurng JH   Liu Ming M   Zhang Yun Y  

Scientific reports 20161108


In 2010, a pathogenic flavivirus termed duck Tembusu virus (DTMUV) caused widespread outbreak of egg-drop syndrome in domesticated ducks in China. Although the glycoprotein E of DTMUV is an important structural component of the virus, the B-cell epitopes of this protein remains uncharacterized. Using phage display and mutagenesis, we identified a minimal B-cell epitope, <sup>374</sup>EXE/DPPFG<sup>380</sup>, that mediates binding to a nonneutralizing monoclonal antibody. DTMUV-positive duck seru  ...[more]

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