数字农科院2.0

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

文献类型： 外文期刊

作者： Li, Chenxi;Bai, Xiaofei;Meng, Runze;Shaozhou, Wulin;Zhang, Qingshan;Hua, Ronghong;Liu, Ming;Zhang, Yun;Liu, Jyung-Hurng

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期刊名称： SCIENTIFIC REPORTS

ISSN： 2045-2322

年卷期： 2016 年 6 卷

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收录情况： SCI

摘要： 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, (EXE)-E-374/DPPFG(380), 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.

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