Identification of three novel B cell epitopes targeting the bovine viral diarrhea virus NS3 protein for use in diagnostics and vaccine development

文献类型： 外文期刊

第一作者： Zhang, Yuanyuan

作者： Zhang, Yuanyuan;Du, Enqi;Zhang, Yuanyuan;Cheng, Jing;Liu, Wenxiao;Zhou, Linyi;Yang, Chun;Li, Yongqing;Zhang, Yuanyuan;Cheng, Jing;Liu, Wenxiao;Zhou, Linyi;Yang, Chun;Li, Yongqing;Zhang, Yuanyuan;Cheng, Jing;Liu, Wenxiao;Zhou, Linyi;Yang, Chun;Li, Yongqing;Du, Enqi;Yang, Chun;Li, Yongqing

作者机构：

关键词： Bovine viral diarrhea virus; NS3 protein; Monoclonal antibody; Epitope mapping; Alanine scanning; Replication inhibition; Diagnostic method

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2025 年 308 卷

页码：

收录情况： SCI

摘要： Bovine viral diarrhea virus (BVDV) is a major pathogen in cattle herds, widely distributed across the globe and causing significant economic losses to the cattle industry. The nonstructural protein NS3 is highly conserved across BVDV subtypes. Identifying and screening epitopes on BVDV NS3 is crucial for developing sensitive, specific diagnostic tools. In this study, we obtained three monoclonal antibodies (mAbs) against the NS3 protein: 2F7, 3E8, and 4D6. Three novel linear B-cell epitope 100EYG102, 384FLDIA388, and 100EYGVK104 were identified through reactions of these mAbs with a series of continuous-truncated peptides and one of which a rare threeamino-acid B-cell epitope 100EYG102. Critical amino acid residues were further characterized through alanine (A)-scanning mutagenesis. Sequence alignment revealed that 100EYG102 and 100EYGVK104 were highly conserved allowing mAbs 2F7 and 4D6 to recognize all BVDV subtypes. In contrast, 384FLDIA388 was specifically conserved in BVDV-1 and BVDV-3 enabling 3E8 mAb to differential diagnosis BVDV-2 from other BVDV subtypes. Additionally, preliminary diagnostic assays for BVDV were established by western blotting and peptide-based blocking ELISA. Moreover, we observed that these mAbs could inhibit the replication of BVDV. These findings provide a theoretical foundation for developing of therapeutic strategies for nonstructural protein and accurate diagnostic procedures.

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