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Fine mapping of conserved neutralizing epitopes within the VP2 protein of Senecavirus A using monoclonal antibodies

文献类型： 外文期刊

作者： Zou, Wanying 1 ; Li, Qingmei 2 ; Li, Chunzhen 1 ; Meng, Zekun 1 ; Sun, Yaning 2 ; Yang, Suzhen 2 ; Guo, Junqing 2 ; Zhang, Gaiping 1 ;

作者机构： 1.Henan Agr Univ, Coll Vet Med, Int Joint Res Ctr Natl Anim Immunol, Zhengzhou 450046, Peoples R China

2.Henan Acad Agr Sci, Inst Anim Hlth, Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

3.Longhu Lab, Zhengzhou 450046, Peoples R China

4.Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Peoples R China

5.Peking Univ, Sch Adv Agr Sci, Beijing 100871, Peoples R China

关键词： Senecavirus A; VP2 protein; Monoclonal antibodies; Neutralizing epitope

期刊名称：VIROLOGY （ 影响因子：2.4； 五年影响因子：2.5 ）

ISSN： 0042-6822

年卷期： 2025 年 606 卷

页码：

收录情况： SCI

摘要： Senecavirus A (SVA) is an emerging swine virus with global prevalence that causes vesicular disease (VD), clinically similar to foot-and-mouth disease (FMD), posing a significant concern for the swine industry. The capsid protein VP2 is a structural protein of SVA, playing a critical role in mediating viral entry into host cells and inducing the production of neutralizing antibodies. In this study, the SVA VP2 protein was expressed using the Bac-to-Bac baculovirus expression system. Six monoclonal antibodies (mAbs) targeting SVA VP2 protein were then produced by immunizing mice with the recombinant VP2 protein, named as 1A1F6, 3D5F9, 3E2C3, 5A6F5, 5F12D10 and 7H10C3, respectively. Among these, mAbs 1A1F6 and 7H10C3 exhibited neutralizing activity against SVA in vitro with IC50 values of 0.64 mu g/mL and 1.21 mu g/mL, respectively. Finally, a linear B-cell neutralizing epitope of 151SLQELN156 on the SVA VP2 protein was identified by determining the reactivity of the neutralizing mAbs with the truncated VP2 protein followed by peptide scanning. Peptide mutation analysis showed that the residues Ser151, Leu152, Leu155, and Asn156 within the epitope were essential for antibody binding. Multiple sequence alignment indicated that this epitope is highly conserved across various SVA strains. These findings provide a foundation for further studies on SVA and offer valuable support for the design of SVA vaccines.

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