Porcine antibodies reveal novel non-neutralizing universal epitopes on FMDV and their overlaps with neutralization sites

文献类型： 外文期刊

第一作者： Sun, Ying

作者： Sun, Ying;Huang, Shenglin;Fan, Huiying;Sun, Ying;Li, Fengjuan;Huang, Shulun;Li, Pinghua;Zhao, Qiongqiong;Wang, Tao;Bao, Huifang;Fu, Yuanfang;Sun, Pu;Bai, Xingwen;Yuan, Hong;Ma, Xueqing;Zhao, Zhixun;Zhang, Jing;Wang, Jian;Li, Dong;Zhang, Qiang;Cao, Yimei;Li, Kun;Lu, Zengjun;Sun, Ying;Fan, Huiying;Sun, Ying;Fan, Huiying

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关键词： Foot and mouth disease virus; Monoclonal antibody; Non-neutralizing universal epitope; Free epitope

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：2.7； 五年影响因子：2.9 ）

ISSN： 0378-1135

年卷期： 2025 年 303 卷

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收录情况： SCI

摘要： Foot-and-mouth disease virus (FMDV) is highly infectious and lacks cross-protection among serotypes, with antibodies playing a key role in antiviral immunity. To map conserved epitopes on the FMDV surface that exhibit cross-serotype reactivity, we constructed a pig-specific B-cell receptor (BCR) library through single B-cell sorting and high-throughput sequencing. This led to the identification of 16 broadly reactive, non-neutralizing monoclonal antibodies (mAbs), with 10 targeting VP2 (pOTB-1, pOTB-10, pOTB-13, pOTB-33, pOTB-37, pONY-14, pONY-17, pONY-23, pONY-30, pONY-60) and 6 targeting VP3 (pOTB-6, pOTB-11, pOTB-22, pOTB-23, pONY3, pONY-59). Among these, a novel free linear epitope was identified at the C-terminus of VP2, recognized by pOTB-1, with the minimal recognition motif "KE." Key residues, T53 and W101, within the complementaritydetermining region (CDR) of the pOTB-1 heavy chain, interact with the carboxyl group of the C-terminal glutamate through hydrogen bonding, contributing to the free-form nature of the epitope. Competitive enzymelinked immunosorbent assays (cELISA) showed that most non-neutralizing antibodies (nNAbs) interfered with the binding of neutralizing antibodies B82 (site 2) and C4 (site 4), confirming the overlap between nonneutralizing and neutralizing epitopes. It has been confirmed that nNAbs mediate antiviral activity in vivo through various mechanisms, such as the formation of immune complexes. These findings reveal new epitopes on VP2 and VP3 and their spatial overlap with neutralizing sites, enhancing our understanding of FMDV immunogenicity and providing novel targets for vaccine and therapeutic development.

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