文献类型: 外文期刊
作者: Meng, Liang 1 ; Tian, Xiao-Xiao 1 ; Xiang, Xu-Yan 1 ; Qi, Xin-Yu 1 ; Zhou, Han-Rong 1 ; Xiao, Pei-Yu 1 ; An, Tong-Qing 1 ; Meng, Fan-Dan 1 ; Wang, Hai-Wei 1 ;
作者机构: 1.Chinese Acad Agr Sci, Harbin Vet Res Inst, State Key Lab Anim Dis Control & Prevent, Harbin 150069, Peoples R China
2.Heilongjiang Prov Key Lab Vet Immunol, Harbin 150069, Peoples R China
关键词:
3A protein; epitope; monoclonal antibody;
期刊名称:TRANSBOUNDARY AND EMERGING DISEASES ( 影响因子:3.0; 五年影响因子:3.4 )
ISSN: 1865-1674
年卷期: 2025 年 2025 卷 1 期
页码:
收录情况: SCI
摘要: Senecavirus A (SVA), an emerging pathogen causing vesicular disease in pigs, poses a significant threat to the swine industry. The nonstructural protein 3A of SVA plays an essential role in the viral replication cycle. In this study, we immunized mice with the prepared SVA 3A protein and produced two monoclonal antibodies (mAbs), AG4 and 2F3. MAb AG4 showed specific reactivity to the linear and conformational 3A protein, whereas mAb 2F3 did not recognize linear epitope of 3A protein. Through truncated 3A protein expression and alanine mutation analysis, we identified 1SPNEND6 as the minimal motif recognized by mAb AG4, with Asn3 being the critical residue. Additionally, we demonstrated that mAb 2F3 failed to recognize the SVA mutant with the 75QEETEG80 deletion in 3A protein, indicating that 75QEETEG80 constitutes an essential epitope for mAb 2F3. Further deletion analysis confirmed that 75QE76 is the crucial motif for mAb 2F3 recognition. Moreover, we found that 1SPNEND6 and 75QEETEG80 are highly conserved among different SVA strains and are exposed on the surface of the 3A protein. This study contributes to further explore the function of SVA 3A protein and develop diagnostic tools for SVA detection.
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