Identification of B-Cell Epitopes Located on the Surface of the S1 Protein of Infectious Bronchitis Virus M41 Strains

文献类型： 外文期刊

第一作者： Gao, Zichen

作者： Gao, Zichen;Hu, Jianing;Cai, Yiqin;Liu, Ye;Yin, Guihu;Guo, Xinyu;Wang, Ruiying;Zhong, Meng;Feng, Xiuli;Gao, Zichen;Hu, Jianing;Cai, Yiqin;Liu, Ye;Yin, Guihu;Guo, Xinyu;Wang, Ruiying;Zhong, Meng;Feng, Xiuli;Liu, Qingtao

作者机构：

关键词： avian infectious bronchitis virus; monoclonal antibody; S1 antigenic determinants; B-cell epitope; peptide scanning; overlapping fragments; prokaryotic expression

期刊名称：VIRUSES-BASEL （ 影响因子：3.5； 五年影响因子：3.7 ）

ISSN：

年卷期： 2025 年 17 卷 4 期

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收录情况： SCI

摘要： Avian infectious bronchitis is caused by the avian infectious bronchitis virus (IBV), which poses a significant threat to the poultry industry and public health. The S1 protein of IBV plays a crucial role in the process of the virus invading host cells. To investigate the significant antigenic targets within the S1 protein, in this study, the truncated S1 sequence of the IBV M41 strain was cloned with approximately 660 bp and expressed. After purification and renaturation, the recombinant S1 protein was immunized into BALB/c mice. Then, following fusion with lymphocytes and SP2/0 cells, the indirect ELISA and Western blotting techniques were employed to screen hybridoma cell lines secreting monoclonal antibodies (mAbs) targeting the S1 protein. Antigenic epitopes of the mAbs were identified using truncated S1 fragments and peptide scanning. The results indicated that three hybridoma cell lines stably secreting S1 protein-specific mAbs (2A10, 4E9, and 5E12) were screened. The heavy chains of the three mAbs were IgG1, and all three mAbs contained kappa light chains. The identified minimal B-cell epitopes were 132RVSAMK137 and 142FYNLTV147. Homology analysis showed these both epitopes were conserved across IBV subtypes and located on the S1 protein surface. The conserved beta-sheet epitope 132RVSAMK137 and the surface-exposed, flexible loop epitope 142FYNLTV147 serve as ideal targets for broad-spectrum diagnostics and early infection detection, respectively. These epitopes provide unique structural advantages for antibody binding, enabling the design of multivalent epitope vaccines or the development of immunomodulatory drugs. They offer novel biomaterials and targets for antibody-based drug development and rapid detection methods for avian infectious bronchitis virus (IBV), holding significant potential for the prevention and control of IBV.

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