Identification of novel epitopes targeting non-structural protein 2 of PRRSV using monoclonal antibodies

文献类型： 外文期刊

第一作者： Bi, Caihong

作者： Bi, Caihong;Shao, Zengyu;Li, Jiangnan;Weng, Changjiang

作者机构：

关键词： Porcine reproductive and respiratory syndrome virus; Nonstructural protein 2; Monoclonal antibodies; Cryptic epitope

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

ISSN： 0175-7598

年卷期： 2019 年 103 卷 6 期

页码：

收录情况： SCI

摘要： Porcine reproductive and respiratory syndrome virus (PRRSV) is leading to huge losses in the swine industry worldwide. Its nonstructural protein 2 (Nsp2), with a cysteine protease domain (PL2), is crucial for virus replication and as a trigger to host innate immune regulation. In this study, three monoclonal antibodies (mAbs) to Nsp2, designated 4A12, 4G8, and 8H11, were generated. Subsequently, a sequence of recombinant peptides with partial overlap was utilized to determine the epitopes using these mAbs. We found three novel minimal linear Nsp2 B cell epitopes, (ELSDDSNRPV197)-E-188, (42)HLKRYSPPAE(51), and (54)CGWHCISA(61), which were identified by the antibodies 4A12, 4G8, and 8H11, respectively. Structure analysis indicates that (42)HLKRYSPPAE(51) and (ELSDDSNRPV197)-E-188 are located separately in hypervariable region 1 and hypervariable region 2 of Nsp2. Interestingly, (54)CGWHCISA(61) is located in the PL2 region, which is highly conserved in all arteriviruses, particularly at the expected conserved catalytic site at Cys54. Importantly, (54)CGWHCISA(61) is located in the inner region of the expected 3D structure of Nsp2, which reveals that the epitope is cryptic. These findings not only provide valuable insight for vaccine design and hold diagnostic potential for the identified epitopes, but also reveal a protective mechanism against variation under selective pressure in an important epitope.

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