为了开发塞尼卡谷病毒（Seneca Valley virus，SVV）的检测试剂盒，克隆3ABC基因进行原核表达和纯化，并将纯化的3ABC蛋白免疫大鼠，制备抗3ABC蛋白的多克隆抗体。通过Western blot鉴定制备的多克隆抗体与表达的3ABC蛋白的特异性识别能力，通过ELISA测定多克隆抗体的效价。结果显示，3ABC基因在大肠杆菌中大量表达，且主要以包涵体形式表达，重组蛋白分子质量约为55 ku，经纯化后得到单一条带。免疫大鼠制备的多克隆抗体效价大于1∶64 000，且与表达的3ABC重组蛋白发生特异性反应。综上，在大肠杆菌中成功表达了SVV 3ABC蛋白，且表达的重组蛋白具有免疫原性。

In order to develop detective kits of Seneca Valley virus(SVV),the 3ABC gene was expressed in E.coli BL21(DE3) and purified,and the purified protein was used to immunize rats.The polyclonal antibody against 3ABC protein was prepared,and its titer was determined by ELISA.Specific reaction was identified between the prepared polyclonal antibody and the expressed 3ABC protein by Western blot.The results showed that the 3ABC gene could be expressed in E.coli(mainly in inclusion body).Molecular weight of the recombinant 3ABC protein was about 55 ku.SDS-PAGE analysis showed that there was a clear single target band for the purified 3ABC protein.The titer of the polyclonal antibody was detected to be higher than 1∶64 000 by indirect ELISA.The polyclonal antibody could specifically recognize the recombinant 3ABC protein.In conclusion,SVV 3ABC gene could be successfully expressed in E.coli and the recombinant 3ABC protein had good immunogenicity.