PRRSV基因缺失片段dNsp2(87)的原核表达  

Prokaryotic Expression of PRRSV dNsp2(87) Gene

作　　者：亓传德[1,2] 吴发兴[2] 梁继望[2,3] 高许雷[2,4] 郑辉[2] 张志[2] 张燕霞[2] 刘爽[2] 王洪斌[1] 黄保续[2] 李晓成[2] 

机构地区：[1]东北农业大学,黑龙江哈尔滨150030 [2]中国动物卫生与流行病学中心,山东青岛266032 [3]新疆农业大学,新疆乌鲁木齐830052 [4]青岛农业大学,山东青岛266109

出　　处：《动物医学进展》2009年第5期1-4,共4页Progress In Veterinary Medicine

基　　金：“十一五”科技支撑计划项目(2007BAD86B05)

摘　　要：将质粒pUC57-dNsp2(87)经BamHⅠ和HindⅢ双酶切后,与经过相同酶切处理的pET-32a相连接,重组质粒转化大肠埃希菌BL21(DE3)进行表达,经SDS-PAGE电泳和Western blot检测,dNsp2(87)重组菌得到了有效表达,融合蛋白的分子质量约为23.5 ku,表达量可达菌体总蛋白的28.9%,重组蛋白能被PRRSV普通株阳性血清所识别,具有一定的生物学活性。The plasmid pUC57-dNsp2 （87） was double digested by BarnH Ⅰ , HindⅢ ,and was cloned into prokaryotic expression vector pET-32a,and the recombinant fusion proteins were expressed in Escherichia coli BL21. The Nsp2 gene were highly expressed and the total mass of fusion protein with 23.5 ku was confirmed by SDS-PAGE and Western-blot. The soluble recombinant protein also existed in the supernate and contained 30% of total somatic protein. The result of Western-blot bacterial that the recombinant protein could be recognized by the porcine antibodies against PRRSV, and it had better biological activity.

关 键 词：猪繁殖与呼吸综合征病毒 NSP2基因 原核表达 

分 类 号：S852.659.2[农业科学—基础兽医学]