Xu Yi-Gang, Cui Li-Chun, Ma Guang-Peng, Tang Li-Jie, Ge Jun-Wei, Xia Chun-Li, Qiao Xin-Yuan, Zhao Li-Li, Li Yi-Jing
Department of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, China.
Sheng Wu Gong Cheng Xue Bao. 2007 Mar;23(2):315-8.
Lactobacillus casei 393 was selected as a bacterial carrier for the expression of Porcine Parvovirus (PPV) protective antigen VP2 protein. The gene encoding PPV VP2 protein was cloned into the Lactobacillus casei surface expression vector pPG, and then the constructed recombinant vector pPG-VP2 was electrotransformed into Lactobacillus casei 393 generating the recombinant system pPG-VP2/L. casei393 expressing PPV VP2 protein. The recombinant strain was induced by 2% Lactose in MRS and about 74kD protein was detected with SDS-PAGE. The result of Western-blot indicated that the expressed protein possessed the antigenic specificity which could be recognized by mouse anti-PPV serum. The indirect immunofluorescent test showed that the expressed protein was secreted on the cell surface Lactobacillus casei.
干酪乳杆菌393被选为表达猪细小病毒(PPV)保护性抗原VP2蛋白的细菌载体。将编码PPV VP2蛋白的基因克隆到干酪乳杆菌表面表达载体pPG中,然后将构建好的重组载体pPG-VP2电转化到干酪乳杆菌393中,构建出表达PPV VP2蛋白的重组系统pPG-VP2/干酪乳杆菌393。重组菌株在MRS中用2%乳糖诱导,通过SDS-PAGE检测到约74kD的蛋白。Western-blot结果表明,表达的蛋白具有抗原特异性,能被小鼠抗PPV血清识别。间接免疫荧光试验表明,表达的蛋白分泌到干酪乳杆菌细胞表面。