Abstract：According to the antigenic analysis of duck plague virus (DPV) gB protein , one pair of primers were designed, with which the gene fragment coding the high antigenic domain of DPV N-terminal gB protein was amplified from the DPV genome. The segment was cloned into pET32a vector to obtain the recombinant pET-gB1 plasmid. The recombinant plasmid was transformed into E. coli BL21, and expressed in very high level as inclusion body after induced with IPTG. The expressived product analyzed by SDS- PAGE and Western blotting. The result indicated that the fusion protein (pET-gB1) has specific antigenicity. The inclusion body was solubilized in urea (8mol/L) . The purified protein was obtained by use of His•Bind affinity chromatography. Mice were inoculated transcutaneous three times at a two-weeks interval with fusion protein and normal saline. To evaluate the prophylaxtic efficacy of fusion protein , Titers of antibodies was detected by ELISA and proliferation of lymphocytes were determined by MTT. The results indicated that fusion protein could elicit specific humoral immune and cellular immune responses.
潘华奇 曹瑞兵 王楠 刘丽 刘磊 胡江春 陈溥言. 鸭瘟病毒gB蛋白N端抗原域的高效表达及其免疫特性初步研究[J]. , 2008, 16(5): 0-.
Hua-Qi Pan Nan Wang Lei Liu Jiang-Chun Hu . Prokaryotic expression of N-terminal antigenic domain of duck plague virus gB. , 2008, 16(5): 0-.
