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目的:研究乙型肝炎病毒(HBV)多表位基因的在原核载体中的克隆、游离表达及其产物的抗原性。方法:设计、并合成HBV多表位抗原基因BPT,克隆入原核表达载体pBAD/gIIIA,进而转化Top10大肠杆菌,阿拉伯糖诱导表达出HBV多表位抗原蛋白(B-BPT),并用Western blot方法初步检测该抗原蛋白的抗原性。结果:成功构建了原核表达载体pBAD/BPT,在大肠杆菌中表达出HBV多表位抗原蛋白B-BPT,Western blot检测显示该蛋白具有良好抗原性。结论:HBV多表位抗原基因的设计是成功的,其在大肠杆菌中表达的非融合蛋白具有良好的抗原性,可能是较理想的HBV治疗性疫苗候选物。
Objective: To study the cloning, free expression and antigenicity of Hepatitis B virus (HBV) multi-epitope gene in prokaryotic vector. Methods: The HBV multi-epitope antigen gene BPT was designed and synthesized and cloned into the prokaryotic expression vector pBAD / gIIIA, which was then transformed into E.coli Top10. The expression of HBV polyepitope antigen protein (B-BPT) The antigenicity of the antigen protein was initially tested. Results: The prokaryotic expression vector pBAD / BPT was constructed successfully, and HBV polyepitope antigen B-BPT was expressed in E. coli. Western blot showed that the protein has good antigenicity. CONCLUSION: The design of HBV multi-epitope antigen gene was successful. The non-fusion protein expressed in E. coli has good antigenicity and may be a better candidate for HBV therapeutic vaccine.