摘要用聚合酶链反应（PCR）从人源噬菌体抗体库中筛选出的宋内痢疾杆菌脂多糖抗独特型抗体基因扩增了重链可变区基因，将其克隆到表达载体pGEX2T内，转化大肠杆菌DH5α，获得高效表达，表达量占全菌总蛋白质的40%左右，表达出的融合蛋白分子量为4×10 4，以包涵体形式存在。将此融合蛋白包涵体变性、复性后通过谷胱甘肽亲和层析柱（GST Sepharose 4B柱），得到电泳纯的融合蛋白，每升培养物能纯化到20～30mg融合蛋白。Western blot分析证明宋内痢疾杆菌脂多糖鼠单抗（5B12）能特异地结合到分子量4×10 4的融合蛋白的带上。ELISA试验显示融合蛋白与宋内痢疾杆菌脂多糖单抗（5B12）有结合活性，而与无关单抗，如大肠杆菌J5株单抗（E3）、炭疽杆菌单抗（F8 FA）、鼠伤寒沙门氏菌单抗（M467）及乙肝病毒单抗（M11）不结合。

abstractsThe gene of heavy chain variable region (Hv) of human anti-idiotypic antibody against Shigella sonnei biopanned from phage antibody libraries was amplified by PCR. The Hv gene was cloned into an expression vector pGEX2T and transformed into E. coli DH5α. Clones harboring plasmid pGEX-Hv produced a 40 kDa of fusion protein in E. coli at a level of 40% of the total cellular protein. After denatured and renatured, the fusion protein from inclusion body was purified to be electrophoretically pure by Glutathione Sepharose 4B affinity chromatography with yields of between 20~30μg/ml of culture. Western blot analysis of the fusion protein showed that 5B12 McAb (anti-LPS of Shigella sonnei) specifically bound to the 40kDa band. The expressed products in E. coli demonstrated significant binding activity with 5B12McAb (anti-LPS of Shigella sonnei) and non-binding activity with E3 McAb (anti-E. coli J5), F8FA McAb (anti- B. anthracis) ,M467 McAb (anti- S. typhimurium) and M11 McAb (anti-HBs) in ELISA.