抗（MUC1粘蛋白）重组双抗体的制备与表征
Production and characterization of an anti-(MUC1 mucin) recombinant diabody.
作者信息
Denton G, Brady K, Lo B K, Murray A, Graves C R, Hughes O D, Tendler S J, Laughton C A, Price M R
机构信息
Cancer Research Laboratories, School of Pharmaceutical Sciences, University of Nottingham, University Park, UK.
出版信息
Cancer Immunol Immunother. 1999 Apr;48(1):29-38. doi: 10.1007/s002620050545.
A recombinant diabody fragment based on the anti-MUC1 monoclonal antibody, C595 has been produced in a bacterial expression system. Substitution of a 7-amino-acid linker sequence (Gly6Ser) for the original single-chain (sc)Fv 15-amino-acid linker (Gly4-Ser)3, using polymerase-chain-reaction-based strategies, forces variable heavy (V(H)) and light (V(L)) domains to pair with complementary domains on neighbouring scFv molecules, forming a scFv dimer (diabody). This recombinant protein shows similar binding characteristics to the parental C595 monoclonal antibody. The ability to bind to MUC1 mucin on carcinoma cell surfaces will allow its potential as a diagnostic and therapeutic reagent of clinical utility to be investigated.
一种基于抗MUC1单克隆抗体C595的重组双抗体片段已在细菌表达系统中产生。使用基于聚合酶链反应的策略，将7个氨基酸的接头序列（Gly6Ser）替换原始单链（sc）Fv的15个氨基酸接头（Gly4-Ser）3，促使重链可变区（V(H)）和轻链可变区（V(L)）与相邻scFv分子上的互补结构域配对，形成scFv二聚体（双抗体）。这种重组蛋白表现出与亲本C595单克隆抗体相似的结合特性。其与癌细胞表面MUC1粘蛋白结合的能力将有助于研究其作为具有临床应用价值的诊断和治疗试剂的潜力。
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