Hombach A, Pohl C, Heuser C, Sircar R, Koch D, Diehl V, Abken H
Klinik 1 für Innere Medizin, Labor Tumorgenetik, Universität zu Köln, Germany.
Scand J Immunol. 1998 Nov;48(5):497-501.
Recombinant single chain antibody fragments (scFv) derived by combining immunoglobulin VL and VH regions provide valuable antibody-like reagents. A number of them are shown to have retained the antigen specificity of the parental monoclonal antibody (MoAb). Little is known about the idiotypic profile of scFv fragments compared with that of the parental MoAb. To address this question we analysed the idiotypic profile of a scFv that was derived by phage-display techniques from the anti-CD30 MoAb HRS3. We assayed (i) binding of HRS3-scFv to recombinant CD30-Fc antigen and to four different anti-idiotypic MoAbs defining at least three different idiotopes on HRS3, and (ii) cross-competition with the parental MoAb HRS3 and the closely related anti-CD30 MoAb HRS4. The assays revealed that the HRS3-scFv fragment exhibits the same specificity for both CD30 antigen and the tested anti-idiotypic MoAbs compared with the parental MoAb demonstrating that the recombinant scFv fragment has retained the complete idiotope of the parental MoAb.
通过组合免疫球蛋白VL和VH区域获得的重组单链抗体片段（scFv）提供了有价值的类抗体试剂。其中许多已显示保留了亲本单克隆抗体（MoAb）的抗原特异性。与亲本MoAb相比，关于scFv片段的独特型谱了解甚少。为了解决这个问题，我们分析了通过噬菌体展示技术从抗CD30 MoAb HRS3获得的scFv的独特型谱。我们检测了（i）HRS3-scFv与重组CD30-Fc抗原以及与定义HRS3上至少三种不同独特位的四种不同抗独特型MoAb的结合，以及（ii）与亲本MoAb HRS3和密切相关的抗CD30 MoAb HRS4的交叉竞争。检测结果显示，与亲本MoAb相比，HRS3-scFv片段对CD30抗原和测试的抗独特型MoAb均表现出相同的特异性，表明重组scFv片段保留了亲本MoAb的完整独特位。
