Le Gall F, Kipriyanov S M, Moldenhauer G, Little M
Recombinant Antibody Research Group, German Cancer Research Center (DKFZ), Heidelberg, Germany.
FEBS Lett. 1999 Jun 18;453(1-2):164-8. doi: 10.1016/s0014-5793(99)00713-9.
Single chain variable fragments (scFv) of the murine monoclonal antibody HD37 specific to human B-cell antigen CD19 were constructed by joining the VH and VL domains with linkers of 18, 10, 1 and 0 residues. ScFv-18 formed monomers, dimers and small amounts of tetramers; scFv-10 formed dimers and small amounts of tetramers; scFv-1 formed exclusively tetramers; scFv-0 formed exclusively trimers. The affinities of the scFv-10 (diabody) and scFv-1 (tetrabody) were approximately 1.5- and 2.5-fold higher, respectively, than that of the scFv-0 (triabody). The tetrabody displayed a significantly prolonged association with cell-bound antigen (t1/2 cell surface retention at 37 degrees C of 26.6 min) compared to both the diabody (13.3 min) and triabody (6.7 min). This increase in avidity of the tetrabody combined with its larger size could prove to be particularly advantageous for imaging and the immunotherapy of B-cell malignancies.
通过用含18、10、1和0个残基的接头连接VH和VL结构域，构建了针对人B细胞抗原CD19的鼠单克隆抗体HD37的单链可变片段（scFv）。ScFv-18形成单体、二聚体和少量四聚体；scFv-10形成二聚体和少量四聚体；scFv-1仅形成四聚体；scFv-0仅形成三聚体。scFv-10（双抗体）和scFv-1（四抗体）的亲和力分别比scFv-0（三抗体）高约1.5倍和2.5倍。与双抗体（13.3分钟）和三抗体（6.7分钟）相比，四抗体与细胞结合抗原的结合时间显著延长（37℃下细胞表面保留半衰期为26.6分钟）。四抗体亲和力的增加及其更大的尺寸可能对B细胞恶性肿瘤的成像和免疫治疗特别有利。
