Coloma M J, Morrison S L
Department of Microbiology and Molecular Genetics, University of California at Los Angeles 90095, USA.
Nat Biotechnol. 1997 Feb;15(2):159-63. doi: 10.1038/nbt0297-159.
We have produced novel bispecific antibodies by fusing the DNA encoding a single chain antibody (ScFv) after the C terminus (CH3-ScFv) or after the hinge (Hinge-ScFv) with an antibody of a different specificity. The fusion protein is expressed by gene transfection in the context of a murine variable region. Transfectomas secrete a homogeneous population of the recombinant antibody with two different specificities, one at the N terminus (anti-dextran) and one at the C terminus (anti-dansyl). The CH3-ScFv antibody, which maintains the constant region of human IgG3, has some of the associated effector functions such as long half-life and Fc receptor binding. The Hinge-ScFv antibody which lacks the CH2 and CH3 domains has no known effector functions.
我们通过将编码单链抗体（ScFv）的DNA在C末端（CH3-ScFv）或铰链区之后（铰链区-ScFv）与具有不同特异性的抗体融合，制备了新型双特异性抗体。融合蛋白通过基因转染在鼠可变区的背景下表达。转染瘤分泌具有两种不同特异性的重组抗体的同质群体，一种在N末端（抗葡聚糖），另一种在C末端（抗丹磺酰）。维持人IgG3恒定区的CH3-ScFv抗体具有一些相关的效应功能，如长半衰期和Fc受体结合。缺乏CH2和CH3结构域的铰链区-ScFv抗体没有已知的效应功能。
