Redpath S, Michaelsen T E, Sandlie I, Clark M R
Department of Pathology, University of Cambridge, UK.
Hum Immunol. 1998 Nov;59(11):720-7. doi: 10.1016/s0198-8859(98)00075-5.
Interactions between human IgG with human FcgammaRI and FcgammaRIIa (R131) were studied to investigate the role of the hinge region of IgG3 and IgG1 in the binding of the antibodies to FcgammaR. It was found that a hinge deletion mutant of IgG3 (IgG3 m15) was reduced in its ability to bind to FcgammaRI and FcgammaRIIa but was more potent at activating ADCC by activated lymphocytes (FcgammaRIIIa-mediated), compared to the wild-type version of IgG3. The human IgG1 allotype G1m(a,z) was more efficient at binding to FcgammaRI than the two IgG3 antibodies tested. The IgG1 and IgG3 wild type antibodies were better able to bind to FcgammaRII than the hinge deletion mutant version of IgG3. The data suggest a role for the hinge region in influencing FcgammaR mediated effector functions in IgG3.
研究了人IgG与人FcγRI和FcγRIIa（R131）之间的相互作用，以探讨IgG3和IgG1铰链区在抗体与FcγR结合中的作用。结果发现，IgG3的铰链缺失突变体（IgG3 m15）与FcγRI和FcγRIIa结合的能力降低，但与野生型IgG3相比，在激活活化淋巴细胞介导的ADCC（FcγRIIIa介导）方面更有效。人IgG1同种异型G1m(a,z)与FcγRI结合的效率高于所测试的两种IgG3抗体。与IgG3的铰链缺失突变体相比，IgG1和IgG3野生型抗体与FcγRII的结合能力更强。数据表明铰链区在影响IgG3中FcγR介导的效应功能方面发挥作用。
