Tao M H, Canfield S M, Morrison S L
Department of Microbiology, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
J Exp Med. 1991 Apr 1;173(4):1025-8. doi: 10.1084/jem.173.4.1025.
Using domain switch chimeric antibodies, we confirm the important role of CH2 in complement activation. In addition, we demonstrate that the structures responsible for the differential ability of human IgG1 and IgG4 to activate complement are located at the COOH-terminal part (from residue 292 to 340) of the CH2 domain. The amino acids in CH2 that might be involved in complement interaction are discussed. While CH3 contributes to efficient complement activation, CH3 from IgG2 and CH3 IgG3 are equally effective.
通过使用结构域切换嵌合抗体,我们证实了CH2在补体激活中的重要作用。此外,我们证明了负责人类IgG1和IgG4激活补体能力差异的结构位于CH2结构域的COOH末端部分(从第292位残基到340位残基)。讨论了CH2中可能参与补体相互作用的氨基酸。虽然CH3有助于高效补体激活,但来自IgG2的CH3和IgG3的CH3同样有效。