Nik Jaafar M I, Lowe J A, Ling N R, Jefferis R
Mol Immunol. 1984 Feb;21(2):137-43. doi: 10.1016/0161-5890(84)90128-7.
Epitopes recognised by a panel of 23 anti-Fc gamma monoclonal antibodies (McAbs) have been subdivided into three groups each having a distinct topographical distribution. One group of mutually inhibitory McAbs are reactive with epitopes expressed on the fy "surface" of the C gamma 2 domain. A second group recognises epitopes in the region of arginine 355 of the C gamma 3 domain whilst the third group recognises epitopes expressed in the inter C gamma 2/C gamma 3 domain region--as evidenced by inhibition of Staphylococcus aureus protein A binding. An antibody of the latter group reactive with IgG1, 2, 4 and IgG3m(15,16) proteins but not IgG3m(5) or IgG3m(21) proteins allows histidine 435 to be identified as a critical residue for expression of the epitope recognised by this antibody.
一组23种抗Fcγ单克隆抗体(McAbs)识别的表位已被细分为三组,每组具有不同的拓扑分布。一组相互抑制的McAbs与Cγ2结构域“表面”表达的表位反应。第二组识别Cγ3结构域精氨酸355区域的表位,而第三组识别在Cγ2/Cγ3结构域间区域表达的表位——这通过金黄色葡萄球菌蛋白A结合的抑制得以证明。后一组中一种与IgG1、2、4和IgG3m(15,16)蛋白反应但不与IgG3m(5)或IgG3m(21)蛋白反应的抗体,使得组氨酸435被鉴定为该抗体识别的表位表达的关键残基。