三种特异性针对小鼠白细胞介素-2受体p55亚基配体结合位点区域的单克隆抗体的特性分析。
Characterization of three monoclonal antibodies specifically directed against the ligand binding site area of the p55 subunit of the mouse interleukin-2 receptor.
作者信息
Moreau J L, Somme G, Dautry-Varsat A, Thèze J
机构信息
Unité d'Immunogénétique Cellulaire, Institut Pasteur, Paris, France.
出版信息
Mol Immunol. 1988 Jan;25(1):57-61. doi: 10.1016/0161-5890(88)90090-9.
Three new rat monoclonal antibodies (MAbs) (5A2, 125A8 and 135D5) directed against the mouse interleukin-2 receptor (IL-2R) were isolated. They were obtained after immunization of LOU rats with 14.1.6 T helper cell clones. These three MAbs recognize the p55 subunit of the IL-2R and compete with the binding of previously characterized MAbs AMT13 and 3C7 specific for this p55 subunit [Moreau et al. (1987) Eur. J. Immun. 15, 723-727]. They recognize the same (or closely related epitopes) since they reciprocally compete with each other's binding. Scatchard plot analysis of the data from inhibition experiments clearly indicate that they recognize with very high affinity the ligand binding site area of the p55 subunit of the IL-2R. The properties of the Fab fragment prepared from 5A2 and 135D5 indicate that at saturation one intact IgG molecule binds two IL-2R molecules.
分离出了三种针对小鼠白细胞介素-2受体（IL-2R）的新型大鼠单克隆抗体（MAb）（5A2、125A8和135D5）。它们是在用14.1.6 T辅助细胞克隆免疫LOU大鼠后获得的。这三种单克隆抗体识别IL-2R的p55亚基，并与先前鉴定的针对该p55亚基的单克隆抗体AMT13和3C7的结合相互竞争[莫罗等人（1987年），《欧洲免疫学杂志》15，723 - 727]。由于它们相互竞争彼此的结合，所以它们识别相同（或密切相关的表位）。对抑制实验数据的Scatchard图分析清楚地表明，它们以非常高的亲和力识别IL-2R的p55亚基的配体结合位点区域。从5A2和135D5制备的Fab片段的特性表明，在饱和状态下，一个完整的IgG分子结合两个IL-2R分子。
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