Gaulton G N, Bangs J, Maddock S, Springer T, Eardley D D, Strom T B
Clin Immunol Immunopathol. 1985 Jul;36(1):18-29. doi: 10.1016/0090-1229(85)90035-2.
Anti-murine interleukin 2 (IL-2) receptor monoclonal antibodies (mAb) were made from rats immunized with murine cytotoxic lymphocytes. One mAb, designated M7/20, strongly inhibited the proliferation of both IL-2 dependent CTLL-2 cells and concanavalin A (Con A)-induced T-cell blasts. Inhibition was linearly dependent on the concentrations of both M7/20 and IL-2. Utilizing FACS analysis, M7/20 was shown to bind selectively to mitogen-activated T lymphocytes and, to a lesser degree, to activated B lymphocytes. 125I-Labeled M7/20 binding assays indicated that 48-hr Con A-induced T-cell blasts possessed 89,000 binding sites/cell with a Kd of 1.2 X 10(-9) M. Competitive binding analyses indicated that M7/20 and IL-2 occupy the same or overlapping cell surface sites. Preliminary biochemical characterization of M7/20 immunoprecipitates of detergent extracts from both surface-iodinated and internally D-[3H]glucosamine-labeled T lymphoblasts indicated that the murine IL-2 receptor is an N-glycosylated 58,000-Da glycoprotein. Together these results suggest that mAb M7/20 binds at or near the IL-2-binding epitope on the murine IL-2 receptor and, thus, upon manipulation may act as an IL-2 agonist.
抗小鼠白细胞介素2（IL-2）受体单克隆抗体（mAb）由用小鼠细胞毒性淋巴细胞免疫的大鼠制备。一种单克隆抗体，命名为M7/20，强烈抑制IL-2依赖的CTLL-2细胞和伴刀豆球蛋白A（Con A）诱导的T细胞母细胞的增殖。抑制作用与M7/20和IL-2的浓度呈线性相关。利用荧光激活细胞分选术（FACS）分析表明，M7/20选择性地结合有丝分裂原激活的T淋巴细胞，在较小程度上也结合激活的B淋巴细胞。125I标记的M7/20结合试验表明，48小时Con A诱导的T细胞母细胞具有89,000个结合位点/细胞，解离常数（Kd）为1.2×10^(-9)M。竞争性结合分析表明，M7/20和IL-2占据相同或重叠的细胞表面位点。对表面碘化和内部用D-[3H]葡萄糖胺标记的T淋巴母细胞的去污剂提取物进行M7/20免疫沉淀的初步生化特性分析表明，小鼠IL-2受体是一种N-糖基化的58,000道尔顿糖蛋白。这些结果共同表明，单克隆抗体M7/20在小鼠IL-2受体上的IL-2结合表位处或其附近结合，因此，经操作后可能作为一种IL-2激动剂起作用。
