Alexander S, Smith E, Davis L, Gooley A, Por S B, Browne L, Williams K L
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Differentiation. 1988 Jul;38(2):82-90. doi: 10.1111/j.1432-0436.1988.tb00201.x.
The monoclonal antibody MUD50 recognizes a group of developmentally regulated proteins, which are almost exclusively expressed by prespore cells in developing aggregates of Dictyostelium discoideum. Some of these antigens are integrally associated with the cell membrane, as assessed by physical and detergent-fractionation procedures. The MUD50-reactive proteins are glycosylated and some are phosphorylated. Post-translational modification is the common antigenic feature that is recognized by the MUD50 antibody in these cell-type-specific proteins. A glycosylation-defective mutant, DL118, (modB) does not express the MUD50 epitope, but does express the MUD52 epitope, which is found on a different group of glycoproteins. Therefore, we conclude that MUD50 recognizes a particular carbohydrate epitope on a restricted group of proteins. These proteins are structurally diverse, but are apparently involved in the maintenance of structure and movement of the multicellular D. discoideum slug.
单克隆抗体MUD50识别一组受发育调控的蛋白质，这些蛋白质几乎只在盘基网柄菌发育中的聚集体的前孢子细胞中表达。通过物理和去污剂分级分离程序评估，其中一些抗原与细胞膜紧密相关。MUD50反应性蛋白是糖基化的，有些是磷酸化的。翻译后修饰是这些细胞类型特异性蛋白中MUD50抗体识别的共同抗原特征。糖基化缺陷突变体DL118（modB）不表达MUD50表位，但表达MUD52表位，MUD52表位存在于另一组糖蛋白上。因此，我们得出结论，MUD50识别一组受限蛋白质上的特定碳水化合物表位。这些蛋白质在结构上各不相同，但显然参与了多细胞盘基网柄菌蛞蝓体的结构维持和运动。
