Gillis T P, Miller R A, Young D B, Khanolkar S R, Buchanan T M
Infect Immun. 1985 Aug;49(2):371-7. doi: 10.1128/iai.49.2.371-377.1985.
A panel of nine monoclonal antibodies to Mycobacterium leprae were used to characterize a protein antigen of the bacillus. Two monoclonal antibodies (IVD8 and IIIE9) were specific for M. leprae and reacted with an epitope (CWPa) present on a protein molecule associated with the cell wall fraction of M. leprae. This protein, designated cell wall-associated protein (CWP), lost its immunoreactivity upon treatment with trypsin and had an apparent molecular weight of 65,000, though additional lower-molecular-weight forms of the protein were observed by immunoblotting. Four other cross-reactive epitopes (CWPb, CWPc, CWPd, and CWPe) were defined on the same molecule using seven independent monoclonal antibodies. Therefore, M. leprae possesses a trypsin-sensitive, heat-stable protein associated with the cell wall which contains at least one species-specific and four cross-reactive antigenic determinants.
一组针对麻风分枝杆菌的九种单克隆抗体被用于鉴定该杆菌的一种蛋白质抗原。两种单克隆抗体（IVD8和IIIE9）对麻风分枝杆菌具有特异性，并与存在于与麻风分枝杆菌细胞壁部分相关的蛋白质分子上的一个表位（CWPa）发生反应。这种蛋白质，命名为细胞壁相关蛋白（CWP），经胰蛋白酶处理后失去免疫反应性，表观分子量为65,000，不过通过免疫印迹观察到该蛋白质还有其他较低分子量的形式。使用七种独立的单克隆抗体在同一分子上确定了另外四个交叉反应表位（CWPb、CWPc、CWPd和CWPe）。因此，麻风分枝杆菌拥有一种与细胞壁相关的、对胰蛋白酶敏感且热稳定的蛋白质，该蛋白质包含至少一个种特异性抗原决定簇和四个交叉反应抗原决定簇。
