Young D B, Fohn M J, Khanolkar S R, Buchanan T M
Clin Exp Immunol. 1985 Jun;60(3):546-52.
Monoclonal antibodies (MoAb) have been used to analyse a protein antigen from Mycobacterium leprae with a subunit mol. wt of 28,000 daltons. Three different patterns of species specificity were observed with two antibodies being specific for M. leprae, two partially specific, and one broadly cross-reactive amongst all mycobacteria. Competitive binding and sandwich assays demonstrated that the specific and partially specific antibodies recognized closely related regions of the molecule while the cross-reactive antibody recognized a spatially separate epitope on the same polypeptide chain. Identification of specific and cross-reactive epitopes on a single antigenic molecule may be of considerable importance for understanding the functioning of the cell-mediated immune system during leprosy infection and the use of MoAb for such analyses is discussed.
单克隆抗体（MoAb）已被用于分析来自麻风分枝杆菌的一种亚基分子量为28,000道尔顿的蛋白质抗原。观察到三种不同的物种特异性模式，其中两种抗体对麻风分枝杆菌具有特异性，两种具有部分特异性，还有一种在所有分枝杆菌中具有广泛交叉反应性。竞争性结合和夹心测定表明，特异性和部分特异性抗体识别分子的密切相关区域，而交叉反应性抗体识别同一多肽链上空间上分离的表位。鉴定单个抗原分子上的特异性和交叉反应性表位对于理解麻风感染期间细胞介导的免疫系统的功能可能具有相当重要的意义，并且讨论了使用单克隆抗体进行此类分析的情况。
