Diamond A G, Butcher G W, Howard J C
J Immunol. 1984 Mar;132(3):1169-75.
We describe two monoclonal antibodies, R3/47 and YR1/1, directed against different epitopes of the expressed rat class I major transplantation antigen RT1Aa, that interact with each other so that the binding of one antibody, YR1/1, is greatly enhanced by the binding of the other. The positive interaction between R3/47 and YR1/1 also occurs when using RT1Aa molecules solubilized from cell membranes in detergent. It is therefore unlikely that the molecular environment of the membrane contributes to the interaction. The ability of R3/47 to modify the YR1/1 determinant on the RT1Aa molecule is mediated without any significant loss of potency by highly purified monomeric Fab fragments. This result suggests that the binding of R3/47 to the RT1Aa molecule alters the YR1/1 determinant by initiating a propagated conformational change in the antigen.
我们描述了两种单克隆抗体，R3/47和YR1/1，它们针对表达的大鼠I类主要移植抗原RT1Aa的不同表位，彼此相互作用，使得一种抗体YR1/1的结合会因另一种抗体的结合而大大增强。当使用在去污剂中从细胞膜溶解的RT1Aa分子时，R3/47和YR1/1之间的正向相互作用也会发生。因此，膜的分子环境不太可能促成这种相互作用。R3/47修饰RT1Aa分子上YR1/1决定簇的能力是由高度纯化的单体Fab片段介导的，且效力没有任何显著损失。这一结果表明，R3/47与RT1Aa分子的结合通过引发抗原中传播的构象变化来改变YR1/1决定簇。
