Ballas M, Eiermann T H, Wölpl A, Goldmann S F
Department of Transplantation Immunology, Red Cross Blood Bank Ulm, Germany.
Tissue Antigens. 1990 Nov;36(5):187-93. doi: 10.1111/j.1399-0039.1990.tb01828.x.
The molecular reaction patterns of the DRw52-specific mouse monoclonal antibodies UL-52 and 7.3.19.1 were investigated. Upon immunoprecipitation and two-dimensional IEF-SDS polyacrylamide gel electrophoresis analysis (2D-PAGE) mAb UL-52 selectively isolated DR beta 1 molecules from DRw52-positive cell lines, whereas mAb 7.3.19.1 predominantly precipitated DR beta 3 molecules. Reduced mAb UL-52 binding affinity was observed to DRw8- and DRw12-positive cells, potentially resulting from structural modifications within the antibody binding site. Comparison of mAb UL-52 reactivity with published DR beta chain amino acid sequences demonstrates that the amino acid residues -S- in positions 11 and 13 on DR beta 1 molecules essentially contribute to the formation of the antibody binding site. mAb 7.3.19.1 reactivity, on the other hand, correlates with the expression of DR beta 3 chain amino acid residues K, G and N, in positions 71, 73 and 77, respectively. In contrast to other DRw52 monoclonal antibodies described so far, mAb UL-52 demonstrates a similar reactivity to DRw52 allosera, suggesting that mAb UL-52 and DRw52 allosera possibly recognize the same or a similar determinant on DR beta 1 molecules.
研究了DRw52特异性小鼠单克隆抗体UL-52和7.3.19.1的分子反应模式。经免疫沉淀和二维IEF-SDS聚丙烯酰胺凝胶电泳分析（2D-PAGE），单克隆抗体UL-52从DRw52阳性细胞系中选择性分离出DRβ1分子，而单克隆抗体7.3.19.1主要沉淀出DRβ3分子。观察到单克隆抗体UL-52与DRw8和DRw12阳性细胞的结合亲和力降低，这可能是由于抗体结合位点内的结构修饰所致。将单克隆抗体UL-52的反应性与已发表的DRβ链氨基酸序列进行比较表明，DRβ1分子第11和13位的氨基酸残基-S-基本上有助于抗体结合位点的形成。另一方面，单克隆抗体7.3.19.1的反应性分别与DRβ3链第71、73和77位的氨基酸残基K、G和N的表达相关。与迄今为止描述的其他DRw52单克隆抗体不同，单克隆抗体UL-52对DRw52同种血清表现出相似的反应性，这表明单克隆抗体UL-52和DRw52同种血清可能识别DRβ1分子上相同或相似的决定簇。
