Rolf J M, Gaudin H M, Tirrell S M, MacDonald A B, Eidels L
Department of Microbiology, University of Texas Southwestern Medical Center, Dallas 75235.
Proc Natl Acad Sci U S A. 1989 Mar;86(6):2036-9. doi: 10.1073/pnas.86.6.2036.
An anti-idiotypic serum prepared against the combining site (idiotype) of specific anti-diphtheria toxoid antibodies was characterized with respect to its interaction with highly diphtheria toxin-sensitive Vero cells. Although the anti-idiotypic serum protected Vero cells against the cytotoxic action of diphtheria toxin, it did not prevent the binding of 125I-labeled diphtheria toxin to the cells but did inhibit the internalization and degradation of 125I-labeled toxin. This anti-idiotypic serum immunoprecipitated a cell-surface protein from radiolabeled Vero cells with an apparent Mr of approximately 15,000. These results are consistent with the hypothesis that the anti-idiotypic serum contains antibodies that carry an internal image of an internalization site on the toxin and that a cell-surface protein involved in toxin internalization possesses a complementary site recognized by both the toxin and the anti-idiotypic antibodies.
制备了一种针对特异性抗白喉类毒素抗体结合位点(独特型)的抗独特型血清,并对其与对白喉毒素高度敏感的非洲绿猴肾细胞(Vero细胞)的相互作用进行了表征。虽然抗独特型血清可保护Vero细胞免受白喉毒素的细胞毒性作用,但它并不能阻止125I标记的白喉毒素与细胞的结合,却能抑制125I标记毒素的内化和降解。这种抗独特型血清从放射性标记的Vero细胞中免疫沉淀出一种表观分子量约为15000的细胞表面蛋白。这些结果与以下假设一致:抗独特型血清含有携带毒素内化位点内影像的抗体,并且参与毒素内化的细胞表面蛋白具有一个能被毒素和抗独特型抗体识别的互补位点。