Florin I, Thelestam M
Department of Bacteriology, Karolinska Institutet, Stockholm, Sweden.
Biochim Biophys Acta. 1991 Jan 10;1091(1):51-4. doi: 10.1016/0167-4889(91)90221-i.
ADP-ribosylation of a protein in human fibroblasts treated with partially purified Clostridium difficile toxin B was previously reported. Here we show that the same protein was ADP-ribosylated also in human fibroblasts exposed to supernatant from a C. difficile strain producing neither toxin A nor toxin B. Furthermore, in Chinese hamster ovary and in Vero cells, showing toxin B-induced cytopathogenic effect, the protein was not significantly ADP-ribosylated. The results indicate that the ADP-ribosylation is unrelated to the cytopathogenic effect of toxin B. It appears to be caused by another unidentified factor from C. difficile, and the substrate may correspond to a protein modified endogenously in cells exposed to stressful situations. Cellular actin was not ADP-ribosylated by toxin B.
先前有报道称，用部分纯化的艰难梭菌毒素B处理的人成纤维细胞中的一种蛋白质会发生ADP核糖基化。在此我们表明，在暴露于既不产生毒素A也不产生毒素B的艰难梭菌菌株的上清液的人成纤维细胞中，同一蛋白质也会发生ADP核糖基化。此外，在表现出毒素B诱导的细胞病变效应的中国仓鼠卵巢细胞和Vero细胞中，该蛋白质并未显著发生ADP核糖基化。结果表明，ADP核糖基化与毒素B的细胞病变效应无关。它似乎是由艰难梭菌的另一种未鉴定因子引起的，并且底物可能对应于在暴露于应激情况的细胞中内源性修饰的一种蛋白质。细胞肌动蛋白不会被毒素B进行ADP核糖基化。
