ADP-ribosylation in Clostridium difficile toxin-treated cells is not related to cytopathogenicity of toxin B

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Bacterial Proteins*
  • Bacterial Toxins / pharmacology*
  • Carbon Radioisotopes
  • Cell Line
  • Clostridium difficile*
  • Cytotoxins / pharmacology*
  • Humans
  • Molecular Weight
  • NAD / metabolism


  • Bacterial Proteins
  • Bacterial Toxins
  • Carbon Radioisotopes
  • Cytotoxins
  • toxB protein, Clostridium difficile
  • NAD
  • Adenosine Diphosphate Ribose