ADP-ribosylation in Clostridium difficile toxin-treated cells is not related to cytopathogenicity of toxin B.
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.
Florin
I
I
Department of Bacteriology, Karolinska Institutet, Stockholm, Sweden.
Thelestam
M
M
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins; D001427:Bacterial Toxins / Q000494:pharmacology*; D002250:Carbon Radioisotopes; D002460:Cell Line; D016360:Clostridioides difficile; D003603:Cytotoxins / Q000494:pharmacology*; D006801:Humans; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism
D001426:Bacterial Proteins; D001427:Bacterial Toxins; D002250:Carbon Radioisotopes; D003603:Cytotoxins; C031815:toxB protein, Clostridium difficile; D009243:NAD; D000246:Adenosine Diphosphate Ribose