Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin

FEBS Lett. 1987 Feb 9;212(1):109-13. doi: 10.1016/0014-5793(87)81566-1.


The culture medium of certain strains of Clostridium botulinum type C contains two separable ADP-ribosyltransferases. Besides the ADP-ribosylation of actin due to botulinum C2 I toxin, a second microbial enzyme causes the mono-ADP-ribosylation of a eukaryotic protein with a molecular mass of about 20 kDa found in platelets, neuroblastoma X glioma hybrid cells, S49 lymphoma cells, chick embryo fibroblasts and sperm. The eukaryotic substrate is inactivated by heating and trypsin treatment. In contrast, the novel ADP-ribosyltransferase, which can be separated by DEAE-Sephadex chromatography, is largely resistant in the short term to trypsin digestion.

MeSH terms

  • ADP Ribose Transferases
  • Actins / metabolism
  • Adenosine Diphosphate Ribose / metabolism
  • Animals
  • Botulinum Toxins / biosynthesis*
  • Botulinum Toxins / isolation & purification
  • Clostridium botulinum / enzymology*
  • Clostridium botulinum / metabolism
  • Hot Temperature
  • Humans
  • Pentosyltransferases / biosynthesis*
  • Proteins / metabolism
  • Trypsin


  • Actins
  • Proteins
  • Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • Pentosyltransferases
  • Trypsin
  • Botulinum Toxins