Clostridium botulinum type C produces a novel ADP‐ribosyltransferase distinct from botulinum C2 toxin
- 9 February 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 212 (1), 109-113
- https://doi.org/10.1016/0014-5793(87)81566-1
Abstract
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 × 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.Keywords
This publication has 6 references indexed in Scilit:
- Botulinum C2 toxin ADP-ribosylates actinNature, 1986
- ADP-Ribosylating Microbial ToxinsCRC Critical Reviews in Microbiology, 1984
- Islet-activating protein, pertussis toxin: a probe for functions of the inhibitory guanine nucleotide regulatory component of adenylate cyclaseTrends in Pharmacological Sciences, 1984
- Cholera Toxin-Catalyzed ADP-Ribosylation of Membrane ProteinsPublished by Elsevier BV ,1982
- Purification and characterization of two components of botulinum C2 toxinInfection and Immunity, 1980
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970