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J Med Microbiol 57 (2008), 690-696; DOI: 10.1099/jmm.0.47742-0
© 2008 Society for General Microbiology
ISSN 1473-5644

Review

Processing of Clostridium difficile toxins

Torsten Giesemann, Martina Egerer, Thomas Jank and Klaus Aktories

Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Universität Freiburg, Albertstrasse 25, D-79104 Freiburg, Germany

Correspondence
Klaus Aktories
Klaus.Aktories{at}pharmakol.uni-freiburg.de


The pathogenicity of Clostridium difficile depends on the large clostridial glucosylating toxins A and B (TcdA and TcdB). The proteins accomplish their own uptake by a modular structure comprising a catalytic and a binding/translocation domain. Based on a proteolytic processing step solely the catalytic domain reaches the cytosol. Within the cells, the glucosyltransferases inactivate small GTPases by mono-O-glucosylation. Here, a short overview is given regarding latest insights into the intramolecular processing, which is mediated by an intrinsic protease activity.




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I. R. Poxton
Proceedings from the 2nd International Clostridium difficile Symposium, Maribor, Slovenia, June 2007.
J. Med. Microbiol., June 1, 2008; 57(Pt 6): 683 - 794.
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