Processing of Clostridium difficile toxins

J Med Microbiol. 2008 Jun;57(Pt 6):690-696. doi: 10.1099/jmm.0.47742-0.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Bacterial Toxins / chemistry
  • Bacterial Toxins / metabolism*
  • Clostridium difficile / metabolism
  • Clostridium difficile / pathogenicity*
  • Enterotoxins / chemistry
  • Enterotoxins / metabolism*
  • Molecular Sequence Data
  • Virulence

Substances

  • Bacterial Proteins
  • Bacterial Toxins
  • Enterotoxins
  • tcdA protein, Clostridium difficile
  • toxB protein, Clostridium difficile