Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects

Infect Immun. 2006 Oct;74(10):6006-10. doi: 10.1128/IAI.00545-06.

Abstract

Mutation of tryptophan-101 in Clostridium difficile toxin A, a 308-kDa glucosyltransferase, resulted in a 50-fold-reduced cytopathic activity in cell culture experiments. The mutant toxin A was characterized and applied to distinguish between glucosyltransferase-dependent and -independent effects with respect to RhoB up-regulation as a cellular stress response.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Toxins / chemistry
  • Bacterial Toxins / genetics
  • Bacterial Toxins / pharmacology*
  • Caco-2 Cells
  • Enterotoxins / chemistry
  • Enterotoxins / genetics
  • Enterotoxins / pharmacology*
  • Fibroblasts / drug effects
  • Fibroblasts / enzymology
  • Glucosyltransferases / chemistry
  • Glucosyltransferases / genetics
  • Glucosyltransferases / pharmacology*
  • Humans
  • Mice
  • Mutation
  • Tryptophan / chemistry
  • Tryptophan / genetics
  • Up-Regulation
  • rhoB GTP-Binding Protein / agonists*
  • rhoB GTP-Binding Protein / metabolism

Substances

  • Bacterial Toxins
  • Enterotoxins
  • tcdA protein, Clostridium difficile
  • Tryptophan
  • Glucosyltransferases
  • rhoB GTP-Binding Protein