Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects.
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.
Teichert
Matthias
M
Institut für Toxikologie, Medizinische Hochschule Hannover, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Tatge
Helma
H
Schoentaube
Janett
J
Just
Ingo
I
Gerhard
Ralf
R
D000818:Animals; D001427:Bacterial Toxins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D018938:Caco-2 Cells; D004768:Enterotoxins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology; D005964:Glucosyltransferases / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D006801:Humans; D051379:Mice; D009154:Mutation; D014364:Tryptophan / Q000737:chemistry / Q000235:genetics; D015854:Up-Regulation; D020743:rhoB GTP-Binding Protein / Q000819:agonists* / Q000378:metabolism
D001427:Bacterial Toxins; D004768:Enterotoxins; C041348:tcdA protein, Clostridium difficile; D014364:Tryptophan; D005964:Glucosyltransferases; D020743:rhoB GTP-Binding Protein