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 wi...

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Bibliographic Details
Published in:Infection and Immunity 2006-10, Vol.74 (10), p.6006-6010
Main Authors: Teichert, Matthias, Tatge, Helma, Schoentaube, Janett, Just, Ingo, Gerhard, Ralf
Format: Article
Language:English
Subjects:
Animals
Bacterial Toxins - chemistry
Bacterial Toxins - genetics
Bacterial Toxins - pharmacology
Biological and medical sciences
Caco-2 Cells
Clostridium difficile
Enterotoxins - chemistry
Enterotoxins - genetics
Enterotoxins - pharmacology
Fibroblasts - drug effects
Fibroblasts - enzymology
Fundamental and applied biological sciences. Psychology
Glucosyltransferases - chemistry
Glucosyltransferases - genetics
Glucosyltransferases - pharmacology
Humans
Mice
Microbiology
Molecular Pathogenesis
Mutation
rhoB GTP-Binding Protein - agonists
rhoB GTP-Binding Protein - metabolism
Tryptophan - chemistry
Tryptophan - genetics
Up-Regulation
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Summary: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.
ISSN:0019-9567
1098-5522
DOI:10.1128/IAI.00545-06