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
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Bacterial Toxins / chemistry
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Bacterial Toxins / genetics
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Bacterial Toxins / pharmacology*
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Caco-2 Cells
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Enterotoxins / chemistry
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Enterotoxins / genetics
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Enterotoxins / pharmacology*
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Fibroblasts / drug effects
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Fibroblasts / enzymology
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Glucosyltransferases / chemistry
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Glucosyltransferases / genetics
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Glucosyltransferases / pharmacology*
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Humans
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Mice
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Mutation
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Tryptophan / chemistry
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Tryptophan / genetics
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Up-Regulation
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rhoB GTP-Binding Protein / agonists*
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rhoB GTP-Binding Protein / metabolism
Substances
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Bacterial Toxins
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Enterotoxins
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tcdA protein, Clostridium difficile
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Tryptophan
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Glucosyltransferases
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rhoB GTP-Binding Protein