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Article

Mutational analysis of the enzymatic domain of Clostridium difficile toxin B reveals novel inhibitors of the wild-type toxin.

Infection and immunity - 1 Jun 2003

Spyres Lea M, Daniel Jeremy, Hensley Amy, Qa'Dan Maen, Ortiz-Leduc William, Ballard Jimmy D

Abstract excerpt

Toxin B (TcdB), a major Clostridium difficile virulence factor, glucosylates and inactivates the small GTP-binding proteins Rho, Rac, and Cdc42. In the present study we provide evidence that enzymatically inactive fragments of the TcdB enzymatic domain are effective intracellular inhibitors of native TcdB. Site-directed and deletion mutants of the TcdB enzymatic region (residues 1 to 556), lacking receptor...

Topics

Animals
Bacterial Proteins
Bacterial Toxins
CHO Cells
Cricetinae
Glycosylation
HeLa Cells
Humans
Mutation
Virulence Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 12761111
DOI: 10.1128/IAI.71.6.3294-3301.2003
PMCID: PMC155706

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Mutational analysis of the enzymatic domain of Clostridium difficile toxin B reveals novel inhibitors of the wild-type toxin.PMID 12761111Read ↗

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