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Updated: Mar 29, 2026

Cefoperazone-treated Mouse Model of Clinically-relevant Clostridium difficile Strain R20291
Published on: December 10, 2016
Binding and entry of Clostridium difficile toxin B is mediated by multiple domains
Jared S Manse1, Michael R Baldwin1
1Department of Molecular Microbiology and Immunology, University of Missouri School of Medicine, Columbia, MO, USA.
Abstract:
Clostridium difficile is responsible for a number of serious gastrointestinal diseases caused primarily by two exotoxins, TcdA and TcdB. These toxins enter host cells by binding unique receptors, at least partially via their combined repetitive oligopeptides (CROPs) domains. Our study investigated structural determinants necessary for binding and entry of TcdB. Deletion analyses identified TcdB residues 1372-1493 as essential for cytotoxicity in three cell lines. Consistent with this observation, overlapping TcdB fragments (residues 1372-1848, 1372-1493 and 1493-1848) were able to independently bind cells. Our data provide new evidence supporting a more complex model of clostridial glucosylating toxin uptake than previously suggested.
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