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Glycobiology Advance Access originally published online on January 19, 2007
Glycobiology 2007 17(4):15R-22R; doi:10.1093/glycob/cwm004
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

REVIEW

Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function

Thomas Jank, Torsten Giesemann and Klaus Aktories1

Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Otto-Krayer-Haus, Albertstrasse 25, D-79104 Freiburg, Germany

1 To whom correspondence should be addressed; Tel: +49-761-2035301; Fax: +49-761-2035311; E-mail: klaus.aktories{at}pharmakol.uni-freiburg.de

Received on December 8, 2006; revised on January 9, 2007; accepted on January 9, 2007

Clostridium difficile causes pseudomembranous colitis and is responsible for many cases of nosocomial antibiotic-associated diarrhea. Major virulence factors of C. difficile are the glucosylating exotoxins A and B. Both toxins enter target cells in a pH- dependent manner from endosomes by forming pores. They translocate the N-terminal catalytic domains into the cytosol of host cells and inactivate Rho guanosine triphosphatases by glucosylation. The crystal structure of the catalytic domain of toxin B was solved in a complex with uridine diphosphate, glucose, and manganese ion, exhibiting a folding of type A family glycosyltransferases. Crystallization of fragments of the C-terminus of toxin A, which is characterized by polypeptide repeats, revealed a solenoid-like structure often found in bacterial cell surface proteins. These studies, which provide new insights into structure, uptake, and function of the family of clostridial glucosylating toxins, are reviewed.

Key words: Bacterial protein toxins / clostridial glucosylating toxins / glycosyltransferases / crystal structure / protein toxin uptake / Rho proteins / UDP-glucose / Clostridium novyi {alpha}-toxin


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