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Glycobiology Advance Access published online on January 19, 2007
Glycobiology, 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

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

Thomas Jank, Torsten Giesemann and Klaus Aktories

Institut für Experimentelle und Klinische Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany

Correspondence address: Dr. Klaus Aktories, Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Otto-Krayer-Haus, Albertstrasse 25, D-79104 Freiburg, Germany, Phone: +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 (AAD). Major virulence factors of Clostridium 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 GTPases by glucosylation. The crystal structure of the catalytic domain of toxin B was solved in a complex with UDP, 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, up-take and function of the family of clostridial glucosylating toxins, are reviewed.

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


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