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Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function Jank T; Giesemann T; Aktories KGlycobiology 2007[Apr]; 17 (4): 15R-22RClostridium 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.|Bacterial Toxins/chemistry/*metabolism[MESH]|Binding Sites[MESH]|Catalytic Domain[MESH]|Crystallography, X-Ray[MESH]|Cytosol/metabolism[MESH]|Endocytosis[MESH]|Enterotoxins/chemistry/*metabolism[MESH]|Glucosyltransferases/*metabolism[MESH]|Receptors, Immunologic/metabolism[MESH]|rho GTP-Binding Proteins/*metabolism[MESH] |
