期刊
GLYCOBIOLOGY
卷 17, 期 4, 页码 15R-22R出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwm004
关键词
bacterial protein toxins; clostridial glucosylating toxins; glycosyltransferases; crystal structure; protein toxin uptake; Rho proteins; UDP-glucose; Clostridium novyi alpha-toxin
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.
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