期刊
FEBS LETTERS
卷 589, 期 24, 页码 3945-3951出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.11.017
关键词
Clostridium difficile toxin B; Binding; Toxicity; Combined repetitive oligopeptide; Modular binding motif (MBM); Clostridium difficile
资金
- University of Missouri
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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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