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Binding and entry of Clostridium difficile toxin B is mediated by multiple domains
Author(s) -
Manse Jared S.,
Baldwin Michael R.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.11.017
Subject(s) - clostridium difficile toxin a , clostridium difficile toxin b , toxin , clostridium difficile , enterotoxin , oligopeptide , receptor , microbiology and biotechnology , biology , cytotoxicity , biochemistry , chemistry , peptide , in vitro , gene , antibiotics , escherichia coli
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.