Auto-catalytic Cleavage of Clostridium difficile Toxins A and B Depends on Cysteine Protease Activity*

@article{Egerer2007AutocatalyticCO,
  title={Auto-catalytic Cleavage of Clostridium difficile Toxins A and B Depends on Cysteine Protease Activity*},
  author={Martina Egerer and T. Giesemann and T. Jank and K. Satchell and K. Aktories},
  journal={Journal of Biological Chemistry},
  year={2007},
  volume={282},
  pages={25314 - 25321}
}
The action of Clostridium difficile toxins A and B depends on processing and translocation of the catalytic glucosyltransferase domain into the cytosol of target cells where Rho GTPases are modified. Here we studied the processing of the toxins. Dithiothreitol and β-mercaptoethanol induced auto-cleavage of purified native toxin A and toxin B into ∼250/210- and ∼63-kDa fragments. The 63-kDa fragment was identified by mass spectrometric analysis as the N-terminal glucosyltransferase domain. This… Expand
Autocatalytic Processing of Clostridium difficile Toxin B
Autoproteolytic cleavage mediates cytotoxicity of Clostridium difficile toxin A
Masking autoprocessing of Clostridium difficile toxin A by the C-terminus combined repetitive oligo peptides.
Structural organization of the functional domains of Clostridium difficile toxins A and B
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