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Structural characterisation of the TcdA toxin from Clostridium difficile

Reference	B15840
Principal Investigator / Supervisor	Professor Neil Fairweather
Co-Investigators / Co-Supervisors	Dr Katherine Brown, Professor Steve Matthews
Institution	Imperial College London
Department	Biological Sciences
Funding type	Research
Value (£)	125,800
Status	Completed
Type	Research Grant
Start date	01/11/2001
End date	30/09/2004
Duration	35 months

Abstract

The bacterial pathogen Clostridium difficile produces two potent high molecular weight protein toxins, TcdA and TcdB. The C-terminal domain of TcdA is essential for binding to host cells, and contains multiple repeated sequences which interact with carbohydrate ligands. We will express and purify the C-terminal repeat region from E. coli and verify functionality using biological assays including direct binding to host cells and competition of TcdA holotoxin binding. We will then use NMR to obtain the three dimensional structure of the repeat domain, both in its free form and as complexes with glycan analogues of its natural glycosylated receptor. In parallel, we will express other domains of TcdA and TcdB in either E. coli or Lactococcus lactis, and carry out crystallisation trials with purified proteins.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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