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Analysis of the glycosylated surface proteins of clostridium difficile
Reference
BBS/B/09708
Principal Investigator / Supervisor
Professor Neil Fairweather
Co-Investigators /
Co-Supervisors
Institution
Imperial College London
Department
Biological Sciences
Funding type
Research
Value (£)
209,254
Status
Completed
Type
Research Grant
Start date
01/09/2004
End date
31/12/2007
Duration
40 months
Abstract
Clostridium difficile, the leading cause of hospital acquired antibiotic associated diarrhoea, binds to human enteric tissues via surface layer Proteins. We have purified these proteins and cloned and sequenced their genes. Preliminary experiments have shown these proteins are glycosylated. We will purify S layer proteins from several strains, trypsin digest and examine the products by a series of mass spectrometric techniques. Using this glycol-proteomics approach, we will identify the O-linked glycans covalently attached to the S-layer proteins. Using both recombinant (non-glycosylated) and native (glycosylated) S-layer proteins, we will determine the role of glycosylation in the binding of these proteins to cell lines derived from gut tissues. This project will therefore investigate functional glycosylation in this important but poorly studied bacterial pathogen.
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
Proteomics and Cell Function (PCF) [2003-2004]
Funding Scheme
X – not Funded via a specific Funding Scheme
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