Journal
JOURNAL OF MASS SPECTROMETRY
Volume 44, Issue 3, Pages 368-374Publisher
WILEY
DOI: 10.1002/jms.1514
Keywords
Clostridium difficile; S-layer; glycosylation; pathogenesis; bacterium
Funding
- BBSRC [BBS/B/09708]
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BBS/B/09708] Funding Source: researchfish
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Like many other bacterial cell surfaces, the cell wall of Clostridium difficile is also encapsulated by a proteinaceous paracrystalline layer, the surface (S)-layer. In many bacterial species, the S-layer proteins (SLPs) have been shown to be glycosylated, whereas in other species glycosylation is absent. Unusually, the S-layer of C. difficile is composed of two distinct proteins, the high-molecular weight (HMW) and low-molecular-weight (LMW) SLPs. Previous investigations have reported that one or both of these SLPs are glycosylated, though no definitive study has been conducted. We have used a variety of mass spectrometric approaches to analyse SLPs from a number of strains of C. difficile for the presence of associated glycans. Analysis of intact SLPs by matrix assisted laser desorption/ionisation time of flight (MALDI-ToF) mass spectrometry demonstrated that the observed molecular masses matched the predicted masses of the LMW and HMW SLPs. Furthermore, analysis of Cyanogen bromide (CNBr) and tryptic peptides displayed no evidence of post-translational modification. In the first in-depth study of its kind, we unequivocally demonstrate that the S-layer proteins from the C. difficile strains investigated are not glycosylated. Copyright (C) 2008 John Wiley & Sons, Ltd.
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