The nosocomially acquired pathogen Clostridium difficile is the primary causative agent of antibiotic associated diarrhoea and causes tens of thousands of deaths globally each year. C. difficile presents a paracrystalline protein array on the surface of the cell known as an S-layer. S-layers have been demonstrated to possess a wide range of important functions, which, combined with their inherent accessibility, makes them a promising drug target. The unusually complex S-layer of C. difficile is primarily comprised of the high- and low- molecular weight S-layer proteins, HMW SLP and LMW SLP, formed from the cleavage of the S-layer precursor protein, SlpA, but may also contain up to 28 SlpA paralogues. A model of how the S-layer functions as a whole is required if it is to be exploited in fighting the bacterium. Here, we provide a summary of what is known about the S-layer of C. difficile and each of the paralogues and, considering some of the domains present, suggest potential roles for them.
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Acknowledgements The authors wish to thank Harry Thorpe (University of Bath) for assistance creating Fig. 2 . Funding This work was supported by a postgraduate studentship from Public Health England (PHE, Porton Down, England) and the University of Bath to WJB and a Medical Research Council (UK) project grant (MR/ K027123/1) to KRA and CCS. KRA wishes to thank University of Bath for a 6-month academic sabbatical leave.
© 2017, The Author(s).
- Bacterial adhesion
- C. difficile Infection
- Cell wall protein
- Clostridium Difficile