Journal
ACS CHEMICAL BIOLOGY
Volume 5, Issue 3, Pages 279-285Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb9002859
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Funding
- Medical Research Council, U K [G0701834, G0900170]
- Department of Chemistry, Imperial College London
- Biochemical Society, U K
- Biotechnology and Biological Sciences Research Council, U K [BB/D02014X/1]
- Biotechnology and Biological Sciences Research Council [BB/D02014X/1] Funding Source: researchfish
- Medical Research Council [G0701834, G0800170] Funding Source: researchfish
- BBSRC [BB/D02014X/1] Funding Source: UKRI
- MRC [G0701834, G0800170] Funding Source: UKRI
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Clostridium difficile, a leading cause of hospital-acquired infection, possesses a dense surface layer (S-layer) that mediates host-pathogen interactions. The key structural components of the S-layer result from proteolytic cleavage of a precursor protein, SlpA, into high- and low-molecular-weight components. Here we report the discovery and optimization of the first inhibitors of this process in live bacteria and their application for probing S-layer processing. We also describe the design and in vivo application of activity-based probes that identify the protein Cwp84 as the cysteine protease that mediates SlpA cleavage. This work provides novel chemical tools for the analysis of S-layer biogenesis and for the potential identification of novel drug targets within clostridia and related bacterial pathogens.
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