ArticleMolecular & cellular proteomics : MCP2014
A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 66 citations in OpenAlex.
- Design and Synthesis of Phosphonoproline-Proline Bioisosteric Mimetics of Proline Dimers: Pseudopeptide Constructs as Potential Inhibitors of the Zn-Metalloprotease PPEP‑1 Associated withACS medicinal chemistry letters · 2026Article
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- Bacterial zinc metalloproteases as facilitators of pathogenic success: a review.Archives of microbiology · 2026Review
- The current riboswitch landscape inMicrobiology (Reading, England) · 2024Review
- Emerging Diagnostics inInternational journal of molecular sciences · 2024Review
- Characterization of the Clostridioides difficile 630Δerm putative Pro-Pro endopeptidase CD1597.Access microbiology · 2024Article
- In-Depth Specificity Profiling of Endopeptidases Using Dedicated Mix-and-Split Synthetic Peptide Libraries and Mass Spectrometry.Analytical chemistry · 2023Article
- Review
- Coordinated modulation of multiple processes through phase variation of a c-di-GMP phosphodiesterase in Clostridioides difficile.PLoS pathogens · 2022Article
- Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.Plants (Basel, Switzerland) · 2022Review
- Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.Current research in microbial sciences · 2021Review
- A Bioluminescent Sensor for Rapid Detection of PPEP-1, aSensors (Basel, Switzerland) · 2021Article
- Clostridium difficile clade 3 (RT023) have a modified cell surface and contain a large transposable island with novel cargo.Scientific reports · 2019Article
- Molecular determinants of the mechanism and substrate specificity ofThe Journal of biological chemistry · 2019Article
- Clostridial Genetics: Genetic Manipulation of the Pathogenic Clostridia.Microbiology spectrum · 2019Review
- Article
- Cyclic diguanylate riboswitches control bacterial pathogenesis mechanisms.PLoS pathogens · 2019Article
- Article
- Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.The Journal of biological chemistry · 2018Article
- Type IV Pili Promote Clostridium difficile Adherence and Persistence in a Mouse Model of Infection.Infection and immunity · 2018Article
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial secreted proteins constitute a biologically important subset of proteins involved in key processes related to infection such as adhesion, colonization, and dissemination. Bacterial extracellular proteases, in particular, have attracted considerable attention, as they have been shown to be indispensable for bacterial virulence. Here, we analyzed the extracellular subproteome of Clostridium difficile and identified a hypothetical protein, CD2830, as a novel secreted metalloprotease. Following the identification of a CD2830 cleavage site in human HSP90β, a series of synthetic peptide substrates was used to identify the favorable CD2830 cleavage motif. This motif was characterized by a high prevalence of proline residues. Intriguingly, CD2830 has a preference for cleaving Pro-Pro bonds, unique among all hitherto described proteases. Strikingly, within the C. difficile proteome two putative adhesion molecules, CD2831 and CD3246, were identified that contain multiple CD2830 cleavage sites (13 in total). We subsequently found that CD2830 efficiently cleaves CD2831 between two prolines at all predicted cleavage sites. Moreover, native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246. These findings highlight CD2830 as a highly specific endoproteinase with a preference for proline residues surrounding the scissile bond. Moreover, the efficient cleavage of two putative surface adhesion proteins points to a possible role of CD2830 in the regulation of C. difficile adhesion.
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