ArticleMicrobiology (Reading, England)2014
Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination.
Article in Microbiology (Reading, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 50 citations in OpenAlex.
- Bile acid dependent attenuation of toxin mediated disease is independent of colonization resistance againstbioRxiv : the preprint server for biology · 2026Article
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- Phenotypic analysis of variousApplied and environmental microbiology · 2025Article
- Targeting SleC and CspB in the Inhibition of Spore Germination inJournal of medicinal chemistry · 2025Article
- Phenotypic analysis of variousbioRxiv : the preprint server for biology · 2025Article
- Influence of microbiota on the growth and gene expression of Clostridioides difficile in an in vitro coculture model.MicrobiologyOpen · 2024Article
- Clostridium septicum manifests a bile salt germinant response mediated by Clostridioides difficile csp gene orthologs.Communications biology · 2024Article
- The small acid-soluble proteins of Clostridioides difficile regulate sporulation in a SpoIVB2-dependent manner.PLoS pathogens · 2024Article
- The small acid-soluble proteins ofbioRxiv : the preprint server for biology · 2024Article
- A dual-action antibiotic that killsProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mucosal Vaccination Strategies againstVaccines · 2023Review
- Clostridioides difficile spore germination: initiation to DPA release.Current opinion in microbiology · 2022Review
- The small acid-soluble proteins of Clostridioides difficile are important for UV resistance and serve as a check point for sporulation.PLoS pathogens · 2021Article
- Cwl0971, a novel peptidoglycan hydrolase, plays pleiotropic roles in Clostridioides difficile R20291.Environmental microbiology · 2021Article
- From Root to Tips: Sporulation Evolution and Specialization in Bacillus subtilis and the Intestinal Pathogen Clostridioides difficile.Molecular biology and evolution · 2019Article
- Sporulation and Germination in Clostridial Pathogens.Microbiology spectrum · 2019Review
- The lytic transglycosylase, LtgG, controls cell morphology and virulence in Burkholderia pseudomallei.Scientific reports · 2019Article
- Updates to Clostridium difficile Spore Germination.Journal of bacteriology · 2018Review
- Article
- Clostridium sordellii outer spore proteins maintain spore structural integrity and promote bacterial clearance from the gastrointestinal tract.PLoS pathogens · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Clostridium difficile is the most common cause of enteric disease and presents a major burden on healthcare systems globally due in part to the observed rapid rise in antibiotic resistance. The ability of C. difficile to form endospores is a key feature in the organism's pathogenesis and transmission, and contributes greatly to its resilient nature. Endospores are highly resistant to disinfection, allowing them to persist on hospital surfaces. In order for the organism to cause disease, the spores must germinate and revert to a vegetative form. While spore germination in Bacillus spp. is well understood, very little is known about this process in Clostridia. Here we report the characterization of SleC (CD0551) from C. difficile 630. Bioinformatic analysis of SleC indicated a multi-domained protein possessing a peptidoglycan-binding (PGB) domain, a SpoIID/LytB domain and an undefined N-terminal region. We have confirmed that SleC is an exo-acting lytic transglycosylase with the catalytic activity localized to the N-terminal region. Additionally, we have shown that both the N-terminal catalytic domain and the C-terminal PGB domain require muramyl-δ-lactam for substrate binding. As with carbohydrate-binding modules from cellulases and xylanases, the PGB domain may be responsible for increasing the processivity of SleC by concentrating the enzyme at the surface of the substrate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.