ArticleThe FEBS journal2017
Cwp2 from Clostridium difficile exhibits an extended three domain fold and cell adhesion in vitro.
Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Article
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- Article
- Unravelling three-way interactions betweenJournal of medical microbiology · 2025Review
- Article
- Review
- Pathogenicity and virulence ofVirulence · 2023Review
- A network of small RNAs regulates sporulation initiation in Clostridioides difficile.The EMBO journal · 2023Article
- Host Immune Responses to Surface S-Layer Proteins (SLPs) ofMicroorganisms · 2023Review
- Review
- Article
- Development of an Effective Nontoxigenic Clostridioides difficile-Based Oral Vaccine against C. difficile Infection.Microbiology spectrum · 2022Article
- Clostridioides difficile phage biology and application.FEMS microbiology reviews · 2021Review
- What's a Biofilm?-How the Choice of the Biofilm Model Impacts the Protein Inventory ofFrontiers in microbiology · 2021Article
- S-layers: The Proteinaceous Multifunctional Armors of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Article
- Cwp22, a novel peptidoglycan cross-linking enzyme, plays pleiotropic roles in Clostridioides difficile.Environmental microbiology · 2019Article
- Slp-coated liposomes for drug delivery and biomedical applications: potential and challenges.International journal of nanomedicine · 2019Review
- Article
- The structure of the S-layer of Clostridium difficile.Journal of cell communication and signaling · 2018Review
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Authors and funding
5 authors.
Funding
Abstract
Colonization of the gut by Clostridium difficile requires the adhesion of the bacterium to host cells. A range of cell surface located factors have been linked to adhesion including the S-layer protein LMW SLP and the related protein Cwp66. As well as these proteins, the S-layer of C. difficile may contain many others. One such protein is Cwp2. Here, we demonstrate the production of a C. difficile strain 630 cwp2 knockout mutant and assess the effect on the bacterium. The mutant results in increased TcdA (toxin A) release and impaired cellular adherence in vitro. We also present the extended three domain structure of the 'functional' region of Cwp2, consisting of residues 29-318 at 1.9 Å, which is compared to that of LMW SLP and Cwp8. The adhesive properties of Cwp2 and LMW SLP, which are likely to be shared by Cwp8, are predicted to be mediated by the variable loop regions in domain 2. DATABASES: Structural data are available in the PDB under the accession number 5NJL.
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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.