Evidence map›Paper›PMID 17693508›Full record

ArticleJournal of bacteriology2007

Cwp84, a surface-associated protein of Clostridium difficile, is a cysteine protease with degrading activity on extracellular matrix proteins.

Claire Janoir, Séverine Péchiné, Charlotte Grosdidier, Anne Collignon

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.

  1. Antibiotic-Associated Diarrhea BeyondThe Brown journal of hospital medicine · 2023
    Pooled it
  2. Review
  3. Article
  4. Immunization Strategies Against Clostridioides difficile.Advances in experimental medicine and biology · 2024
    Review
  5. Review
  6. Review
  7. Microbiology (Reading, England) · 2023
    Review
  8. Article
  9. Article
  10. International journal of molecular sciences · 2022
    Article
  11. Genetic Mechanisms of Vancomycin Resistance inAntibiotics (Basel, Switzerland) · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. The structure of the S-layer of Clostridium difficile.Journal of cell communication and signaling · 2018
    Review
  18. TargetingFrontiers in microbiology · 2018
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Claire JanoirUniversité de Paris-Sud, Faculté de Pharmacie, Département de Microbiologie, 5 rue JB Clément, 92296, Châtenay-Malabry Cedex, France.
Séverine Péchiné
Charlotte Grosdidier
Anne Collignon
Université Paris-Sud · FRAssistance Publique – Hôpitaux de Paris · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clostridium difficile pathogenicity is mediated mainly by its A and B toxins, but the colonization process is thought to be a necessary preliminary step in the course of infection. The aim of this study was to characterize the Cwp84 protease of C. difficile, which is highly immunogenic in patients with C. difficile-associated disease and is potentially involved in the pathogenic process. Cwp84 was purified as a recombinant His-tagged protein, and specific antibodies were generated in rabbits. Treatment of multiple-band-containing eluted fractions with a reducing agent or with trypsin led to accumulation of a unique protein species with an estimated molecular mass of 61 kDa, corresponding most likely to mature autoprocessed Cwp84 (mCwp84). mCwp84 showed concentration-dependent caseinolytic activity, with maximum activity at pH 7.5. The Cwp84 activity was inhibited by various cysteine protease inhibitors, such as the specific inhibitor E64, and the anti-Cwp84-specific antibodies. Using fractionation experiments followed by immunoblot detection, the protease was found to be associated with the S-layer proteins, mostly as a nonmature species. Proteolytic assays were performed with extracellular matrix proteins to assess the putative role of Cwp84 in the pathogenicity of C. difficile. No degrading activity was detected with type IV collagen. In contrast, Cwp84 exhibited degrading activity with fibronectin, laminin, and vitronectin, which was neutralized by the E64 inhibitor and specific antibodies. In vivo, this proteolytic activity could contribute to the degradation of the host tissue integrity and to the dissemination of the infection.

Indexed as

Antibodies, BacterialBacterial ProteinsCaseinsClostridioides difficileCysteine EndopeptidasesCysteine Proteinase InhibitorsEnzyme StabilityExtracellular Matrix ProteinsHydrogen-Ion ConcentrationImmunoblottingMembrane GlycoproteinsMolecular WeightRecombinant ProteinsAntibodies, BacterialBacterial ProteinsCaseinsCwp84 protein, Clostridium difficileCysteine EndopeptidasesCysteine Proteinase InhibitorsExtracellular Matrix ProteinsMembrane GlycoproteinsRecombinant ProteinsS-layer proteins

Identifiers

PMID17693508
PMCPMC2168428
OpenAlexW2144447845

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.