Evidence map›Paper›PMID 21531808›Full record

ArticleJournal of bacteriology2011

Roles of cysteine proteases Cwp84 and Cwp13 in biogenesis of the cell wall of Clostridium difficile.

Lucía de la Riva, Stephanie E Willing, Edward W Tate, Neil F Fairweather

Abstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Catalytically Active Recombinant Cysteine Proteases ofInternational journal of molecular sciences · 2025
    Article
  3. Review
  4. AgainstToxins · 2025
    Review
  5. Article
  6. Clostridioides difficile Biofilm.Advances in experimental medicine and biology · 2024
    Article
  7. Review
  8. Microbiology (Reading, England) · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Virulence Factors ofThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2019
    Review
  16. Review
  17. The structure of the S-layer of Clostridium difficile.Journal of cell communication and signaling · 2018
    Review
  18. Review
  19. Review
  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 1 institution in 1 country.

Lucía de la RivaDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Stephanie E Willing
Edward W Tate
Neil F Fairweather
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D02014X/1Medical Research Council G0701834Wellcome Trust
6 · The paper itself

Abstract

Clostridium difficile expresses a number of cell wall proteins, including the abundant high-molecular-weight and low-molecular-weight S-layer proteins (SLPs). These proteins are generated by posttranslational cleavage of the precursor SlpA by the cysteine protease Cwp84. We compared the phenotypes of C. difficile strains containing insertional mutations in either cwp84 or its paralog cwp13 and complemented with plasmids expressing wild-type or mutant forms of their genes. We show that the presence of uncleaved SlpA in the cell wall of the cwp84 mutant results in aberrant retention of other cell wall proteins at the cell surface, as demonstrated by secretion of the proteins Cwp66 and Cwp2 into the growth medium. These phenotypes are restored by complementation with a plasmid expressing wild-type Cwp84 enzyme but not with one encoding a Cys116Ala substitution in the active site. The cwp13 mutant cleaved the SlpA precursor normally and had a wild-type-like colony phenotype. Both Cwp84 and Cwp13 are produced as proenzymes which are processed by cleavage to produce mature enzymes. In the case of Cwp84, this cleavage does not appear to be autocatalytic, whereas in Cwp13 autocatalysis was demonstrated as a Cys109Ala mutant did not undergo processing. Cwp13 appears to have a role in processing of Cwp84 but is not essential for Cwp84 activity. Cwp13 cleaves SlpA in the HMW SLP domain, which we suggest may reflect a role in cleavage and degradation of misfolded proteins at the cell surface.

Indexed as

Amino Acid SequenceCell WallClostridioides difficileCysteine EndopeptidasesGene Knockout TechniquesGenetic Complementation TestMembrane ProteinsMolecular Sequence DataMutagenesis, InsertionalMutant ProteinsProtein Processing, Post-TranslationalCwp84 protein, Clostridium difficileCysteine EndopeptidasesMembrane ProteinsMutant Proteins

Identifiers

PMID21531808
PMCPMC3133288
OpenAlexW1997642820

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.