Evidence map›Paper›PMID 31201325›Full record

ArticleNature communications2019

The pore structure of Clostridium perfringens epsilon toxin.

Christos G Savva, Alice R Clark, Claire E Naylor, Michel R Popoff, David S Moss, Ajit K Basak, Richard W Titball, Monika Bokori-Brown

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. A Comprehensive Structural and Functional Analysis ofbioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Cytotoxic effects of epsilon toxin fromToxicology research · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Computational and structural biotechnology journal · 2025
    Article
  13. Article
  14. Article
  15. Microorganisms · 2024
    Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review
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

8 authors at 6 institutions in 2 countries.

Christos G SavvaLeicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester, LE1 7HB, UK.
Alice R ClarkFaculty of Science and Engineering, University of Wolverhampton, Wulfruna Street, Wolverhampton, WV1 1LY, UK.
Claire E NaylorMolecular Dimensions, Willie Snaith Road, Newmarket, CB8 7SQ, UK.
Michel R PopoffBactéries Anaérobies et Toxines, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724, Paris Cedex 15, France.
David S MossDepartment of Biological Sciences, Birkbeck College, Malet Street, London, WC1E 7HX, UK.
Ajit K BasakDepartment of Biological Sciences, Birkbeck College, Malet Street, London, WC1E 7HX, UK.
Richard W TitballCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK.
Monika Bokori-BrownCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK. m.bokori-brown@exeter.ac.uk.ORCID http://orcid.org/0000-0002-9540-5590
Birkbeck, University of London · GBUniversity of Exeter · GBInstitut Pasteur · FRMolecular DimensionsUniversity of Leicester · GBUniversity of Wolverhampton · GB

Funding

Medical Research Council MC_PC_17136RCUK | Medical Research Council (MRC) MC-A021-53019Wellcome TrustWellcome Trust (Wellcome) WT089618MA
6 · The paper itself

Abstract

Epsilon toxin (Etx), a potent pore forming toxin (PFT) produced by Clostridium perfringens, is responsible for the pathogenesis of enterotoxaemia of ruminants and has been suggested to play a role in multiple sclerosis in humans. Etx is a member of the aerolysin family of β-PFTs (aβ-PFTs). While the Etx soluble monomer structure was solved in 2004, Etx pore structure has remained elusive due to the difficulty of isolating the pore complex. Here we show the cryo-electron microscopy structure of Etx pore assembled on the membrane of susceptible cells. The pore structure explains important mutant phenotypes and suggests that the double β-barrel, a common feature of the aβ-PFTs, may be an important structural element in driving efficient pore formation. These insights provide the framework for the development of novel therapeutics to prevent human and animal infections, and are relevant for nano-biotechnology applications.

Indexed as

AnimalsBacterial ToxinsBiotechnologyCell LineClostridium InfectionsClostridium perfringensCryoelectron MicroscopyDogsEnterotoxemiaModels, MolecularMutagenesis, Site-DirectedNanotechnologyProtein Conformation, beta-StrandProtein MultimerizationRecombinant ProteinsBacterial ToxinsClostridium perfringens epsilon-toxinRecombinant Proteins

Identifiers

PMID31201325
PMCPMC6572795
OpenAlexW2952148325

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.