Evidence map›Paper›PMID 24453976›Full record

ArticlePLoS pathogens2014

Lu/BCAM adhesion glycoprotein is a receptor for Escherichia coli Cytotoxic Necrotizing Factor 1 (CNF1).

Marianne Piteau, Panagiotis Papatheodorou, Carsten Schwan, Andreas Schlosser, Klaus Aktories, Gudula Schmidt

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Effects of theInternational journal of molecular sciences · 2021
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Contribution of pks+Microorganisms · 2024
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Immunomodulatory properties of CNF1 toxin fromAmerican journal of cancer research · 2022
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Marianne PiteauInstitute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University of Freiburg, Freiburg, Germany ; Biological Faculty, Albert-Ludwigs-University of Freiburg, Freiburg, Germany.
Panagiotis PapatheodorouInstitute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University of Freiburg, Freiburg, Germany.
Carsten SchwanInstitute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University of Freiburg, Freiburg, Germany.
Andreas SchlosserRudolf-Virchow-Zentrum für Experimentelle Biomedizin, Universität Würzburg, Würzburg, Germany.
Klaus AktoriesInstitute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University of Freiburg, Freiburg, Germany ; BIOSS (Centre for Biological Signalling Studies), Freiburg, Germany.
Gudula SchmidtInstitute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University of Freiburg, Freiburg, Germany.
University of Freiburg · DEUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Cytotoxic Necrotizing Factor 1 (CNF1) is a protein toxin which is a major virulence factor of pathogenic Escherichia coli strains. Here, we identified the Lutheran (Lu) adhesion glycoprotein/basal cell adhesion molecule (BCAM) as cellular receptor for CNF1 by co-precipitation of cell surface molecules with tagged toxin. The CNF1-Lu/BCAM interaction was verified by direct protein-protein interaction analysis and competition studies. These studies revealed amino acids 720 to 1014 of CNF1 as the binding site for Lu/BCAM. We suggest two cell interaction sites in CNF1: first the N-terminus, which binds to p37LRP as postulated before. Binding of CNF1 to p37LRP seems to be crucial for the toxin's action. However, it is not sufficient for the binding of CNF1 to the cell surface. A region directly adjacent to the catalytic domain is a high affinity interaction site for Lu/BCAM. We found Lu/BCAM to be essential for the binding of CNF1 to cells. Cells deficient in Lu/BCAM but expressing p37LRP could not bind labeled CNF1. Therefore, we conclude that LRP and Lu/BCAM are both required for toxin action but with different functions.

Indexed as

Bacterial ToxinsCell Adhesion MoleculesEscherichia coliEscherichia coli ProteinsHEK293 CellsHeLa CellsHumansLutheran Blood-Group SystemProtein BindingProtein Structure, TertiaryVirulence FactorsBacterial ToxinsBCAM protein, humanCell Adhesion Moleculescytotoxic necrotizing factor type 1Escherichia coli ProteinsLutheran Blood-Group SystemVirulence Factors

Identifiers

PMID24453976
PMCPMC3894216
OpenAlexW1987393474

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.