Evidence map›Paper›PMID 10948163›Full record

ArticleInfection and immunity2000

Apically exposed, tight junction-associated beta1-integrins allow binding and YopE-mediated perturbation of epithelial barriers by wild-type Yersinia bacteria.

F Tafazoli, A Holmström, A Forsberg, K E Magnusson

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Mechanosensory entities and functionality of endothelial cells.Frontiers in cell and developmental biology · 2024
    Review
  3. mBio · 2023
    Article
  4. bioRxiv : the preprint server for biology · 2023
    Article
  5. Review
  6. Above the Matrix: Functional Roles for Apically Localized Integrins.Frontiers in cell and developmental biology · 2021
    Review
  7. Modulation of epithelial cell polarity by bacterial pathogens.Annals of the New York Academy of Sciences · 2017
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  20. Type III secretion systems and disease.Clinical microbiology reviews · 2007
    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

4 authors at 2 institutions in 1 country.

F TafazoliDivision of Medical Microbiology, Department of Health and Environment, Linköping University, S-581 85 Linköping, Sweden. farta@mme.liu.se
A Holmström
A Forsberg
K E Magnusson
Linköping University · SESwedish Defence Research Agency · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using polarized epithelial cells, primarily MDCK-1, we assessed the mode of binding and effects on epithelial cell structure and permeability of Yersinia pseudotuberculosis yadA-deficient mutants. Initially, all bacteria except the invasin-deficient (inv) mutant adhered apically to the tight junction areas. These contact points of adjacent cells displayed beta1-integrins together with tight junction-associated ZO-1 and occludin proteins. Indeed, beta1-integrin expression was maximal in the tight junction area and then gradually decreased along the basolateral membranes. Wild-type bacteria also opened gradually the tight junction to paracellular permeation of different-sized markers, viz., 20-, 40-, and 70-kDa dextrans and 45-kDa ovalbumin, as well as to their own translocation between adjacent cells in intimate contact with beta1-integrins. The effects on the epithelial cells and their barrier properties could primarily be attributed to expression of the Yersinia outer membrane protein YopE, as the yopE mutant bound but caused no cytotoxicity. Moreover, the apical structure of filamentous actin (F-actin) was disturbed and tight junction-associated proteins (ZO-1 and occludin) were dispersed along the basolateral membranes. It is concluded that the Yersinia bacteria attach to beta1-integrins at tight junctions. Via this localized injection of YopE, they perturb the F-actin structure and distribution of proteins forming and regulating tight junctions. Thereby they promote paracellular translocation of bacteria and soluble compounds.

Indexed as

Bacterial AdhesionAnimalsBacterial Outer Membrane ProteinsCell LineCell PolarityDogsEpithelial CellsIntegrin beta1Membrane ProteinsOccludinPermeabilityPhosphoproteinsTight JunctionsYersinia pseudotuberculosisZonula Occludens-1 ProteinBacterial Outer Membrane ProteinsIntegrin beta1Membrane ProteinsOccludinPhosphoproteinsyopE protein, YersiniaZonula Occludens-1 Protein

Identifiers

PMID10948163
PMCPMC101797
OpenAlexW2144750575

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.