Evidence map›Paper›PMID 16428775›Full record

ArticleInfection and immunity2006

The established intimin receptor Tir and the putative eucaryotic intimin receptors nucleolin and beta1 integrin localize at or near the site of enterohemorrhagic Escherichia coli O157:H7 adherence to enterocytes in vivo.

James F Sinclair, Evelyn A Dean-Nystrom, Alison D O'Brien

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.9field-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, 53 citations in OpenAlex.

  1. Article
  2. ThemSphere · 2024
    Article
  3. Nucleolin: a cell portal for viruses, bacteria, and toxins.Cellular and molecular life sciences : CMLS · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. A new twist on plasma membrane repair.Communicative & integrative biology · 2011
    Article
  17. Review
  18. Article
  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

3 authors at 2 institutions in 1 country.

James F SinclairDepartment of Microbiology and Immunology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Rd., Bethesda, MD 20814, USA.
Evelyn A Dean-Nystrom
Alison D O'Brien
Uniformed Services University of the Health Sciences · USAgricultural Research Service · US

Funding

Pathogenicity of Shiga Toxin Producing E.coliR37AI020148 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI O'BRIEN, ALISON DAVIS · 2008 to 2016
$3.8M
SHIGA-LIKE TOXIN OF ESCHERICHIA COLIR01AI020148 · NIAID · U.S. UNIFORMED SERVICES UNIV OF HLTH SCI · PI MELTON-CELSA, ANGELA · 1987 to 2017
$3.3M
SHIGA-LIKE TOXIN OF ESCHERICHIA COLIR22AI020148 · NIAID · U.S. UNIFORMED SERVICES UNIV OF HLTH SCI · PI O'BRIEN, ALISON DAVIS · 1985 to 1991
–
NIAID NIH HHS AI 20148-22NIAID NIH HHS R01 AI020148NIAID NIH HHS R37 AI020148
6 · The paper itself

Abstract

For enterohemorrhagic Escherichia coli (EHEC) O157:H7 to adhere tightly to the intestinal epithelium and produce attach and efface (A/E) lesions, the organism must express the adhesin intimin and insert the bacterially encoded translocated intimin receptor Tir into the plasma membrane of the host enterocyte. Additionally, some reports based on tissue culture experiments indicate that intimin has affinity for the eucaryotic proteins nucleolin and beta1 integrin. To address the potential biological relevance of these eucaryotic proteins in the infection process in vivo, we sought to compare the proximity of Tir, nucleolin, and beta1 integrin to regions of EHEC O157:H7 attachment in intestinal sections from three different inoculated animals: piglets, neonatal calves, and mice. Piglets and neonatal calves were chosen because intimin-mediated adherence of EHEC O157:H7 and subsequent A/E lesion formation occur at high levels in these animals. Mice were selected because of their ease of manipulation but only after we first demonstrated that in competition with the normal mouse gut flora, an EHEC O157:H7 strain with a nonpolar deletion in the intimin gene was cleared faster than strains that produced wild-type or hybrid intimin. In all three animal species, we noted immunostained Tir beneath and stained nucleolin closely associated with adherent bacteria in intestinal sections. We also observed immunostained beta1 integrin clustered at locations of bacterial adherence in porcine and bovine tissue. These findings indicate that nucleolin and beta1 integrin are present on the luminal surface of intestinal epithelia and are potentially accessible as receptors for intimin during EHEC O157:H7 infection.

Indexed as

Bacterial AdhesionAdhesins, BacterialAnimalsAnimals, NewbornCattleCattle DiseasesEnterocytesEscherichia coli InfectionsEscherichia coli O157Escherichia coli ProteinsFluorescent Antibody TechniqueGene DeletionHumansIntegrin beta1MiceMice, Inbred BALB CAdhesins, BacterialeaeA protein, E coliEscherichia coli ProteinsIntegrin beta1NucleolinPhosphoproteinsReceptors, Cell SurfaceRNA-Binding ProteinsTir protein, E coli

Identifiers

PMID16428775
PMCPMC1360320
OpenAlexW2166266726

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.