Evidence map›Paper›PMID 22691138›Full record

ArticleBMC microbiology2012

Proteins other than the locus of enterocyte effacement-encoded proteins contribute to Escherichia coli O157:H7 adherence to bovine rectoanal junction stratified squamous epithelial cells.

Indira T Kudva, Robert W Griffin, Bryan Krastins, David A Sarracino, Stephen B Calderwood, Manohar John

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  8. Nonfimbrial Adhesin Mutants Reveal DivergentInternational journal of microbiology · 2021
    Article
  9. Review
  10. Article
  11. SupershedInternational journal of microbiology · 2020
    Article
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  13. Article
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  15. Article
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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

6 authors at 3 institutions in 1 country.

Indira T KudvaFood Safety and Enteric Pathogens Research Unit, National Animal Disease Center, Agricultural Research Service, US Department of Agriculture, Ames, Iowa 50010, USA. Indira.Kudva@ars.usda.gov
Robert W Griffin
Bryan Krastins
David A Sarracino
Stephen B Calderwood
Manohar John
Massachusetts General Hospital · USCenter for Human Genetics · USNational Animal Disease Center · US

Funding

E. coli O157:H7 genes induced during human infectionR21AI055963 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI KUDVA, INDIRA T · 2004 to 2005
$698k
NIAID NIH HHS R21 AI055963
6 · The paper itself

Abstract

backgroundIn this study, we present evidence that proteins encoded by the Locus of Enterocyte Effacement (LEE), considered critical for Escherichia coli O157 (O157) adherence to follicle-associated epithelial (FAE) cells at the bovine recto-anal junction (RAJ), do not appear to contribute to O157 adherence to squamous epithelial (RSE) cells also constituting this primary site of O157 colonization in cattle.

resultsAntisera targeting intimin-γ, the primary O157 adhesin, and other essential LEE proteins failed to block O157 adherence to RSE cells, when this pathogen was grown in DMEM, a culture medium that enhances expression of LEE proteins. In addition, RSE adherence of a DMEM-grown-O157 mutant lacking the intimin protein was comparable to that seen with its wild-type parent O157 strain grown in the same media. These adherence patterns were in complete contrast to that observed with HEp-2 cells (the adherence to which is mediated by intimin-γ), assayed under same conditions. This suggested that proteins other than intimin-γ that contribute to adherence to RSE cells are expressed by this pathogen during growth in DMEM. To identify such proteins, we defined the proteome of DMEM-grown-O157 (DMEM-proteome). GeLC-MS/MS revealed that the O157 DMEM-proteome comprised 684 proteins including several components of the cattle and human O157 immunome, orthologs of adhesins, hypothetical secreted and outer membrane proteins, in addition to the known virulence and LEE proteins. Bioinformatics-based analysis of the components of the O157 DMEM proteome revealed several new O157-specific proteins with adhesin potential.

conclusionProteins other than LEE and intimin-γ proteins are involved in O157 adherence to RSE cells at the bovine RAJ. Such proteins, with adhesin potential, are expressed by this human pathogen during growth in DMEM. Ongoing experiments to evaluate their role in RSE adherence should provide both valuable insights into the O157-RSE interactions and new targets for more efficacious anti-adhesion O157 vaccines.

Indexed as

Bacterial AdhesionAdhesins, BacterialAnimalsCattleCell LineElectrophoresisEpithelial CellsEscherichia coli O157Escherichia coli ProteinsHumansProteomeTandem Mass SpectrometryAdhesins, BacterialEscherichia coli ProteinsProteome

Identifiers

PMID22691138
PMCPMC3420319
OpenAlexW2160705782

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.