Evidence map›Paper›PMID 16040989›Full record

ArticleInfection and immunity2005

Pathoadaptive mutation that mediates adherence of shiga toxin-producing Escherichia coli O111.

Alfredo G Torres, Roberto C Vazquez-Juarez, Christopher B Tutt, J Gerardo Garcia-Gallegos

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-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

16 citing papers in PubMed, 38 citations in OpenAlex.

  1. Cadaverine Is a Switch in the Lysine Degradation Pathway inFrontiers in cellular and infection microbiology · 2022
    Article
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  3. Review
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  6. Review
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  8. Review
  9. Intestinal barrier: A gentlemen's agreement between microbiota and immunity.World journal of gastrointestinal pathophysiology · 2014
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Physiological polyamines: simple primordial stress molecules.Journal of cellular and molecular medicine
    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 2 countries.

Alfredo G TorresDepartment of Microbiology and Immunology and Department of Pathology and Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston, TX 77555-1070, USA. altorres@utmb.edu
Roberto C Vazquez-Juarez
Christopher B Tutt
J Gerardo Garcia-Gallegos
The University of Texas Medical Branch at Galveston · USCentro de Investigaciones Biológicas Margarita Salas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The adherence of pathogenic Escherichia coli strains to intestinal epithelium is essential for initiation of infection. The cad operon encodes the lysine decarboxylase (LDC) system responsible for metabolizing lysine, and this operon has been proposed as an antivirulence mechanism in enteroinvasive E. coli and Shigella flexneri and as a factor mediating E. coli O157:H7 adherence. We sought to determine whether the LDC activity was present in a phylogenetically characterized collection of diarrheagenic E. coli (DEC) strains and to establish whether its expression was associated with their adherence to tissue culture cells. LDC activity was found in most of the pathogenic E. coli strains tested and was absent from Shiga toxin-producing E. coli (STEC) O111 strains (DEC pathotype 8). Analysis of the cad region in these O111 strains indicates that the operon has been rearranged and some of the genes are either missing or disrupted. A similar rearrangement was found in an E. coli O111:H8 strain recently isolated from an outbreak in Texas. Complementation of the LDC-negative strains with the cad operon in trans restored the LDC activity and resulted in a reduction in adherence to tissue culture cells. Initial analysis of the protein profiles on the surface of the O111 strains indicates that the LDC activity has an effect on the expression of the adhesin intimin. Cadaverine had a slight effect on LDC-negative strain adhesion but none on intimin expression. Our data suggest that this pathoadaptive mutation is an important mechanism to control functions potentially implicated in the pathogenesis of these organisms.

Indexed as

Adhesins, BacterialBacterial AdhesionCadaverineCarboxy-LyasesEscherichia coliEscherichia coli ProteinsHeLa CellsHumansLysineSequence Analysis, DNAShiga ToxinAdhesins, BacterialCadaverineCarboxy-LyaseseaeA protein, E coliEscherichia coli ProteinsLysinelysine decarboxylaseShiga Toxin

Identifiers

PMID16040989
PMCPMC1201210
OpenAlexW2098432784

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.