Evidence map›Paper›PMID 21708988›Full record

ArticleInfection and immunity2011

Long polar fimbriae of enterohemorrhagic Escherichia coli O157:H7 bind to extracellular matrix proteins.

Mauricio J Farfan, Lidia Cantero, Roberto Vidal, Douglas J Botkin, Alfredo G Torres

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Shiga-Toxin-Producing Strains ofMicroorganisms · 2023
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  5. The EcpD Tip Adhesin of theInternational journal of molecular sciences · 2022
    Article
  6. Article
  7. Shiga Toxin-ProducingMicroorganisms · 2022
    Review
  8. Article
  9. Article
  10. Genomic Epidemiology of Shiga Toxin-ProducingAnimals : an open access journal from MDPI · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  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

5 authors at 3 institutions in 2 countries.

Mauricio J FarfanCentro de Estudios Moleculares, Departamento de Pediatría, Hospital Dr. Luis Calvo Mackenna, Santiago, Chile. mfarfan@med.uchile.cl
Lidia Cantero
Roberto Vidal
Douglas J Botkin
Alfredo G Torres
The University of Texas Medical Branch at Galveston · USUniversity of Chile · CLHospital Luis Calvo Mackenna · CL

Funding

Training in Emerging Infectious Diseases and BiodefenseT32AI007536 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI WHITE, ARTHUR CLINTON · 1998 to 2013
$4.1M
Long Polar Fimbriae of Attaching and Effacing Escherichia coliR01AI079154 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI TORRES, ALFREDO G · 2009 to 2013
$1.9M
NIAID NIH HHS 5R01AI079154-03NIAID NIH HHS 5-T32-AI007536-12NIAID NIH HHS R01 AI079154NIAID NIH HHS T32 AI007536
6 · The paper itself

Abstract

Adherence to intestinal cells is a key process in infection caused by enterohemorrhagic Escherichia coli (EHEC). Several adhesion factors that mediate the binding of EHEC to intestinal cells have been described, but the receptors involved in their recognition are not fully characterized. Extracellular matrix (ECM) proteins might act as receptors involved in the recognition of enteric pathogens, including EHEC. In this study, we sought to characterize the binding of EHEC O157:H7 to ECM proteins commonly present in the intestine. We found that EHEC prototype strains as well as other clinical isolates adhered more abundantly to surfaces coated with fibronectin, laminin, and collagen IV. Further characterization of this phenotype, by using antiserum raised against the LpfA1 putative major fimbrial subunit and by addition of mannose, showed that a reduced binding of EHEC to ECM proteins was observed in a long polar fimbria (lpf) mutant. We also found that the two regulators, H-NS and Ler, had an effect in EHEC Lpf-mediated binding to ECM, supporting the roles of these tightly regulated fimbriae as adherence factors. Purified Lpf major subunit bound to all of the ECM proteins tested. Finally, increased bacterial adherence was observed when T84 cells, preincubated with ECM proteins, were infected with EHEC. Taken together, these findings suggest that the interaction of Lpf and ECM proteins contributes to the EHEC colonization of the gastrointestinal tract.

Indexed as

Bacterial AdhesionAntibodiesBacterial ProteinsCell Line, TumorCollagen Type IVDNA-Binding ProteinsEnzyme-Linked Immunosorbent AssayEscherichia coli O157Escherichia coli ProteinsExtracellular Matrix ProteinsFibronectinsFimbriae, BacterialFimbriae ProteinsHumansIntestinal MucosaIntestinesAntibodiesBacterial ProteinsCollagen Type IVDNA-Binding ProteinsEscherichia coli ProteinsExtracellular Matrix ProteinsFibronectinsFimbriae ProteinsH-NS protein, bacteriaLamininLer protein, E coliRecombinant ProteinsTrans-Activators

Identifiers

PMID21708988
PMCPMC3165468
OpenAlexW2149594409

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.