Evidence map›Paper›PMID 24292100›Full record

ArticleScientific reports2013

P-fimbriae in the presence of anti-PapA antibodies: new insight of antibodies action against pathogens.

Narges Mortezaei, Bhupender Singh, Esther Bullitt, Bernt Eric Uhlin, Magnus Andersson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

10 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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 2 institutions in 2 countries.

Narges Mortezaei1] Department of Physics, Umeå University, SE-901 87 Umeå, Sweden [2].
Bhupender Singh
Esther Bullitt
Bernt Eric Uhlin
Magnus Andersson
Umeå University · SEBoston University · US

Funding

STRUCTURE/FUNCTION OF BACTERIAL ADHESION PILIR01GM055722 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BULLITT, ESTHER · 1998 to 2009
$2.1M
NIGMS NIH HHS R01 GM055722
6 · The paper itself

Abstract

Uropathogenic strains of Escherichia coli establish urinary tract infections by attaching to host epithelial cells using adhesive organelles called fimbriae. Fimbriae are helix-like structures with a remarkable adaptability, offering safeguarding for bacteria exposed to changing fluid forces in the urinary tract. We challenged this property of P-fimbriae by cross-linking their subunits with shaft-specific antibodies and measuring the corresponding force response at a single organelle level. Our data show compromised extension and rewinding of P-fimbriae in the presence of antibodies and reduced fimbrial elasticity, which are important properties of fimbriae contributing to the ability of bacteria to cause urinary tract infections. The reduced elasticity found by cross-linking fimbrial subunits could thus be another assignment for antibodies; in addition to marking bacteria as foreign, antibodies physically compromise fimbrial function. We suggest that our assay and results will be a starting point for further investigations aimed at inhibiting sustained bacterial adhesion by antibodies.

Indexed as

AntibodiesBacterial AdhesionEpithelial CellsEscherichia coliEscherichia coli ProteinsFimbriae, BacterialFimbriae ProteinsProtein Structure, SecondaryUrinary Tract InfectionsAntibodiesAtpA protein, E coliEscherichia coli ProteinsFimbriae Proteins

Identifiers

PMID24292100
PMCPMC3848023
OpenAlexW2132131826

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.