Evidence map›Paper›PMID 24627488›Full record

ArticleThe Journal of biological chemistry2014

Evidence for steric regulation of fibrinogen binding to Staphylococcus aureus fibronectin-binding protein A (FnBPA).

Vaclav Stemberk, Richard P O Jones, Olga Moroz, Kate E Atkin, Andrew M Edwards, Johan P Turkenburg, Andrew P Leech, Ruth C Massey, Jennifer R Potts

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Targeted and quantitatively modeled biologic delivery via dual-functional probiotic yeast in inflammatory bowel disease.Journal of controlled release : official journal of the Controlled Release Society · 2026
    Article
  3. Article
  4. Article
  5. The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. The Two-Track Investigation of Fibronectin Binding Protein A ofInternational journal of molecular sciences · 2023
    Article
  8. Interaction of theACS nanoscience Au · 2023
    Article
  9. Adhesive Virulence Factors ofACS bio & med chem Au · 2022
    Article
  10. Article
  11. Mechanical Stabilization of a Bacterial Adhesion Complex.Journal of the American Chemical Society · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Biological characteristics and conjugated antigens of ClfA A-FnBPA and CP5 inCanadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2018
    Article
  19. Article
  20. The remarkably multifunctional fibronectin binding proteins of Staphylococcus aureus.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016
    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

9 authors at 2 institutions in 1 country.

Vaclav StemberkFrom the Departments of Biology and.
Richard P O Jones
Olga Moroz
Kate E Atkin
Andrew M Edwards
Johan P Turkenburg
Andrew P Leech
Ruth C Massey
Jennifer R Potts
University of Bath · GBUniversity of York · GB

Funding

Biotechnology and Biological Sciences Research CouncilBritish Heart Foundation FS/07/034/22969British Heart Foundation FS/12/36/29588British Heart Foundation PG/09/079/28008Medical Research Council MR/J006874/1
6 · The paper itself

Abstract

The adjacent fibrinogen (Fg)- and fibronectin (Fn)-binding sites on Fn-binding protein A (FnBPA), a cell surface protein from Staphylococcus aureus, are implicated in the initiation and persistence of infection. FnBPA contains a single Fg-binding site (that also binds elastin) and multiple Fn-binding sites. Here, we solved the structure of the N2N3 domains containing the Fg-binding site of FnBPA in the apo form and in complex with a Fg peptide. The Fg binding mechanism is similar to that of homologous bacterial proteins but without the requirement for "latch" strand residues. We show that the Fg-binding sites and the most N-terminal Fn-binding sites are nonoverlapping but in close proximity. Although Fg and a subdomain of Fn can form a ternary complex on an FnBPA protein construct containing a Fg-binding site and single Fn-binding site, binding of intact Fn appears to inhibit Fg binding, suggesting steric regulation. Given the concentrations of Fn and Fg in the plasma, this mechanism might result in targeting of S. aureus to fibrin-rich thrombi or elastin-rich tissues.

Indexed as

Adhesins, BacterialAmino Acid SequenceBinding SitesCrystallography, X-RayFibrinogenFibronectinsHumansModels, MolecularMolecular Sequence DataPeptidesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryStaphylococcus aureusSurface Plasmon ResonanceAdhesins, BacterialFibrinogenfibronectin-binding proteins, bacterialFibronectinsPeptidesFibrinogenFibronectinFnBPAIsothermal Titration CalorimetryStaphylococcus aureusSurface Plasmon Resonance (SPR)X-ray Crystallography

Identifiers

PMID24627488
PMCPMC4007472
OpenAlexW1973479917

What OpenQuestion holds

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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.