Evidence map›Paper›PMID 26627825›Full record

ArticleThe Journal of biological chemistry2016

Extracellular Fibrinogen-binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet-Leukocyte Complexes.

Mareike G Posner, Abhishek Upadhyay, Aisha Alsheikh Abubaker, Tiago M Fortunato, Dina Vara, Ilaria Canobbio, Stefan Bagby, Giordano Pula

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. 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
1.2field-weighted citation impact, top 21% 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, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Antibodies to coagulase ofFrontiers in immunology · 2023
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  8. Review
  9. Multimerin-1 and cancer: a review.Bioscience reports · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Transcriptomic Adjustments ofFrontiers in microbiology · 2019
    Article
  14. Review
  15. Characterization of Foodborne Strains ofFrontiers in microbiology · 2017
    Article
  16. 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

8 authors at 3 institutions in 3 countries.

Mareike G PosnerFrom the Departments of Biology and Biochemistry and.
Abhishek UpadhyayFrom the Departments of Biology and Biochemistry and.
Aisha Alsheikh AbubakerPharmacy and Pharmacology, University of Bath, Bath BA2 7AY, United Kingdom and.
Tiago M FortunatoPharmacy and Pharmacology, University of Bath, Bath BA2 7AY, United Kingdom and.
Dina VaraPharmacy and Pharmacology, University of Bath, Bath BA2 7AY, United Kingdom and.
Ilaria Canobbiothe Department of Biology and Biotechnology, University of Pavia, 27100 Pavia PV, Italy.
Stefan BagbyFrom the Departments of Biology and Biochemistry and bsssb@bath.ac.uk.
Giordano PulaPharmacy and Pharmacology, University of Bath, Bath BA2 7AY, United Kingdom and.
University of Bath · GBLaboratoire de Biochimie · FRUniversity of Pavia · IT

Funding

Biotechnology and Biological Sciences Research Council BB/J002690/1Biotechnology and Biological Sciences Research Council BB/J008176/1British Heart Foundation PG/15/40/31522Wellcome Trust ZR-W0258A
6 · The paper itself

Abstract

Extracellular fibrinogen-binding protein (Efb) from Staphylococcus aureus inhibits platelet activation, although its mechanism of action has not been established. In this study, we discovered that the N-terminal region of Efb (Efb-N) promotes platelet binding of fibrinogen and that Efb-N binding to platelets proceeds via two independent mechanisms: fibrinogen-mediated and fibrinogen-independent. By proteomic analysis of Efb-interacting proteins within platelets and confirmation by pulldown assays followed by immunoblotting, we identified P-selectin and multimerin-1 as novel Efb interaction partners. The interaction of both P-selectin and multimerin-1 with Efb is independent of fibrinogen. We focused on Efb interaction with P-selectin. Excess of P-selectin extracellular domain significantly impaired Efb binding by activated platelets, suggesting that P-selectin is the main receptor for Efb on the surface of activated platelets. Efb-N interaction with P-selectin inhibited P-selectin binding to its physiological ligand, P-selectin glycoprotein ligand-1 (PSGL-1), both in cell lysates and in cell-free assays. Because of the importance of P-selectin-PSGL-1 binding in the interaction between platelets and leukocytes, we tested human whole blood and found that Efb abolishes the formation of platelet-monocyte and platelet-granulocyte complexes. In summary, we present evidence that in addition to its documented antithrombotic activity, Efb can play an immunoregulatory role via inhibition of P-selectin-PSGL-1-dependent formation of platelet-leukocyte complexes.

Indexed as

Bacterial ProteinsBlood PlateletsBlood ProteinsHumansMembrane GlycoproteinsMonocytesP-SelectinStaphylococcus aureusBacterial ProteinsBlood ProteinsEfb protein, Staphylococcus aureusMembrane GlycoproteinsmultimerinP-SelectinP-selectin ligand proteinbacterial pathogenesisfibrinogenmonocyteneutrophilplateletprotein-protein interactionsproteomicsP-selectinPSGL-1Staphylococcus aureus (S. aureus)

Identifiers

PMID26627825
PMCPMC4742742
OpenAlexW2265165715

What OpenQuestion holds

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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.