Evidence map›Paper›PMID 29166667›Full record

ArticlePLoS pathogens2017

Flotillin scaffold activity contributes to type VII secretion system assembly in Staphylococcus aureus.

Benjamin Mielich-Süss, Rabea M Wagner, Nicole Mietrach, Tobias Hertlein, Gabriella Marincola, Knut Ohlsen, Sebastian Geibel, Daniel Lopez

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-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

30 citing papers in PubMed, 49 citations in OpenAlex.

  1. Host-driven remodelling of theMicrobiology (Reading, England) · 2026
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  5. Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025
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  8. Article
  9. Article
  10. Review
  11. Bacterial lipid biophysics and membrane organization.Current opinion in microbiology · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Type VII Secretion System ofAnnual review of microbiology · 2021
    Article
  18. Article
  19. Article
  20. Frontiers in microbiology · 2021
    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

8 authors at 2 institutions in 2 countries.

Benjamin Mielich-SüssResearch Center for Infectious Diseases ZINF, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0002-8276-1967
Rabea M WagnerResearch Center for Infectious Diseases ZINF, University of Würzburg, Würzburg, Germany.
Nicole MietrachResearch Center for Infectious Diseases ZINF, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0002-6885-1544
Tobias HertleinInstitute for Molecular Infection Biology IMIB, University of Würzburg, Würzburg, Germany.
Gabriella MarincolaResearch Center for Infectious Diseases ZINF, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0001-9227-6554
Knut OhlsenInstitute for Molecular Infection Biology IMIB, University of Würzburg, Würzburg, Germany.
Sebastian GeibelResearch Center for Infectious Diseases ZINF, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0003-0068-680X
Daniel LopezResearch Center for Infectious Diseases ZINF, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0002-8627-3813
University of Würzburg · DEConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scaffold proteins are ubiquitous chaperones that promote efficient interactions between partners of multi-enzymatic protein complexes; although they are well studied in eukaryotes, their role in prokaryotic systems is poorly understood. Bacterial membranes have functional membrane microdomains (FMM), a structure homologous to eukaryotic lipid rafts. Similar to their eukaryotic counterparts, bacterial FMM harbor a scaffold protein termed flotillin that is thought to promote interactions between proteins spatially confined to the FMM. Here we used biochemical approaches to define the scaffold activity of the flotillin homolog FloA of the human pathogen Staphylococcus aureus, using assembly of interacting protein partners of the type VII secretion system (T7SS) as a case study. Staphylococcus aureus cells that lacked FloA showed reduced T7SS function, and thus reduced secretion of T7SS-related effectors, probably due to the supporting scaffold activity of flotillin. We found that the presence of flotillin mediates intermolecular interactions of T7SS proteins. We tested several small molecules that interfere with flotillin scaffold activity, which perturbed T7SS activity in vitro and in vivo. Our results suggest that flotillin assists in the assembly of S. aureus membrane components that participate in infection and influences the infective potential of this pathogen.

Indexed as

Staphylococcus aureusBacillus subtilisBacterial ProteinsGene Expression Regulation, BacterialHumansMembrane MicrodomainsMembrane ProteinsStaphylococcal InfectionsType VII Secretion SystemsBacterial ProteinsflotillinsMembrane ProteinsType VII Secretion Systems

Identifiers

PMID29166667
PMCPMC5718613
OpenAlexW2770145234

What OpenQuestion holds

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LicenceCC BY
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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.