Evidence map›Paper›PMID 28669526›Full record

ArticleCell chemical biology2017

Attenuating Staphylococcus aureus Virulence by Targeting Flotillin Protein Scaffold Activity.

Gudrun Koch, Charlotte Wermser, Ivan C Acosta, Lara Kricks, Stephanie T Stengel, Ana Yepes, Daniel Lopez

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-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

29 citing papers in PubMed, 43 citations in OpenAlex.

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  6. Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025
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  15. Article
  16. Moonlighting inMicroorganisms · 2021
    Review
  17. Article
  18. Frontiers in microbiology · 2021
    Article
  19. SFPH proteins as therapeutic targets for a myriad of diseases.Bioorganic & medicinal chemistry letters · 2020
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Gudrun KochResearch Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
Charlotte WermserResearch Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
Ivan C AcostaNational Centre for Biotechnology (CNB), Spanish Research Council (CSIC), Darwin 3, Madrid 28049, Spain.
Lara KricksNational Centre for Biotechnology (CNB), Spanish Research Council (CSIC), Darwin 3, Madrid 28049, Spain.
Stephanie T StengelResearch Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
Ana YepesResearch Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany.
Daniel LopezResearch Centre for Infectious Diseases (ZINF), University of Würzburg, Würzburg 97080, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, Würzburg 97080, Germany; National Centre for Biotechnology (CNB), Spanish Research Council (CSIC), Darwin 3, Madrid 28049, Spain. Electronic address: dlopez@cnb.csic.es.
University of Würzburg · DECentro Nacional de Biotecnología · ES

Funding

European Research Council 335568
6 · The paper itself

Abstract

Scaffold proteins are ubiquitous chaperones that bind proteins and facilitate physical interaction of multi-enzyme complexes. Here we used a biochemical approach to dissect the scaffold activity of the flotillin-homolog protein FloA of the multi-drug-resistant human pathogen Staphylococcus aureus. We show that FloA promotes oligomerization of membrane protein complexes, such as the membrane-associated RNase Rny, which forms part of the RNA-degradation machinery called the degradosome. Cells lacking FloA had reduced Rny function and a consequent increase in the targeted sRNA transcripts that negatively regulate S. aureus toxin expression. Small molecules that altered FloA oligomerization also reduced Rny function and decreased the virulence potential of S. aureus in vitro, as well as in vivo, using invertebrate and murine infection models. Our results suggest that flotillin assists in the assembly of protein complexes involved in S. aureus virulence, and could thus be an attractive target for the development of new antimicrobial therapies.

Indexed as

VirulenceAnimalsBacterial ProteinsDisease Models, AnimalDrug Resistance, Multiple, BacterialEndoribonucleasesFemaleMembrane MicrodomainsMembrane ProteinsMiceMice, Inbred BALB CPhosphorylcholineProtein MultimerizationRNA, BacterialRNA, Ribosomal, 5SSmall Molecule LibrariesBacterial ProteinsEndoribonucleasesflotillinsMembrane ProteinsmiltefosinePhosphorylcholineRNA, BacterialRNA, Ribosomal, 5SSmall Molecule Librariesflotillinmembrane organizationRnyStaphylococcus

Identifiers

PMID28669526
PMCPMC5536197
OpenAlexW2730854633

What OpenQuestion holds

Textmetadata
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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.