Evidence map›Paper›PMID 29103614›Full record

ArticleCell2017

Membrane Microdomain Disassembly Inhibits MRSA Antibiotic Resistance.

Esther García-Fernández, Gudrun Koch, Rabea M Wagner, Agnes Fekete, Stephanie T Stengel, Johannes Schneider, Benjamin Mielich-Süss, Sebastian Geibel, Sebastian M Markert, Christian Stigloher and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed
8.9field-weighted citation impact, top 1% 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

145 citing papers in PubMed, 249 citations in OpenAlex.

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  14. Sphingolipid-mediated vesiculation in multidrug-resistantApplied and environmental microbiology · 2025
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  17. Review
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  19. Review
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85 more citing papers are in PubMed but not listed here.

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

11 authors at 2 institutions in 2 countries.

Esther García-FernándezNational Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), 28049 Madrid, Spain.
Gudrun KochResearch Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany.
Rabea M WagnerNational Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), 28049 Madrid, Spain; Research Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany.
Agnes FeketeJulius-von-Sachs-Institute Biocenter, Pharmaceutical Biology, University of Würzburg, 97082 Würzburg, Germany.
Stephanie T StengelResearch Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany.
Johannes SchneiderResearch Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany.
Benjamin Mielich-SüssResearch Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany.
Sebastian GeibelResearch Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany.
Sebastian M MarkertDivision of Electron Microscopy, Biocenter, University of Würzburg, 97074 Würzburg, Germany.
Christian StigloherDivision of Electron Microscopy, Biocenter, University of Würzburg, 97074 Würzburg, Germany.
Daniel LopezNational Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), 28049 Madrid, Spain; Research Centre for Infectious Diseases (ZINF), University of Würzburg, 97080 Würzburg, Germany; Institute for Molecular Infection Biology (IMIB), University of Würzburg, 97080 Würzburg, Germany; National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Darwin 3, Campus de Cantoblanco, 28049 Madrid, Spain. Electronic address: dlopez@cnb.csic.es.
University of Würzburg · DECentro Nacional de Biotecnología · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of bacterial cell processes are confined functional membrane microdomains (FMMs), structurally and functionally similar to lipid rafts of eukaryotic cells. How bacteria organize these intricate platforms and what their biological significance is remain important questions. Using the pathogen methicillin-resistant Staphylococcus aureus (MRSA), we show here that membrane-carotenoid interaction with the scaffold protein flotillin leads to FMM formation, which can be visualized using super-resolution array tomography. These membrane platforms accumulate multimeric protein complexes, for which flotillin facilitates efficient oligomerization. One of these proteins is PBP2a, responsible for penicillin resistance in MRSA. Flotillin mutants are defective in PBP2a oligomerization. Perturbation of FMM assembly using available drugs interferes with PBP2a oligomerization and disables MRSA penicillin resistance in vitro and in vivo, resulting in MRSA infections that are susceptible to penicillin treatment. Our study demonstrates that bacteria possess sophisticated cell organization programs and defines alternative therapies to fight multidrug-resistant pathogens using conventional antibiotics.

Indexed as

AnimalsBacterial ProteinsCarotenoidsCell MembraneFemaleMembrane MicrodomainsMembrane ProteinsMethicillin-Resistant Staphylococcus aureusMiceMice, Inbred BALB CPenicillin-Binding ProteinsStaphylococcal InfectionsXanthophyllsBacterial ProteinsCarotenoidsflotillinsmecA protein, Staphylococcus aureusMembrane ProteinsPenicillin-Binding ProteinsstaphyloxanthinXanthophylls

Identifiers

PMID29103614
PMCPMC5720476
OpenAlexW2766734789

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.