Evidence map›Paper›PMID 37486930›Full record

ArticlePLoS pathogens2023

Metabolic reprogramming and altered cell envelope characteristics in a pentose phosphate pathway mutant increases MRSA resistance to β-lactam antibiotics.

Merve S Zeden, Laura A Gallagher, Emilio Bueno, Aaron C Nolan, Jongsam Ahn, Dhananjay Shinde, Fareha Razvi, Margaret Sladek, Órla Burke, Eoghan O'Neill and 4 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mutation of lipoprotein processing pathway geneAntimicrobial agents and chemotherapy · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Antibiotics (Basel, Switzerland) · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Evolution of polyamine resistance inbioRxiv : the preprint server for biology · 2024
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 3 countries.

Merve S ZedenMicrobiology, School of Biological and Chemical Sciences, University of Galway, Galway, Ireland.ORCID 0000-0003-3636-700X
Laura A GallagherMicrobiology, School of Biological and Chemical Sciences, University of Galway, Galway, Ireland.
Emilio BuenoDepartment of Molecular Biology, Umeå University, MIMS-Laboratory for Molecular Infection Medicine Sweden, Umeå, Sweden.
Aaron C NolanMicrobiology, School of Biological and Chemical Sciences, University of Galway, Galway, Ireland.
Jongsam AhnDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Dhananjay ShindeDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Fareha RazviDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Margaret SladekDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Órla BurkeMicrobiology, School of Biological and Chemical Sciences, University of Galway, Galway, Ireland.
Eoghan O'NeillDepartment of Clinical Microbiology, Royal College of Surgeons in Ireland, Dublin, Ireland.
Paul D FeyDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Felipe CavaDepartment of Molecular Biology, Umeå University, MIMS-Laboratory for Molecular Infection Medicine Sweden, Umeå, Sweden.
Vinai C ThomasDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
James P O'GaraMicrobiology, School of Biological and Chemical Sciences, University of Galway, Galway, Ireland.ORCID 0000-0003-3866-7161
University of Nebraska Medical Center · USOllscoil na Gaillimhe – University of Galway · IEUmeå University · SERoyal College of Surgeons in Ireland · IE

Funding

The S. aureus biofilm lifecycleP01AI083211 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI KIELIAN, TAMMY L · 2009 to 2023
$32.1M
The role of arginine catabolic pathways in modulating staphylococcal fitnessR01AI125588 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI THOMAS, VINAI · 2018 to 2022
$1.9M
NIAID NIH HHS P01 AI083211NIAID NIH HHS R01 AI125588
6 · The paper itself

Abstract

Central metabolic pathways control virulence and antibiotic resistance, and constitute potential targets for antibacterial drugs. In Staphylococcus aureus the role of the pentose phosphate pathway (PPP) remains largely unexplored. Mutation of the 6-phosphogluconolactonase gene pgl, which encodes the only non-essential enzyme in the oxidative phase of the PPP, significantly increased MRSA resistance to β-lactam antibiotics, particularly in chemically defined media with physiologically-relevant concentrations of glucose, and reduced oxacillin (OX)-induced lysis. Expression of the methicillin-resistance penicillin binding protein 2a and peptidoglycan architecture were unaffected. Carbon tracing and metabolomics revealed extensive metabolic reprogramming in the pgl mutant including increased flux to glycolysis, the TCA cycle, and several cell envelope precursors, which was consistent with increased β-lactam resistance. Morphologically, pgl mutant cells were smaller than wild-type with a thicker cell wall and ruffled surface when grown in OX. The pgl mutation reduced resistance to Congo Red, sulfamethoxazole and oxidative stress, and increased resistance to targocil, fosfomycin and vancomycin. Levels of lipoteichoic acids (LTAs) were significantly reduced in pgl, which may limit cell lysis, while the surface charge of pgl cells was significantly more positive. A vraG mutation in pgl reversed the increased OX resistance phenotype, and partially restored wild-type surface charge, but not LTA levels. Mutations in vraF or graRS from the VraFG/GraRS complex that regulates DltABCD-mediated d-alanylation of teichoic acids (which in turn controls β-lactam resistance and surface charge), also restored wild-type OX susceptibility. Collectively these data show that reduced levels of LTAs and OX-induced lysis combined with a VraFG/GraRS-dependent increase in cell surface positive charge are accompanied by significantly increased OX resistance in an MRSA pgl mutant.

Indexed as

Methicillin-Resistant Staphylococcus aureusAnti-Bacterial AgentsBacterial Proteinsbeta-Lactam ResistanceCell WallMicrobial Sensitivity TestsMonobactamsOxacillinPentose Phosphate PathwayAnti-Bacterial AgentsBacterial ProteinsMonobactamsOxacillin

Identifiers

PMID37486930
PMCPMC10399904
OpenAlexW4385211735

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.