Evidence map›Paper›PMID 34782466›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase.

Abdulelah A Alqarzaee, Sujata S Chaudhari, Mohammad Mazharul Islam, Vikas Kumar, Matthew C Zimmerman, Rajib Saha, Kenneth W Bayles, Dorte Frees, Vinai C Thomas

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Broad-spectrum tolerance to disinfectant-mediated bacterial killing due to mutation of the PheS aminoacyl tRNA synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Article
  11. Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Targeting the Achilles' Heel of Multidrug-ResistantInternational journal of molecular sciences · 2022
    Article
  13. Bacteria clip out damaged cells from populations.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Abdulelah A AlqarzaeeCenter for Staphylococcal Research, Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0000-0003-0000-9040
Sujata S ChaudhariCenter for Staphylococcal Research, Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0000-0002-9609-152X
Mohammad Mazharul IslamDepartment of Chemical and Biomolecular Engineering, University of Nebraska, Lincoln, NE 68588.ORCID 0000-0002-9745-0344
Vikas KumarDepartment of Genetics, Cell Biology, and Anatomy, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0000-0001-7513-6832
Matthew C ZimmermanCellular and Integrative Physiology, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0000-0001-5658-9051
Rajib SahaDepartment of Chemical and Biomolecular Engineering, University of Nebraska, Lincoln, NE 68588.ORCID 0000-0002-2974-0243
Kenneth W BaylesCenter for Staphylococcal Research, Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198.
Dorte FreesDepartment of Veterinary and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, 1870 Frederiksberg C, Denmark.ORCID 0000-0003-4946-2890
Vinai C ThomasCenter for Staphylococcal Research, Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198; vinai.thomas@unmc.edu.ORCID 0000-0002-7886-0727
University of Nebraska Medical Center · USUniversity of Nebraska–Lincoln · USUniversity of Copenhagen · DK

Funding

The S. aureus biofilm lifecycleP01AI083211 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI KIELIAN, TAMMY L · 2009 to 2023
$32.1M
Redox Biology CenterP30GM103335 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2012 to 2016
$4.3M
The role of arginine catabolic pathways in modulating staphylococcal fitnessR01AI125588 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI THOMAS, VINAI · 2018 to 2022
$1.9M
The molecular control of bacterial programmed cell deathR01AI125589 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI BAYLES, KENNETH W. · 2016 to 2020
$1.9M
NIAID NIH HHS P01 AI083211NIAID NIH HHS R01 AI125588NIAID NIH HHS R01 AI125589NIGMS NIH HHS P30 GM103335
6 · The paper itself

Abstract

The transition from growth to stationary phase is a natural response of bacteria to starvation and stress. When stress is alleviated and more favorable growth conditions return, bacteria resume proliferation without a significant loss in fitness. Although specific adaptations that enhance the persistence and survival of bacteria in stationary phase have been identified, mechanisms that help maintain the competitive fitness potential of nondividing bacterial populations have remained obscure. Here, we demonstrate that staphylococci that enter stationary phase following growth in media supplemented with excess glucose, undergo regulated cell death to maintain the competitive fitness potential of the population. Upon a decrease in extracellular pH, the acetate generated as a byproduct of glucose metabolism induces cytoplasmic acidification and extensive protein damage in nondividing cells. Although cell death ensues, it does not occur as a passive consequence of protein damage. Instead, we demonstrate that the expression and activity of the ClpXP protease is induced, resulting in the degeneration of cellular antioxidant capacity and, ultimately, cell death. Under these conditions, inactivation of either

Indexed as

Acetic AcidAntioxidantsBacteriaBacterial ProteinsCell DeathEndopeptidase ClpGene Expression Regulation, BacterialGlucoseStaphylococcus aureusAcetic AcidAntioxidantsBacterial ProteinsEndopeptidase ClpGlucoseclpPclpXsodAStaphylococcus aureusstationary phase fitness

Identifiers

PMID34782466
PMCPMC8617462
OpenAlexW3214040756

What OpenQuestion holds

Textmetadata
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.