Evidence map›Paper›PMID 28103306›Full record

ArticlePLoS pathogens2017

A Superoxide Dismutase Capable of Functioning with Iron or Manganese Promotes the Resistance of Staphylococcus aureus to Calprotectin and Nutritional Immunity.

Yuritzi M Garcia, Anna Barwinska-Sendra, Emma Tarrant, Eric P Skaar, Kevin J Waldron, Thomas E Kehl-Fie

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 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 124 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Metal-independent effects of calprotectin on cocultures ofbioRxiv : the preprint server for biology · 2026
    Article
  10. Cobalt mitigates zinc-starvation effects in Pseudomonas aeruginosa.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  11. Article
  12. Article
  13. The innate immune protein calprotectin ablates the bactericidal activity of β-lactam antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Proteomic Analysis of the Differential Response ofAntibiotics (Basel, Switzerland) · 2025
    Article
  16. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  17. Article
  18. Article
  19. Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025
    Article
  20. Article

32 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

6 authors at 3 institutions in 2 countries.

Yuritzi M GarciaDepartment of Microbiology, University of Illinois Urbana-Champaign, Urbana, IL, United States of America.ORCID 0000-0002-3858-4684
Anna Barwinska-SendraInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.ORCID 0000-0002-9342-2805
Emma TarrantInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Eric P SkaarDepartment of Pathology Microbiology and Immunology, Vanderbilt University Medical Center Nashville TN, United States of America.
Kevin J WaldronInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.ORCID 0000-0002-5577-7357
Thomas E Kehl-FieDepartment of Microbiology, University of Illinois Urbana-Champaign, Urbana, IL, United States of America.ORCID 0000-0001-8234-1113
Newcastle University · GBUniversity of Illinois Urbana-Champaign · USVanderbilt University Medical Center · US

Funding

Host-mediated zinc sequestration during Acinetobacter baumannii infectionR01AI101171 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI WALTER J. CHAZIN, DAVID P. GIEDROC · 2013 to 2026
$8.2M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Overcoming nutritional immunity: Staphylococcal adaptation to host-imposed manganese and zinc starvationR01AI118880 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI KEHL-FIE, THOMAS EVERETT · 2016 to 2020
$1.9M
Adaptation of Staphylococcus aureus to Mn and Zn starvation imposed by the hostK22AI104805 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI KEHL-FIE, THOMAS EVERETT · 2014 to 2015
$264k
Biotechnology and Biological Sciences Research CouncilNIAID NIH HHS K22 AI104805NIAID NIH HHS R01 AI101171NIAID NIH HHS R01 AI118880NIGMS NIH HHS T32 GM008320Wellcome TrustWellcome Trust 098375/Z/12/Z
6 · The paper itself

Abstract

Staphylococcus aureus is a devastating mammalian pathogen for which the development of new therapeutic approaches is urgently needed due to the prevalence of antibiotic resistance. During infection pathogens must overcome the dual threats of host-imposed manganese starvation, termed nutritional immunity, and the oxidative burst of immune cells. These defenses function synergistically, as host-imposed manganese starvation reduces activity of the manganese-dependent enzyme superoxide dismutase (SOD). S. aureus expresses two SODs, denoted SodA and SodM. While all staphylococci possess SodA, SodM is unique to S. aureus, but the advantage that S. aureus gains by expressing two apparently manganese-dependent SODs is unknown. Surprisingly, loss of both SODs renders S. aureus more sensitive to host-imposed manganese starvation, suggesting a role for these proteins in overcoming nutritional immunity. In this study, we have elucidated the respective contributions of SodA and SodM to resisting oxidative stress and nutritional immunity. These analyses revealed that SodA is important for resisting oxidative stress and for disease development when manganese is abundant, while SodM is important under manganese-deplete conditions. In vitro analysis demonstrated that SodA is strictly manganese-dependent whereas SodM is in fact cambialistic, possessing equal enzymatic activity when loaded with manganese or iron. Cumulatively, these studies provide a mechanistic rationale for the acquisition of a second superoxide dismutase by S. aureus and demonstrate an important contribution of cambialistic SODs to bacterial pathogenesis. Furthermore, they also suggest a new mechanism for resisting manganese starvation, namely populating manganese-utilizing enzymes with iron.

Indexed as

AnimalsChromatography, Ion ExchangeDisease Models, AnimalIronLeukocyte L1 Antigen ComplexManganeseMass SpectrometryMiceMice, Inbred C57BLPolymerase Chain ReactionStaphylococcal InfectionsStaphylococcus aureusSuperoxide DismutaseIronLeukocyte L1 Antigen ComplexManganeseSuperoxide Dismutase

Identifiers

PMID28103306
PMCPMC5245786
OpenAlexW2573968363

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.