Evidence map›Paper›PMID 27481926›Full record

ArticleJournal of bacteriology2016

Identification and Characterization of a Putative Manganese Export Protein in Vibrio cholerae.

Carolyn R Fisher, Elizabeth E Wyckoff, Eric D Peng, Shelley M Payne

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Functional characterization of a TerC family protein ofApplied and environmental microbiology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Bacterial manganese sensing and homeostasis.Current opinion in chemical biology · 2020
    Review
  14. Article
  15. The yeast protein Gdt1p transports MnThe Journal of biological chemistry · 2018
    Article
  16. Article
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

4 authors at 1 institution in 1 country.

Carolyn R FisherDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Elizabeth E WyckoffDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Eric D PengDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.
Shelley M PayneDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA smpayne@utexas.edu.
The University of Texas at Austin · US

Funding

Characterization of the ferrous iron transporter Feo in Vibrio choleraeR01AI091957 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI PAYNE, SHELLEY M. · 2011 to 2021
$3.9M
NIAID NIH HHS R01 AI091957
6 · The paper itself

Abstract

unlabelledManganese plays an important role in the cellular physiology and metabolism of bacterial species, including the human pathogen Vibrio cholerae The intracellular level of manganese ions is controlled through coordinated regulation of the import and export of this element. We have identified a putative manganese exporter (VC0022), named mneA (manganese exporter A), which is highly conserved among Vibrio spp. An mneA mutant exhibited sensitivity to manganese but not to other cations. Under high-manganese conditions, the mneA mutant showed an almost 50-fold increase in intracellular manganese levels and reduced intracellular iron relative to those of its wild-type parent, suggesting that the mutant's manganese sensitivity is due to the accumulation of toxic levels of manganese and reduced iron. Expression of mneA suppressed the manganese-sensitive phenotype of an Escherichia coli strain carrying a mutation in the nonhomologous manganese export gene, mntP, further supporting a manganese export function for V. cholerae MneA. The level of mneA mRNA was induced approximately 2.5-fold after addition of manganese to the medium, indicating regulation of this gene by manganese. This study offers the first insights into understanding manganese homeostasis in this important pathogen. IMPORTANCE: Bacterial cells control intracellular metal concentrations by coordinating acquisition in metal-limited environments with export in metal-excess environments. We identified a putative manganese export protein, MneA, in Vibrio cholerae An mneA mutant was sensitive to manganese, and this effect was specific to manganese. The mneA mutant accumulated high levels of intracellular manganese with a concomitant decrease in intracellular iron levels when grown in manganese-supplemented medium. Expression of mneA in trans suppressed the manganese sensitivity of an E. coli mntP mutant. This study is the first to investigate manganese export in V. cholerae.

Indexed as

Bacterial ProteinsBiological TransportGene Expression Regulation, BacterialIronManganeseMembrane Transport ProteinsMutationVibrio choleraeBacterial ProteinsIronManganeseMembrane Transport Proteins

Identifiers

PMID27481926
PMCPMC5038002
OpenAlexW2485429606

What OpenQuestion holds

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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.