Evidence map›Paper›PMID 18492255›Full record

ArticleBMC microbiology2008

Functional comparison of plasma-membrane Na+/H+ antiporters from two pathogenic Candida species.

Yannick Krauke, Hana Sychrova

Open access · goldAbstract readComparative Study
In one paragraph

Article in BMC microbiology, 2008. 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
1.6field-weighted citation impact, top 18% 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, 27 citations in OpenAlex.

  1. Review
  2. Cation Transporters ofBiomolecules · 2021
    Review
  3. An Update onFrontiers in microbiology · 2017
    Review
  4. Evaluation of Virulence FactorsFrontiers in microbiology · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Alkali metal cation transport and homeostasis in yeasts.Microbiology and molecular biology reviews : MMBR · 2010
    Review
  13. 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

2 authors at 1 institution in 1 country.

Yannick KraukeDepartment of Membrane Transport, Institute of Physiology AS CR, v,v,i,, Videnska 1083, 14220 Prague 4, Czech Republic. krauke@biomed.cas.cz
Hana Sychrova
Czech Academy of Sciences, Institute of Physiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe virulence of Candida species depends on many environmental conditions. Extracellular pH and concentration of alkali metal cations belong among important factors. Nevertheless, the contribution of transporters mediating the exchange of alkali metal cations for protons across the plasma membrane to the cell salt tolerance and other physiological properties of various Candida species has not been studied so far.

resultsThe tolerance/sensitivity of four pathogenic Candida species to alkali metal cations was tested and the role of one of the cation transporters in that tolerance (presumed to be the plasma-membrane Na+/H+ antiporter) was studied. The genes encoding these antiporters in the most and least salt sensitive species, C. dubliniensis and C. parapsilosis respectively, were identified, cloned and functionally expressed in the plasma membranes of Saccharomyces cerevisiae cells lacking their own cation exporters. Both CpCnh1 and CdCnh1 antiporters had broad substrate specificity and transported Na+, K+, Li+, and Rb+. Their activity in S. cerevisiae cells differed; CpCnh1p provided cells with a much higher salt tolerance than the CdCnh1 antiporter. The observed difference in activity was confirmed by direct measurements of sodium and potassium efflux mediated by these antiporters.

conclusionWe have cloned two genes encoding putative Na+/H+ antiporters in C. parapsilosis and C. dubliniensis, and characterized the transport properties of encoded proteins. Our results show that the activity of plasma-membrane Na+/H+ antiporters is one of the factors determining the tolerance of pathogenic Candida species to high external concentrations of alkali metal cations.

Indexed as

Base SequenceCandidaCationsCation Transport ProteinsFungal ProteinsLithiumMembrane ProteinsMetals, AlkaliMicroscopy, FluorescenceMolecular Sequence DataPotassiumProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaltsSodium-Hydrogen ExchangersCationsCation Transport ProteinsCNH1 protein, Candida albicansFungal ProteinsLithiumMembrane ProteinsMetals, AlkaliNHA1 protein, S cerevisiaePotassiumSaccharomyces cerevisiae ProteinsSaltsSodium-Hydrogen ExchangersSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID18492255
PMCPMC2424070
OpenAlexW1974063203

What OpenQuestion holds

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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.