Evidence map›Paper›PMID 28750048›Full record

ArticlePloS one2017

Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.

Miyer Patiño-Ruiz, Constanța Ganea, Klaus Fendler, Octavian Călinescu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Prokaryotic NaInternational journal of molecular sciences · 2022
    Review
  4. Article
  5. 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 2 institutions in 2 countries.

Miyer Patiño-RuizDepartment of Biophysical Chemistry, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Constanța GaneaDepartment of Biophysical Chemistry, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Klaus FendlerDepartment of Biophysical Chemistry, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Octavian CălinescuDepartment of Biophysical Chemistry, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0001-8003-0442
Carol Davila University of Medicine and Pharmacy · ROMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Na+/H+ exchange is essential for survival of all organisms, having a role in the regulation of the intracellular Na+ concentration, pH and cell volume. Furthermore, Na+/H+ exchangers were shown to be involved in the virulence of the bacterium Yersinia pestis, indicating they might be potential targets for novel antibiotic treatments. The model system for Na+/H+ exchangers is the NhaA transporter from Escherichia coli, EcNhaA. Therefore, the general transport mechanism of NhaA exchangers is currently well characterized. However, much less is known about NhaB exchangers, with only a limited number of studies available. The pathogen Klebsiella pneumoniae, which is a major source of nosocomial infection, possesses three electrogenic Na+/H+ exchangers, KpNhaA1, KpNhaA2 and KpNhaB, none of which have been previously investigated. Our aim in this study was to functionally characterize KpNhaB using solid supported membrane-based electrophysiology as the main investigation technique, and thus provide the first electrophysiological investigation of an NhaB Na+/H+ exchanger. We found that NhaB can be described by the same competition-based mechanism that was shown to be valid for electrogenic NhaA and NapA, and for electroneutral NhaP Na+/H+ exchangers. For comparison we also characterized the activity of KpNhaA1 and KpNhaA2 and found that the three exchangers have complementary activity profiles, which is likely a survival advantage for K. pneumoniae when faced with environments of different salinity and pH. This underlines their importance as potential antibiotic drug targets.

Indexed as

Acridine OrangeAmino Acid SequenceBacterial ProteinsBiological TransportCell MembraneEscherichia coliHydrogen-Ion ConcentrationKineticsKlebsiella pneumoniaeLithiumMicrobial ViabilitySequence AlignmentSodiumSodium-Hydrogen ExchangersSubstrate SpecificityAcridine OrangeBacterial ProteinsLithiumSodiumSodium-Hydrogen Exchangers

Identifiers

PMID28750048
PMCPMC5531510
OpenAlexW2741742781

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.