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

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 targe...

Full description

Bibliographic Details
Main Authors: Miyer Patiño-Ruiz, Constanța Ganea, Klaus Fendler, Octavian Călinescu
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5531510?pdf=render
id doaj-318cdeed6d3944b387c7439ad247bdf2
record_format Article
spelling doaj-318cdeed6d3944b387c7439ad247bdf22020-11-24T20:45:28ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01127e018229310.1371/journal.pone.0182293Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.Miyer Patiño-RuizConstanța GaneaKlaus FendlerOctavian CălinescuNa+/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.http://europepmc.org/articles/PMC5531510?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Miyer Patiño-Ruiz
Constanța Ganea
Klaus Fendler
Octavian Călinescu
spellingShingle Miyer Patiño-Ruiz
Constanța Ganea
Klaus Fendler
Octavian Călinescu
Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
PLoS ONE
author_facet Miyer Patiño-Ruiz
Constanța Ganea
Klaus Fendler
Octavian Călinescu
author_sort Miyer Patiño-Ruiz
title Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
title_short Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
title_full Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
title_fullStr Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
title_full_unstemmed Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
title_sort competition is the basis of the transport mechanism of the nhab na+/h+ exchanger from klebsiella pneumoniae.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2017-01-01
description 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.
url http://europepmc.org/articles/PMC5531510?pdf=render
work_keys_str_mv AT miyerpatinoruiz competitionisthebasisofthetransportmechanismofthenhabnahexchangerfromklebsiellapneumoniae
AT constantaganea competitionisthebasisofthetransportmechanismofthenhabnahexchangerfromklebsiellapneumoniae
AT klausfendler competitionisthebasisofthetransportmechanismofthenhabnahexchangerfromklebsiellapneumoniae
AT octaviancalinescu competitionisthebasisofthetransportmechanismofthenhabnahexchangerfromklebsiellapneumoniae
_version_ 1716814721807548416