Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autorschaft

  • Kerstin Stingl
  • Sonja Brandt
  • Eva-Maria Uhlemann
  • Roland Schmid
  • Karlheinz Altendorf
  • Carsten Zeilinger
  • Chantal Ecobichon
  • Agnès Labigne
  • Evert P Bakker
  • Hilde de Reuse

Externe Organisationen

  • Institut Pasteur de Tunis
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)232-41
Seitenumfang10
FachzeitschriftThe EMBO journal
Jahrgang26
Ausgabenummer1
PublikationsstatusVeröffentlicht - 10 Jan. 2007

Abstract

To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.

Zitieren

Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization. / Stingl, Kerstin; Brandt, Sonja; Uhlemann, Eva-Maria et al.
in: The EMBO journal, Jahrgang 26, Nr. 1, 10.01.2007, S. 232-41.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Stingl, K, Brandt, S, Uhlemann, E-M, Schmid, R, Altendorf, K, Zeilinger, C, Ecobichon, C, Labigne, A, Bakker, EP & de Reuse, H 2007, 'Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization', The EMBO journal, Jg. 26, Nr. 1, S. 232-41. https://doi.org/10.1038/sj.emboj.7601471
Stingl, K., Brandt, S., Uhlemann, E.-M., Schmid, R., Altendorf, K., Zeilinger, C., Ecobichon, C., Labigne, A., Bakker, E. P., & de Reuse, H. (2007). Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization. The EMBO journal, 26(1), 232-41. https://doi.org/10.1038/sj.emboj.7601471
Stingl K, Brandt S, Uhlemann EM, Schmid R, Altendorf K, Zeilinger C et al. Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization. The EMBO journal. 2007 Jan 10;26(1):232-41. doi: 10.1038/sj.emboj.7601471
Stingl, Kerstin ; Brandt, Sonja ; Uhlemann, Eva-Maria et al. / Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization. in: The EMBO journal. 2007 ; Jahrgang 26, Nr. 1. S. 232-41.
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title = "Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization",
abstract = "To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.",
keywords = "Amino Acid Sequence, Animals, Codon, Initiator, Cytoplasm/metabolism, Gastric Mucosa/microbiology, Helicobacter pylori/metabolism, Hydrogen-Ion Concentration, Mice, Models, Biological, Molecular Sequence Data, Potassium/chemistry, Potassium Channels/chemistry, Protein Structure, Tertiary, Sequence Homology, Amino Acid",
author = "Kerstin Stingl and Sonja Brandt and Eva-Maria Uhlemann and Roland Schmid and Karlheinz Altendorf and Carsten Zeilinger and Chantal Ecobichon and Agn{\`e}s Labigne and Bakker, {Evert P} and {de Reuse}, Hilde",
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TY - JOUR

T1 - Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization

AU - Stingl, Kerstin

AU - Brandt, Sonja

AU - Uhlemann, Eva-Maria

AU - Schmid, Roland

AU - Altendorf, Karlheinz

AU - Zeilinger, Carsten

AU - Ecobichon, Chantal

AU - Labigne, Agnès

AU - Bakker, Evert P

AU - de Reuse, Hilde

PY - 2007/1/10

Y1 - 2007/1/10

N2 - To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.

AB - To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.

KW - Amino Acid Sequence

KW - Animals

KW - Codon, Initiator

KW - Cytoplasm/metabolism

KW - Gastric Mucosa/microbiology

KW - Helicobacter pylori/metabolism

KW - Hydrogen-Ion Concentration

KW - Mice

KW - Models, Biological

KW - Molecular Sequence Data

KW - Potassium/chemistry

KW - Potassium Channels/chemistry

KW - Protein Structure, Tertiary

KW - Sequence Homology, Amino Acid

U2 - 10.1038/sj.emboj.7601471

DO - 10.1038/sj.emboj.7601471

M3 - Article

C2 - 17159901

VL - 26

SP - 232

EP - 241

JO - The EMBO journal

JF - The EMBO journal

SN - 0261-4189

IS - 1

ER -