ArticleThe EMBO journal2007
Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Insights intoFrontiers in cellular and infection microbiology · 2025Article
- Mycobacterium tuberculosis response to cholesterol is integrated with environmental pH and potassium levels via a lipid metabolism regulator.PLoS genetics · 2024Article
- The PTSmBio · 2022Article
- Genome-wide association study of gastric cancer- and duodenal ulcer-derivedMicrobial genomics · 2021Article
- Unappreciated Roles for KTrends in microbiology · 2021Review
- Molecular Mechanisms for Bacterial Potassium Homeostasis.Journal of molecular biology · 2021Review
- Beyond Homeostasis: Potassium and Pathogenesis during Bacterial Infections.Infection and immunity · 2021Review
- Abundant Monovalent Ions as Environmental Signposts for Pathogens during Host Colonization.Infection and immunity · 2021Review
- The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix.Frontiers in molecular biosciences · 2020Article
- Potassium response and homeostasis in Mycobacterium tuberculosis modulates environmental adaptation and is important for host colonization.PLoS pathogens · 2019Article
- Effects of Salts on the Activity and Growth of "Candidatus Scalindua sp.", a Marine Anammox Bacterium.Microbes and environments · 2018Article
- Article
- Mechanistic insights into type I toxin antitoxin systems in Helicobacter pylori: the importance of mRNA folding in controlling toxin expression.Nucleic acids research · 2017Article
- Comparative genomic and phenomic analysis of Clostridium difficile and Clostridium sordellii, two related pathogens with differing host tissue preference.BMC genomics · 2015Article
- Relationship between Ni(II) and Zn(II) coordination and nucleotide binding by the Helicobacter pylori [NiFe]-hydrogenase and urease maturation factor HypB.The Journal of biological chemistry · 2014Article
- The Ktr potassium transport system in Staphylococcus aureus and its role in cell physiology, antimicrobial resistance and pathogenesis.Molecular microbiology · 2013Article
- The KdpD/KdpE two-component system: integrating K⁺ homeostasis and virulence.PLoS pathogens · 2013Article
- Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.The Journal of biological chemistry · 2010Article
- A novel potassium channel in photosynthetic cyanobacteria.PloS one · 2010Article
- Identification of trkH, encoding a potassium uptake protein required for Francisella tularensis systemic dissemination in mice.PloS one · 2010Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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