ArticleJournal of molecular microbiology and biotechnology2009
The Vibrio cholerae Mrp system: cation/proton antiport properties and enhancement of bile salt resistance in a heterologous host.
Article in Journal of molecular microbiology and biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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.
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.
Who cites it
38 citing papers in PubMed, 55 citations in OpenAlex.
- The evolution of a NaJournal of bacteriology · 2026Article
- Article
- The evolution of a NabioRxiv : the preprint server for biology · 2026Article
- Loss of essential outer membrane functions causes drug hypersensitization inbioRxiv : the preprint server for biology · 2025Article
- Article
- Genetic characteristics of novel extreme alkaline-inducible promoter located in five prime upstream region of peptidyl-prolyl cis/trans isomerase from Vibrio anguillarum.Scientific reports · 2025Article
- Prokaryotic NaInternational journal of molecular sciences · 2022Review
- Genetic and Biochemical Characterization of the NaJournal of bacteriology · 2021Article
- Functional Characterization of MultipleInternational journal of molecular sciences · 2021Article
- Berberine alters gut microbial function through modulation of bile acids.BMC microbiology · 2021Article
- NamBio · 2020Article
- Article
- Sodium antiporters of Pseudomonas aeruginosa in challenging conditions: effects on growth, biofilm formation, and swarming motility.Journal, genetic engineering & biotechnology · 2020Article
- Roles of Staphylococcus aureus Mnh1 and Mnh2 Antiporters in Salt Tolerance, Alkali Tolerance, and Pathogenesis.Journal of bacteriology · 2018Article
- Article
- Characterization of a Functionally Unknown Arginine-Aspartate-Aspartate Family Protein FromFrontiers in microbiology · 2018Article
- A genetic system for targeted mutations to disrupt and restore genes in the obligate bacterium, Ehrlichia chaffeensis.Scientific reports · 2017Article
- Characterization of a novel two-component NaScientific reports · 2017Article
- A UPF0118 family protein with uncharacterized function from the moderate halophile Halobacillus andaensis represents a novel class of NaScientific reports · 2017Article
- Physiology of the Vc-NhaP paralogous group of cation-proton antiporters in Vibrio cholerae.Molecular and cellular biochemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The mrp operon from Vibrio cholerae encoding a putative multisubunit Na(+)/H(+) antiporter was cloned and functionally expressed in the antiporter-deficient strain of Escherichia coli EP432. Cells of EP432 expressing Vc-Mrp exhibited resistance to Na(+) and Li(+) as well as to natural bile salts such as sodium cholate and taurocholate. When assayed in everted membrane vesicles of the E. coli EP432 host, Vc-Mrp had sufficiently high antiport activity to facilitate the first extensive analysis of Mrp system from a Gram-negative bacterium encoded by a group 2 mrp operon. Vc-Mrp was found to exchange protons for Li(+), Na(+), and K(+) ions in pH-dependent manner with maximal activity at pH 9.0-9.5. Exchange was electrogenic (more than one H(+) translocated per cation moved in opposite direction). The apparent K(m) at pH 9.0 was 1.08, 1.30, and 68.5 mM for Li(+), Na(+), and K(+), respectively. Kinetic analyses suggested that Vc-Mrp operates in a binding exchange mode with all cations and protons competing for binding to the antiporter. The robust ion antiport activity of Vc-Mrp in sub-bacterial vesicles and its effect on bile resistance of the heterologous host make Vc-Mrp an attractive experimental model for the further studies of biochemistry and physiology of Mrp systems.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.