ArticleJournal of bacteriology2006
Mutations in the central cavity and periplasmic domain affect efflux activity of the resistance-nodulation-division pump EmhB from Pseudomonas fluorescens cLP6a.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 38 citations in OpenAlex.
- Regulation, structure, and activity of theAntimicrobial agents and chemotherapy · 2025Review
- Genomic and phenotypic insight into antimicrobial resistance ofFrontiers in microbiology · 2025Article
- Comparative Genomic Analysis of Multi-Drug ResistantMicroorganisms · 2023Article
- Article
- Review
- Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition.Nature communications · 2018Article
- Article
- An alternative physiological role for the EmhABC efflux pump in Pseudomonas fluorescens cLP6a.BMC microbiology · 2011Article
- Vestibules are part of the substrate path in the multidrug efflux transporter AcrB of Escherichia coli.Journal of bacteriology · 2011Article
- Structure and mechanism of RND-type multidrug efflux pumps.Advances in enzymology and related areas of molecular biology · 2011Review
- Substrate path in the AcrB multidrug efflux pump of Escherichia coli.Molecular microbiology · 2010Article
- Review
- Mechanisms of RND multidrug efflux pumps.Biochimica et biophysica acta · 2009Review
- Site-directed mutagenesis reveals amino acid residues in the Escherichia coli RND efflux pump AcrB that confer macrolide resistance.Antimicrobial agents and chemotherapy · 2009Article
- Site-directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB.Journal of bacteriology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The EmhABC efflux system in Pseudomonas fluorescens cLP6a is homologous to the multidrug and solvent efflux systems belonging to the resistance-nodulation-division (RND) family and is responsible for polycyclic aromatic hydrocarbon transport, antibiotic resistance, and toluene efflux. To gain a better understanding of substrate transport in RND efflux pumps, the EmhB pump was subjected to mutational analysis. Mutagenesis of amino acids within the central cavity of the predicted three-dimensional structure of EmhB showed selective activity towards antibiotic substrates. An A384P/A385Y double mutant showed increased susceptibility toward rhodamine 6G compared to the wild type, and F386A and N99A single mutants showed increased susceptibility to dequalinium compared to the wild type. As well, the carboxylic acid side chain of D101, located in the central cavity region, was found to be essential for polycyclic aromatic hydrocarbon transport and resistance to all antibiotic substrates of EmhB. Phenylalanine residues located within the periplasmic pore domain were also targeted for mutagenesis, and the F325A and F281A mutations significantly impaired efflux activity for all EmhB substrates. One mutation (A206S) in the outer membrane protein docking domain increased antibiotic resistance and toluene tolerance, demonstrating the important role of this domain in transport activity. These data demonstrate the roles of the central cavity and periplasmic domains in the function of the RND efflux pump EmhB.
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