ArticleJournal of bacteriology2013
Mutagenesis and modeling to predict structural and functional characteristics of the Staphylococcus aureus MepA multidrug efflux pump.
Article in Journal of bacteriology, 2013. 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, 37 citations in OpenAlex.
- Occurrence, variability and evolutionary relations of efflux pump determinants across five pathogenicFrontiers in pharmacology · 2026Article
- Molecular docking and antibacterial and antibiotic-modifying activities of synthetic chalcone (2E)-1-(3'-aminophenyl)-3-(4-dimethylaminophenyl)-prop-2-en-1-one in a MepA efflux pump-expressing Staphylococcus aureus strain.Folia microbiologica · 2025Article
- Identification of genetic mutations conferring tedizolid resistance in MRSA mutants.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- Antibacterial and Inhibitory Activity of Nora and Mepa Efflux Pumps of Estragole Complexed to β-Cyclodextrin (ES/β-CD) In Vitro AgainstPharmaceutics · 2024Article
- Enhanced Efficacy of Ciprofloxacin and Tobramycin againstAntibiotics (Basel, Switzerland) · 2024Article
- Whole Genome Sequencing and Pan-Genomic Analysis of Multidrug-ResistantMicroorganisms · 2023Article
- Evaluation of ellagic acid and gallic acid as efflux pump inhibitors in strains of Staphylococcus aureus.Biology open · 2022Article
- Efflux Pump Mediated Antimicrobial Resistance by Staphylococci in Health-Related Environments: Challenges and the Quest for Inhibition.Antibiotics (Basel, Switzerland) · 2021Review
- Predicting drug targets by homology modelling of Pseudomonas aeruginosa proteins of unknown function.PloS one · 2021Article
- Resistance in In Vitro Selected Tigecycline-Resistant Methicillin-Resistant Staphylococcus aureus Sequence Type 5 Is Driven by Mutations in mepR and mepA Genes.Microbial drug resistance (Larchmont, N.Y.) · 2018Article
- Mutations at the Ribosomal S10 Gene in Clinical Strains of Staphylococcus aureus with Reduced Susceptibility to Tigecycline.Antimicrobial agents and chemotherapy · 2018Article
- Attaching the NorA Efflux Pump Inhibitor INF55 to Methylene Blue Enhances Antimicrobial Photodynamic Inactivation of Methicillin-Resistant Staphylococcus aureus in Vitro and in Vivo.ACS infectious diseases · 2017Article
- Topoisomerase Inhibitors: Fluoroquinolone Mechanisms of Action and Resistance.Cold Spring Harbor perspectives in medicine · 2016Review
- Mechanisms of drug resistance: quinolone resistance.Annals of the New York Academy of Sciences · 2015Review
- Functional consequences of substitution mutations in MepR, a repressor of the Staphylococcus aureus MepA multidrug efflux pump gene.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
MepA is a multidrug and toxin extrusion (MATE) family protein and the only MATE protein encoded within the Staphylococcus aureus genome. Structural data for MATE proteins are limited to a single high-resolution example, NorM of Vibrio cholerae. Substitution mutations were created in MepA using gradient plates containing both a substrate and reserpine as an efflux pump inhibitor. Site-directed mutagenesis of plasmid-based mepA was used to reproduce these mutations, as well as unique or low-frequency mutations identified in mepA-overexpressing clinical strains, and to mutagenize conserved acidic residues. The effect of these changes on protein function was quantitated in a norA-disrupted host strain by susceptibility testing with and without inhibitors and by determining the proficiency of ethidium efflux. Up-function substitutions clustered in the carboxy half of MepA, near the cytoplasmic face of the protein. Repeated application of the same gradient plate conditions frequently reproduced identical substitution mutations, suggesting that individual residues are required for interaction with specific substrates. Acidic residues critical to protein function were identified in helices 4 and 5. In silico modeling revealed an outward-facing molecule, with helices 1, 2, 4, 7, 8, and 10 having contact with a central cavity that may represent a substrate translocation pathway. Functionally important residues within this cavity included S81, A161, M291, and A302. These data provide a critical starting point for understanding how MATE multidrug efflux proteins function and will be useful in refining crystallographic data when they are available.
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