ArticleNature chemical biology2022
Structural basis for inhibition of the drug efflux pump NorA from Staphylococcus aureus.
Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 80 citations in OpenAlex.
- IntegratedACS omega · 2026Article
- Small-molecule inhibitors block NorA efflux by conformational trapping.Nature chemical biology · 2026Article
- Evaluation of the antimicrobial and NorA and MepA efflux pump inhibitory activity of a hydrazone derivative of hydralazine against Staphylococcus aureus.Archives of microbiology · 2026Article
- Nanomaterial strategies for antibiotic-resistant infections: Mechanistic frameworks, rational design, and clinical translation.Materials today. Bio · 2026Review
- Miniprotein inhibitors of thebioRxiv : the preprint server for biology · 2026Article
- Evaluation of the effects of hybrids of metronidazole and eugenol analogues as inhibitors of the Staphylococcus aureus NorA efflux pump: an in vitro and in silico analysis.Folia microbiologica · 2026Article
- Action of Betulinic Acid in the Inhibition of Efflux Pump NorA in Staphylococcus aureus Strains: In Vitro and In Silico Approaches.Chemistry & biodiversity · 2026Article
- Screening ofFrontiers in microbiology · 2026Article
- Occurrence, variability and evolutionary relations of efflux pump determinants across five pathogenicFrontiers in pharmacology · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Energetic and structural control of polyspecificity in a multidrug transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Staphylococcus aureus: Antimicrobial resistance, quorum sensing, and antibiofilm approaches.European journal of microbiology & immunology · 2025Review
- Integrated in Vitro, in Vivo, Molecular Docking, and ADMET in Silico Assessment of β-Caryophyllene as a NorA Efflux Pump inhibitor in Resistant Staphylococcus Aureus (MRSA).Current microbiology · 2025Article
- Evaluating the ciprofloxacin potentiation efficacy of repurposed drug flupentixol through efflux pump inhibition of pathogenic bacteria.Scientific reports · 2025Article
- α-Pinene and β-Pinene as Natural Adjuvants Against MRSA: Evidence from in vivo Models and Molecular Docking.Current microbiology · 2025Article
- Evaluation of the Activity of Amino Chalcone AgainstPharmaceuticals (Basel, Switzerland) · 2025Article
- Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.Nature communications · 2025Article
- Inhibitory potential of pentagalloyl glucose against efflux pumps inRSC advances · 2025Article
- Biofilm Formation and the Role of Efflux Pumps in ESKAPE Pathogens.Microorganisms · 2025Review
- NorA Efflux Pump Inhibitors: Expanding SAR Knowledge of Pyrazolo[4,3-c][1,2]benzothiazine 5,5-Dioxide Derivatives.Archiv der Pharmazie · 2025Article
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14 authors at 3 institutions in 3 countries.
Funding
Abstract
Membrane protein efflux pumps confer antibiotic resistance by extruding structurally distinct compounds and lowering their intracellular concentration. Yet, there are no clinically approved drugs to inhibit efflux pumps, which would potentiate the efficacy of existing antibiotics rendered ineffective by drug efflux. Here we identified synthetic antigen-binding fragments (Fabs) that inhibit the quinolone transporter NorA from methicillin-resistant Staphylococcus aureus (MRSA). Structures of two NorA-Fab complexes determined using cryo-electron microscopy reveal a Fab loop deeply inserted in the substrate-binding pocket of NorA. An arginine residue on this loop interacts with two neighboring aspartate and glutamate residues essential for NorA-mediated antibiotic resistance in MRSA. Peptide mimics of the Fab loop inhibit NorA with submicromolar potency and ablate MRSA growth in combination with the antibiotic norfloxacin. These findings establish a class of peptide inhibitors that block antibiotic efflux in MRSA by targeting indispensable residues in NorA without the need for membrane permeability.
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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.