ArticleNature communications2020
Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- High resolution cryo-EM structure of theJournal of structural biology: X · 2026Article
- Structural insights into a substrate translocation pathway revealed by the RND efflux pump complex MexJK fromScience advances · 2026Article
- Efflux-mediated carbapenem resistance: unveiling genetic drivers, clinical implications, and strategies for global antimicrobial stewardship.Antonie van Leeuwenhoek · 2026Review
- Efflux pump activation confers mupirocin resistance and enhances rhizosphere fitness inApplied and environmental microbiology · 2026Article
- Structural mechanisms of pump assembly and drug transport in the AcrAB-TolC efflux system.eLife · 2026Article
- Genomic and GWAS-Based Insights into Antimicrobial Resistance inAntibiotics (Basel, Switzerland) · 2026Article
- A lipoprotein partner for theeLife · 2026Article
- A missing link for efflux pumps.eLife · 2026Article
- A model for drug transport across two membranes of Gram-negative bacteria by an MFS tripartite assembly.Nature communications · 2026Article
- Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Structure-Based Drug Design Targeting the Substrate-Binding Pocket of MexB.The protein journal · 2026Review
- Computer Simulations of Multidrug Efflux Pumps of the Resistance-Nodulation-Cell Division Superfamily.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Alanine Scanning Analysis of MexB in Multidrug-Resistant Pseudomonas aeruginosa Using the Native Type I-F CRISPR-Cas-Mediated Genome Editing.Methods in molecular biology (Clifton, N.J.) · 2026Article
- RND efflux pump inhibitor-like natural products as antibiotic adjuvants against multidrug-resistant gram-negative bacteria: a graded-evidence review.Frontiers in microbiology · 2026Review
- Conformational plasticity across phylogenetic clusters of RND multidrug efflux pumps and its impact on substrate specificity.Nature communications · 2025Article
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- Antimicrobial and Anti-Efflux Machinery of FDA-Approved Proton Pump Inhibitors and Vitamins AgainstMicroorganisms · 2025Article
- An alternative approach to combat multidrug-resistant bacteria: new insights into traditional Chinese medicine monomers combined with antibiotics.Advanced biotechnology · 2025Review
- Article
- First genome sequence and functional profiling ofFrontiers in microbiology · 2025Article
Corrections and comments
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tripartite multidrug efflux system MexAB-OprM is a major actor in Pseudomonas aeruginosa antibiotic resistance by exporting a large variety of antimicrobial compounds. Crystal structures of MexB and of its Escherichia coli homolog AcrB had revealed asymmetric trimers depicting a directional drug pathway by a conformational interconversion (from Loose and Tight binding pockets to Open gate (LTO) for drug exit). It remains unclear how MexB acquires its LTO form. Here by performing functional and cryo-EM structural investigations of MexB at various stages of the assembly process, we unveil that MexB inserted in lipid membrane is not set for active transport because it displays an inactive LTC form with a Closed exit gate. In the tripartite complex, OprM and MexA form a corset-like platform that converts MexB into the active form. Our findings shed new light on the resistance nodulation cell division (RND) cognate partners which act as allosteric factors eliciting the functional drug extrusion.
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