ReviewFrontiers in microbiology2015
Mechanism of coupling drug transport reactions located in two different membranes.
Review in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 62 citations in OpenAlex.
- Antimicrobial efficacy of carbon nanotube-based nano drug onBiochemistry and biophysics reports · 2026Article
- Computer Simulations of Multidrug Efflux Pumps of the Resistance-Nodulation-Cell Division Superfamily.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A review of research progress on periplasmic adaptor proteins in bacterial tripartite pumps.Frontiers in microbiology · 2026Review
- Dual-function regulator MexL as a target to control phenazines production and pathogenesis of Pseudomonas aeruginosa.Nature communications · 2025Article
- Molecular Mechanism of Ciprofloxacin Translocation Through the Major Diffusion Channels of the ESKAPE PathogensThe journal of physical chemistry. B · 2024Article
- MgbioRxiv : the preprint server for biology · 2024Article
- A Genetic Locus inAntibiotics (Basel, Switzerland) · 2024Article
- The role of TMS 12 in the staphylococcal multidrug efflux protein QacA.The Journal of antimicrobial chemotherapy · 2023Article
- Global genomic epidemiology of chromosomally mediated non-enzymatic carbapenem resistance inFrontiers in microbiology · 2023Article
- A Model for Allosteric Communication in Drug Transport by the AcrAB-TolC Tripartite Efflux Pump.Antibiotics (Basel, Switzerland) · 2022Article
- Preparation, urease inhibition mechanisms, and anti-Current research in microbial sciences · 2022Article
- Molecular rationale for the impairment of the MexAB-OprM efflux pump by a single mutation in MexA.Computational and structural biotechnology journal · 2022Article
- Loss of RND-Type Multidrug Efflux Pumps Triggers Iron Starvation and Lipid A Modifications in Pseudomonas aeruginosa.Antimicrobial agents and chemotherapy · 2021Article
- Insight into the AcrAB-TolC Complex Assembly Process Learned from Competition Studies.Antibiotics (Basel, Switzerland) · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- A "Drug Sweeping" State of the TriABC Triclosan Efflux Pump from Pseudomonas aeruginosa.Structure (London, England : 1993) · 2021Article
- Biofilms as Promoters of Bacterial Antibiotic Resistance and Tolerance.Antibiotics (Basel, Switzerland) · 2020Review
- Kinetic and Equilibrium Studies of Doxorubicin Adsorption onto Carbon Nanotubes.International journal of molecular sciences · 2020Article
- Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.ACS infectious diseases · 2020Review
- Permeability barriers of Gram-negative pathogens.Annals of the New York Academy of Sciences · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Gram- negative bacteria utilize a diverse array of multidrug transporters to pump toxic compounds out of the cell. Some transporters, together with periplasmic membrane fusion proteins (MFPs) and outer membrane channels, assemble trans-envelope complexes that expel multiple antibiotics across outer membranes of Gram-negative bacteria and into the external medium. Others further potentiate this efflux by pumping drugs across the inner membrane into the periplasm. Together these transporters create a powerful network of efflux that protects bacteria against a broad range of antimicrobial agents. This review is focused on the mechanism of coupling transport reactions located in two different membranes of Gram-negative bacteria. Using a combination of biochemical, genetic and biophysical approaches we have reconstructed the sequence of events leading to the assembly of trans-envelope drug efflux complexes and characterized the roles of periplasmic and outer membrane proteins in this process. Our recent data suggest a critical step in the activation of intermembrane efflux pumps, which is controlled by MFPs. We propose that the reaction cycles of transporters are tightly coupled to the assembly of the trans-envelope complexes. Transporters and MFPs exist in the inner membrane as dormant complexes. The activation of complexes is triggered by MFP binding to the outer membrane channel, which leads to a conformational change in the membrane proximal domain of MFP needed for stimulation of transporters. The activated MFP-transporter complex engages the outer membrane channel to expel substrates across the outer membrane. The recruitment of the channel is likely triggered by binding of effectors (substrates) to MFP or MFP-transporter complexes. This model together with recent structural and functional advances in the field of drug efflux provides a fairly detailed understanding of the mechanism of drug efflux across the two membranes.
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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.