ArticleCommunications biology2024
Structural shifts in TolC facilitate Efflux-Mediated β-lactam resistance.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Genetic profiling of the tolC component of the acrAB-TolC efflux pump in clinical Klebsiella pneumoniae isolates: a cross-sectional study in Pontianak, Indonesia.Osong public health and research perspectives · 2026Article
- The Omp85 family protein, TamA, exhibits characteristics of a suitable drug target againstMicrobiology (Reading, England) · 2026Article
- Clinical breakpoint meropenem concentration modulate outer membrane vesicle production in enterotoxigenic Bacteroides fragilis.Archives of microbiology · 2025Article
- Based on quorum sensing: reverse effect of traditional Chinese medicine on bacterial drug resistance mechanism.Frontiers in cellular and infection microbiology · 2025Review
- Multidrug resistance in Pseudomonas aeruginosa: genetic control mechanisms and therapeutic advances.Molecular biomedicine · 2024Review
- Structural shifts in TolC facilitate Efflux-Mediated β-lactam resistance.Communications biology · 2024Article
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Authors and funding
7 authors.
Funding
Abstract
Efflux-mediated β-lactam resistance is a major public health concern, reducing the effectiveness of β-lactam antibiotics against many bacteria. Structural analyses show the efflux protein TolC in Gram-negative bacteria acts as a channel for antibiotics, impacting bacterial susceptibility and virulence. This study examines β-lactam drug efflux mediated by TolC using experimental and computational methods. Molecular dynamics simulations of drug-free TolC reveal essential movements and key residues involved in TolC opening. A whole-gene-saturation mutagenesis assay, mutating each TolC residue and measuring fitness effects under β-lactam selection, is performed. Here we show the TolC-mediated efflux of three antibiotics: oxacillin, piperacillin, and carbenicillin. Steered molecular dynamics simulations identify general and drug-specific efflux mechanisms, revealing key positions at TolC's periplasmic entry affecting efflux motions. Our findings provide insights into TolC's structural dynamics, aiding the design of new antibiotics to overcome bacterial efflux mechanisms.
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Registered trials
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