ArticleProceedings of the National Academy of Sciences of the United States of America2013
Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
74 citing papers in PubMed, 152 citations in OpenAlex.
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- Exogenous glutamate potentiates gentamicin to kill multidrug- and carbapenem-resistantmSystems · 2025Article
- Unraveling the mechanisms behind the enhanced efficacy of β-lactam-based sideromycins.Communications biology · 2025Article
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- Navigating the complexities of drug development for metallo-β-lactamase inhibitors.RSC medicinal chemistry · 2025Review
- Peptidoglycan-outer membrane attachment generates periplasmic pressure to prevent lysis in Gram-negative bacteria.Nature microbiology · 2025Article
- Outer membrane permeability ofMicrobiology spectrum · 2025Article
- Seeking Correlation Among Porin Permeabilities and Minimum Inhibitory Concentrations Through Machine Learning: A Promising Route to the Essential Molecular Descriptors.Molecules (Basel, Switzerland) · 2025Article
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- Glutamine potentiates cefoperazone-sulbactam activity againstFrontiers in microbiology · 2025Article
- Advances in methods and concepts provide new insight into antibiotic fluxes across the bacterial membrane.Communications biology · 2024Article
- Molecular Mechanism of Ciprofloxacin Translocation Through the Major Diffusion Channels of the ESKAPE PathogensThe journal of physical chemistry. B · 2024Article
- Semi-mechanistic modeling of resistance development to β-lactam and β-lactamase-inhibitor combinations.Journal of pharmacokinetics and pharmacodynamics · 2024Article
- Bioluminescence-Based Determination of Cytosolic Accumulation of Antibiotics inACS infectious diseases · 2024Article
- Multidrug efflux in Gram-negative bacteria: structural modifications in active compounds leading to efflux pump avoidance.npj antimicrobials and resistance · 2024Article
- Fosfomycin Uptake inACS infectious diseases · 2024Article
- Guiding the Way: Traditional Medicinal Chemistry Inspiration for Rational Gram-Negative Drug Design.Journal of medicinal chemistry · 2024Review
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Small, hydrophilic compounds such as β-lactams diffuse across the outer membrane of Gram-negative bacteria through porin channels, which were originally thought to be nonspecific channels devoid of any specificity. However, since the discovery of an ampicillin-binding site within the OmpF channel in 2002, much attention has been focused on the potential specificity of the channel, where the binding site was assumed either to facilitate or to retard the penetration of β-lactams. Since the earlier studies on porin permeability were done without the knowledge of the contribution of multidrug efflux pumps in the overall flux process across the cell envelope, in this study we have carefully studied both the porin permeability and active efflux of ampicillin and benzylpenicillin. We found that the influx occurs apparently by a spontaneous passive diffusion without any indication of specific binding within the concentration range relevant to the antibiotic action of these drugs, and that the higher permeability for ampicillin is totally as expected from the gross property of this drug as a zwitterionic compound. The active efflux by AcrAB was more effective for benzylpenicillin due to the stronger affinity and high degree of positive cooperativity. Our data now give a complete quantitative picture of the influx, efflux, and periplasmic degradation (catalyzed by AmpC β-lactamase) of these two compounds, and correlate closely with the susceptibility of Escherichia coli strains used here, thus validating not only our model but also the parameters obtained in this study.
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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.