ArticlePloS one2013
Polyamines inhibit porin-mediated fluoroquinolone uptake in mycobacteria.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The trial behind it
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
17 citing papers in PubMed, 30 citations in OpenAlex.
- Chemical-mediated alteration of antibiotic susceptibility: mechanisms and potential new targets for antibiotic adjuvant discovery.Journal of bacteriology · 2026Review
- The arginase-polyamine signaling axis in immune cells: Implications for immune modulation and host-pathogen interactions.iScience · 2026Review
- Overexpression of outer membrane protein A (OmpA) increases aminoglycoside sensitivity in mycobacteria.BMC microbiology · 2024Article
- Article
- Polyamine and Ethanolamine Metabolism in Bacteria as an Important Component of Nitrogen Assimilation for Survival and Pathogenicity.Medical sciences (Basel, Switzerland) · 2022Review
- Itaconate, Arginine, and Gamma-Aminobutyric Acid: A Host Metabolite Triad Protective Against Mycobacterial Infection.Frontiers in immunology · 2022Review
- Elucidating the Antimycobacterial Mechanism of Action of Ciprofloxacin Using Metabolomics.Microorganisms · 2021Article
- A Fluorogenic Trehalose Probe for Tracking PhagocytosedJournal of the American Chemical Society · 2020Article
- Comprehensive Examination of the Mouse Lung Metabolome FollowingJournal of proteome research · 2020Article
- The Macrophage Response toFrontiers in cellular and infection microbiology · 2020Review
- Identification of a Novel Polyamine Scaffold With Potent Efflux Pump Inhibition Activity Toward Multi-Drug Resistant Bacterial Pathogens.Frontiers in microbiology · 2018Article
- Antibiotic-Induced Changes to the Host Metabolic Environment Inhibit Drug Efficacy and Alter Immune Function.Cell host & microbe · 2017Article
- Gamma-Glutamylpolyamine Synthetase GlnA3 Is Involved in the First Step of Polyamine Degradation Pathway inFrontiers in microbiology · 2017Article
- Eagle Effect in Nonreplicating Persister Mycobacteria.Antimicrobial agents and chemotherapy · 2015Article
- UDP-N-acetylmuramic acid l-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death.Antimicrobial agents and chemotherapy · 2014Article
- The path of anti-tuberculosis drugs: from blood to lesions to mycobacterial cells.Nature reviews. Microbiology · 2014Review
- Porins increase copper susceptibility of Mycobacterium tuberculosis.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyamines decrease the permeability of the outer membrane of Escherichia coli to fluoroquinolones and β-lactams. In this study, we tested the effect of four polyamines (spermidine, spermine, cadaverine and putrescine) on fluoroquinolone uptake in Mycobacterium bovis BCG. Our results show that polyamines are also capable of reducing the permeability of the mycobacterial outer membrane to fluoroquinolones. Spermidine was most effective and demonstrated reversible dose- and pH-dependent inhibition of ciprofloxacin accumulation. The extent of this inhibition was demonstrated across the fluoroquinolone compound class to varying degrees. Furthermore, we have shown that the addition of spermidine increases the survival of M. bovis BCG after a 5-day exposure to ciprofloxacin by up to 25 times. The treatment of actively-replicating Mycobacterium tuberculosis with spermidine reduced ciprofloxacin accumulation by half while non-replicating nutrient-starved M. tuberculosis cultures lacked similar sensitivity to polyamines. Gene expression studies showed that several outer membrane proteins are significantly down-regulated during the shift to non-replication. Collectively, these characteristics of fluoroquinolone uptake in M. bovis BCG are consistent with facilitated transport by porin-like proteins and suggest that a reduction in intracellular uptake contributes to the phenotypic drug resistance demonstrated by M. tuberculosis in the non-replicating state.
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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.