ArticleThe Journal of antimicrobial chemotherapy2014
Target optimization for peptide nucleic acid (PNA)-mediated antisense inhibition of the CmeABC multidrug efflux pump in Campylobacter jejuni.
Article in The Journal of antimicrobial chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Developing antisense oligomer biotics "asobiotics" as precision antibacterials: designs, strategies, and considerations for future success.FEMS microbiology reviews · 2026Review
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- Identifying Cell-Penetrating Peptides for Effectively Delivering Antimicrobial Molecules intoAntibiotics (Basel, Switzerland) · 2024Article
- Promising strategies employing nucleic acids as antimicrobial drugs.Molecular therapy. Nucleic acids · 2024Review
- Sequence-Specific Gene Silencing of acrA in the Multi-drug Efflux System AcrAB Induces Sensitivity in Drug-Resistant Klebsiella pneumoniae.Molecular biotechnology · 2023Article
- Design and off-target prediction for antisense oligomers targeting bacterial mRNAs with the MASON web server.RNA (New York, N.Y.) · 2023Article
- Antimicrobial Activity of Peptide-Coupled Antisense Peptide Nucleic Acids in Streptococcus pneumoniae.Microbiology spectrum · 2022Article
- Developing New Tools to Fight Human Pathogens: A Journey through the Advances in RNA Technologies.Microorganisms · 2022Review
- Antisense inhibition of the Escherichia coli NrdAB aerobic ribonucleotide reductase is bactericidal due to induction of DNA strand breaks.The Journal of antimicrobial chemotherapy · 2021Article
- Evaluation of accessible regions ofIranian journal of microbiology · 2021Article
- Bacterial Nosocomial Infections: Multidrug Resistance as a Trigger for the Development of Novel Antimicrobials.Antibiotics (Basel, Switzerland) · 2021Review
- Therapeutic effects, immunogenicity and cytotoxicity of a cell penetrating peptide-peptide nucleic acid conjugate againstIranian journal of microbiology · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- New and alternative strategies for the prevention, control, and treatment of antibiotic-resistant Campylobacter.Translational research : the journal of laboratory and clinical medicine · 2020Review
- Antisense peptide nucleic acids as a potential anti-infective agent.Journal of microbiology (Seoul, Korea) · 2019Review
- Advances in therapeutic bacterial antisense biotechnology.Applied microbiology and biotechnology · 2018Review
- Peptide nucleic acids: Advanced tools for biomedical applications.Journal of biotechnology · 2017Review
- Antisense antimicrobial therapeutics.Current opinion in microbiology · 2016Review
- Silencing of Essential Genes within a Highly Coordinated Operon in Escherichia coli.Applied and environmental microbiology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
objectivesCmeABC is a resistance-nodulation-cell division (RND)-type multidrug efflux pump conferring resistance to clinically important antibiotics in Campylobacter. This study aimed to identify the optimal target sites for the inhibition of CmeABC with antisense peptide nucleic acid (PNA).
methodsEighteen PNAs were designed to bind to the translational initiation regions of cmeABC, spanning the ribosome-binding site (RBS) and the start codon of the cmeABC genes. Campylobacter jejuni was treated with CmeABC-specific PNAs (CmeABC-PNAs) at various concentrations and subjected to western blotting to measure changes in the level of CmeABC expression. The MICs of ciprofloxacin and erythromycin were measured to evaluate the impact of CmeABC knockdown on antibiotic susceptibility.
resultsWhile antisense PNA significantly affected CmeA and CmeB expression, interestingly, CmeC expression was not altered by any of the CmeC-PNAs used in this study. A CmeA-PNA targeting the RBS of cmeA and its upstream region reduced CmeA expression most efficiently, and CmeB expression was most significantly decreased by PNA binding to the RBS of cmeB and its downstream region. CmeA- and CmeB-PNAs increased the susceptibility of C. jejuni to ciprofloxacin and erythromycin in proportion to the inhibition levels observed in western blotting.
conclusionsThe cmeA gene is the best target to knockdown CmeABC with antisense PNA. The RBS is the major target for the PNA-mediated antisense inhibition of CmeABC. However, regions in its vicinity also significantly influence the effectiveness of the PNA-based knockdown of CmeABC.
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