ArticleThe Journal of antimicrobial chemotherapy2024
Penicillin-binding protein 3 sequence variations reduce susceptibility of Pseudomonas aeruginosa to β-lactams but inhibit cell division.
Article in The Journal of antimicrobial chemotherapy, 2024. 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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17 citing papers in PubMed.
- Altered regulation of septal peptidoglycan synthesis modulates β-lactam susceptibility in Pseudomonas aeruginosa.PLoS genetics · 2026Article
- Characterizing the V516M penicillin-binding protein 2 (PBP2) mutation causing zidebactam resistance inAntimicrobial agents and chemotherapy · 2026Article
- Integrating resistance biology, virulence networks, and precision therapeutics against multidrug-resistant Pseudomonas aeruginosa.Infection · 2026Review
- Hi-C Metagenome Deconvolution of Double-Crested Cormorant (Microorganisms · 2026Article
- Glnk Mediates Carbapenem Resistance Through the NtrB/NtrC-OprD Regulatory Pathway inPathogens (Basel, Switzerland) · 2026Article
- Novel Insights into Carbapenem Resistance: Mechanisms, Diagnostics, and Future Directions.Antibiotics (Basel, Switzerland) · 2026Review
- Antibiotic resistance inFrontiers in microbiology · 2026Review
- First nationwide survey onAntimicrobial agents and chemotherapy · 2025Article
- Bacteriophage-Based Approach Against Biofilm Infections Associated with Medical Devices: A Narrative Review of ESKAPE Pathogens.International journal of molecular sciences · 2025Review
- A unified annotation scheme for class D β-lactamases.Antimicrobial agents and chemotherapy · 2025Article
- Specific variants inMicrobiology spectrum · 2025Article
- Growth-Phase-Dependent Modulation of Quorum Sensing and Virulence Factors inAntibiotics (Basel, Switzerland) · 2025Article
- Direct and indirect pathways linking the Lon protease to motility behaviors in the pathogen Pseudomonas aeruginosa.PLoS pathogens · 2025Article
- Mutations leading to ceftolozane/tazobactam and imipenem/cilastatin/relebactam resistance duringMicrobiology spectrum · 2025Article
- Mechanisms, therapeutic strategies, and emerging therapeutic alternatives for carbapenem resistance in Gram-negative bacteria.Archives of microbiology · 2025Review
- Article
- Resistance mechanisms and therapeutic strategies forTherapeutic advances in infectious diseaseReview
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2 authors.
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Abstract
backgroundβ-lactam antibiotics, which inhibit penicillin-binding protein 3 (PBP3) that is required for cell division, play a key role in treating P. aeruginosa infections. Some sequence variations in PBP3 have been associated with β-lactam resistance but the effects of variations on antibiotic susceptibility and on cell division have not been quantified. Antibiotic efflux can also reduce susceptibility.
objectivesTo quantify the effects of PBP3 variations on β-lactam susceptibility and cell morphology in P. aeruginosa.
methodsNineteen PBP3 variants were expressed from a plasmid in the reference strain P. aeruginosa PAO1 and genome engineering was used to construct five mutants expressing PBP3 variants from the chromosome. The effects of the variations on β-lactam minimum inhibitory concentration (MIC) and cell morphology were measured.
resultsSome PBP3 variations reduced susceptibility to a variety of β-lactam antibiotics including meropenem, ceftazidime, cefepime and ticarcillin with different variations affecting different antibiotics. None of the tested variations reduced susceptibility to imipenem or piperacillin. Antibiotic susceptibility was further reduced when PBP3 variants were expressed in mutant bacteria overexpressing the MexAB-OprM efflux pump, with some variations conferring clinical levels of resistance. Some PBP3 variations, and sub-MIC levels of β-lactams, reduced bacterial growth rates and inhibited cell division, causing elongated cells.
conclusionsPBP3 variations in P. aeruginosa can increase the MIC of multiple β-lactam antibiotics, although not imipenem or piperacillin. PBP3 variations, or the presence of sub-lethal levels of β-lactams, result in elongated cells indicating that variations reduce the activity of PBP3 and may reduce bacterial fitness.
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