ArticleAntimicrobial agents and chemotherapy2017
Penicillin-Binding Protein 3 Is Essential for Growth of Pseudomonas aeruginosa.
Article in Antimicrobial agents and chemotherapy, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 68 citations in OpenAlex.
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- High level non-carbapenemase carbapenem resistance by overlaying mutations ofMicrobiology spectrum · 2025Article
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- Penicillin-binding protein 3 sequence variations reduce susceptibility of Pseudomonas aeruginosa to β-lactams but inhibit cell division.The Journal of antimicrobial chemotherapy · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Penicillin-Binding Protein 5/6 Acting as a Decoy Target in Pseudomonas aeruginosa Identified by Whole-Cell Receptor Binding and Quantitative Systems Pharmacology.Antimicrobial agents and chemotherapy · 2023Article
- β-Lactam Resistance in ESKAPE Pathogens Mediated Through Modifications in Penicillin-Binding Proteins: An Overview.Infectious diseases and therapy · 2023Review
- Genomic attributes of Vibrio cholerae O1 responsible for 2022 massive cholera outbreak in Bangladesh.Nature communications · 2023Article
- Revisiting ESKAPE Pathogens: virulence, resistance, and combating strategies focusing on quorum sensing.Frontiers in cellular and infection microbiology · 2023Review
- Resveratrol-Schiff Base Hybrid Compounds with Selective Antibacterial Activity: Synthesis, Biological Activity, and Computational Study.Microorganisms · 2022Article
- Effects of Inactivation of d,d-Transpeptidases of Acinetobacter baumannii on Bacterial Growth and Susceptibility to β-Lactam Antibiotics.Antimicrobial agents and chemotherapy · 2022Article
- Responses of carbapenemase-producing and non-producing carbapenem-resistantFrontiers in microbiology · 2022Article
- β-lactam Resistance inPathogens (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Penicillin-binding proteins (PBPs) function as transpeptidases, carboxypeptidases, or endopeptidases during peptidoglycan synthesis in bacteria. As the well-known drug targets for β-lactam antibiotics, the physiological functions of PBPs and whether they are essential for growth are of significant interest. The pathogen Pseudomonas aeruginosa poses a particular risk to immunocompromised and cystic fibrosis patients, and infections caused by this pathogen are difficult to treat due to antibiotic resistance. To identify potential drug targets among the PBPs in P. aeruginosa, we performed gene knockouts of all the high-molecular-mass (HMM) PBPs and determined the impacts on cell growth and morphology, susceptibility to β-lactams, peptidoglycan structure, virulence, and pathogenicity. Disruptions of the transpeptidase domains of most HMM PBPs, including double disruptions, had only minimal effects on cell growth. The exception was PBP3, where cell growth occurred only when the protein was conditionally expressed on an integrated plasmid. Conditional deletion of PBP3 also caused a defect in cell division and increased susceptibility to β-lactams. Knockout of PBP1a led to impaired motility, and this observation, together with its localization at the cell poles, suggests its involvement in flagellar function. Overall, these findings reveal that PBP3 represents the most promising target for drug discovery against P. aeruginosa, whereas other HMM PBPs have less potential.
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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.