ArticleAntimicrobial agents and chemotherapy2013
Changes to its peptidoglycan-remodeling enzyme repertoire modulate β-lactam resistance in Pseudomonas aeruginosa.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 73 citations in OpenAlex.
- Molecular determinants associated with resistance to imipenem and imipenem-relebactam in clinical Pseudomonas aeruginosa isolates.BMC genomics · 2026Article
- Prevalence and mechanisms of high-level carbapenem antibiotic tolerance in clinical isolates of Klebsiella pneumoniae.PLoS pathogens · 2026Article
- Structural Characterization of Lytic Transglycosylase SltB2 ofACS omega · 2025Article
- Temocillin: A Narrative Review of Its Clinical Reappraisal.Antibiotics (Basel, Switzerland) · 2025Review
- Evolution of Resistant Mutants inMicroorganisms · 2025Article
- Azithromycin represses evolution of ceftazidime/avibactam resistance by translational repression ofJournal of bacteriology · 2025Article
- Perturbation ofmBio · 2025Article
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- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Structural characterization of lytic transglycosylase MltD of Pseudomonas aeruginosa, a target for the natural product bulgecin A.International journal of biological macromolecules · 2024Article
- Cell envelope structural and functional contributions to antibiotic resistance inJournal of bacteriology · 2024Article
- A new variant of the colistin resistance gene MCR-1 with co-resistance to β-lactam antibiotics reveals a potential novel antimicrobial peptide.PLoS biology · 2023Article
- Article
- In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.Communications biology · 2022Article
- Cefazolin and imipenem enhance AmpC expression and resistance in NagZ-dependent manner in Enterobacter cloacae complex.BMC microbiology · 2022Article
- β-Lactam Resistance inJournal of bacteriology · 2022Article
- Responses of carbapenemase-producing and non-producing carbapenem-resistantFrontiers in microbiology · 2022Article
- The Building Blocks of Antimicrobial Resistance inFrontiers in cellular and infection microbiology · 2021Review
- Modulation of Peptidoglycan Synthesis by Recycled Cell Wall Tetrapeptides.Cell reports · 2020Article
- Article
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5 authors at 1 institution in 1 country.
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Abstract
Pseudomonas aeruginosa is a leading cause of hospital-acquired infections and is resistant to many antibiotics. Among its primary mechanisms of resistance is expression of a chromosomally encoded AmpC β-lactamase that inactivates β-lactams. The mechanisms leading to AmpC expression in P. aeruginosa remain incompletely understood but are intricately linked to cell wall metabolism. To better understand the roles of peptidoglycan-active enzymes in AmpC expression-and consequent β-lactam resistance-a phenotypic screen of P. aeruginosa mutants lacking such enzymes was performed. Mutants lacking one of four lytic transglycosylases (LTs) or the nonessential penicillin-binding protein PBP4 (dacB) had altered β-lactam resistance. mltF and slt mutants with reduced β-lactam resistance were designated WIMPs (wall-impaired mutant phenotypes), while highly resistant dacB, sltB1, and mltB mutants were designated HARMs (high-level AmpC resistant mutants). Double mutants lacking dacB and sltB1 had extreme piperacillin resistance (>256 μg/ml) compared to either of the single knockouts (64 μg/ml for a dacB mutant and 12 μg/ml for an sltB1 mutant). Inactivation of ampC reverted these mutants to wild-type susceptibility, confirming that AmpC expression underlies resistance. dacB mutants had constitutively elevated AmpC expression, but the LT mutants had wild-type levels of AmpC in the absence of antibiotic exposure. These data suggest that there are at least two different pathways leading to AmpC expression in P. aeruginosa and that their simultaneous activation leads to extreme β-lactam resistance.
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