ArticleAntimicrobial agents and chemotherapy2012
Expression of OXA-type and SFO-1 β-lactamases induces changes in peptidoglycan composition and affects bacterial fitness.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 59 citations in OpenAlex.
- Antibiotic-induced gut microbiome dysbiosis: risks and strategies for mitigation.The EMBO journal · 2026Review
- Characterization of outer membrane vesicles from Acinetobacter haemolyticus and their role in the dissemination of carbapenem resistance.Medical microbiology and immunology · 2026Article
- Phage-meropenem synergy against OXA-48-producing Klebsiella pneumoniae clinical isolates.npj antimicrobials and resistance · 2026Article
- Extended-Spectrum β-Lactamase-ProducingAntibiotics (Basel, Switzerland) · 2025Review
- The lipoprotein biosynthesis pathway: key to OXA-mediated carbapenem resistance inAntimicrobial agents and chemotherapy · 2025Article
- Subinhibitory Concentrations of Oxacillin Alter Motility, Biofilm Production, and Transformation Capability of the Oxacillinase-Producing Acinetobacter baumannii.Current microbiology · 2025Article
- Dissecting pOXA-48 fitness effects in clinical Enterobacterales using plasmid-wide CRISPRi screens.Nature communications · 2025Article
- Molecular insights into the evolutionary trajectory of aAntimicrobial agents and chemotherapy · 2024Article
- Impact of multidrug resistance on the virulence and fitness of Pseudomonas aeruginosa: a microbiological and clinical perspective.Infection · 2024Review
- β-lactamase expression induces collateral sensitivity in Escherichia coli.Nature communications · 2024Article
- Costs of antibiotic resistance genes depend on host strain and environment and can influence community composition.Proceedings. Biological sciences · 2024Article
- Transferable AmpCs inAntimicrobial agents and chemotherapy · 2024Article
- The Biofilm Lifestyle Shapes the Evolution of β-Lactamases.Genome biology and evolution · 2024Article
- Article
- Filling knowledge gaps related to AmpC-dependent β-lactam resistance in Enterobacter cloacae.Scientific reports · 2024Article
- In vitro and in vivo evaluation of two combined β-lactamase inhibitors against carbapenem-resistant Acinetobacter baumannii.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2023Article
- Bacterial virulence regulation through soluble peptidoglycan fragments sensing and response: knowledge gaps and therapeutic potential.FEMS microbiology reviews · 2023Article
- Sub-MIC antibiotics influence the microbiome, resistome and structure of riverine biofilm communities.Frontiers in microbiology · 2023Article
- The balance between antibiotic resistance and fitness/virulence inFrontiers in microbiology · 2023Review
- Virulence genes, phylogenetic analysis, and antimicrobial resistance of Escherichia coli isolated from urinary tract infection in hospitalized patients and outpatients.Journal of applied genetics · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Lactamases and penicillin-binding proteins (PBPs) have evolved from a common ancestor. β-Lactamases are enzymes that degrade β-lactam antibiotics, whereas PBPs are involved in the synthesis and processing of peptidoglycan, which forms an elastic network in the bacterial cell wall. This study analyzed the interaction between β-lactamases and peptidoglycan and the impact on fitness and biofilm production. A representative set of all classes of β-lactamases was cloned in the expression vector pBGS18 under the control of the CTX-M promoter and expressed in Escherichia coli MG1655. The peptidoglycan composition of all clones was evaluated, and quantitative changes were found in E. coli strains expressing OXA-24, OXA-10-like, and SFO-1 (with its upstream regulator AmpR) β-lactamases; the level of cross-linked muropeptides decreased, and their average length increased. These changes were associated with a statistically significant fitness cost, which was demonstrated in both in vitro and in vivo experiments. The observed changes in peptidoglycan may be explained by the presence of residual DD-endopeptidase activity in these β-lactamases, which may result in hydrolysis of the peptide cross bridge. The biological cost associated with these changes provides important data regarding the interaction between β-lactamases and the metabolism of peptidoglycan and may provide an explanation for the epidemiology of these β-lactamases in Enterobacteriaceae.
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