ArticleThe Journal of antimicrobial chemotherapy2024
Impact of chromosomally encoded resistance mechanisms and transferable β-lactamases on the activity of cefiderocol and innovative β-lactam/β-lactamase inhibitor combinations against Pseudomonas aeruginosa.
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 23 papers.
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Who cites it
23 citing papers in PubMed.
- Breaking the deadlock of metallo-β-lactamases: evidence and prospects for Aztreonam/Avibactam.Emerging microbes & infections · 2026Review
- Transcriptional regulation drives heteroresistance inmSystems · 2026Article
- Beyond Carbapenemases: Chromosomal Resistance Mechanisms and Carbapenemase Type Determine Susceptibility to Novel β-Lactam/β-Lactamase Inhibitor Combinations and Cefiderocol in Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026Article
- Mechanisms involved in cefiderocol resistance in FrenchAntimicrobial agents and chemotherapy · 2026Article
- Cefiderocol nonsusceptibility among carbapenem-resistantAntimicrobial agents and chemotherapy · 2026Article
- Genetic and biochemical characterization of OXA-1054, a carbapenem-hydrolyzing class D β-lactamase conferring broad-spectrum β-lactam resistance inAntimicrobial agents and chemotherapy · 2026Article
- Emergence of KPC-producingAntimicrobial agents and chemotherapy · 2026Article
- Loss of the ferripyochelin receptor FptA drives reduced cefiderocol susceptibility and impairs fitness inAntimicrobial agents and chemotherapy · 2026Article
- Cefepime Combined with Late-Generation β-Lactamase Inhibitors: Mechanisms of Action, In Vitro Activity, PK/PD Characteristics, Clinical Evidence and Resistance Mechanisms.Antibiotics (Basel, Switzerland) · 2026Review
- Mechanisms ofMedicina (Kaunas, Lithuania) · 2026Review
- Pan-ResistantClinical medicine insights. Case reports · 2026Article
- Metallo-β-lactamase-producingFrontiers in microbiology · 2026Review
- Contribution of mutational resistance mechanisms and acquired β-lactamases to cefiderocol/xeruborbactam susceptibility inAntimicrobial agents and chemotherapy · 2025Article
- Efficacy of cefiderocol in combination with xeruborbactam versus taniborbactam against cefiderocol-resistant NDM-producingAntimicrobial agents and chemotherapy · 2025Article
- Loss of the Ferripyochelin Receptor FptA Drives Reduced Cefiderocol Susceptibility and Impairs Fitness inbioRxiv : the preprint server for biology · 2025Article
- The emerging concern of IMP variants being resistant to the only IMP-type metallo-β-lactamase inhibitor, xeruborbactam.Antimicrobial agents and chemotherapy · 2025Article
- CombattingAntibiotics (Basel, Switzerland) · 2025Review
- Rapid prediction of carbapenemases inJournal of clinical microbiology · 2025Article
- Spectrum of cefepime-taniborbactam coverage against 190 β-lactamases defined in engineered isogenicAntimicrobial agents and chemotherapy · 2025Article
- In vitro activity and resistance mechanisms of novel antimicrobial agents against metallo-β-lactamase producers.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Review
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16 authors.
Funding
Abstract
objectivesWe aimed to compare the stability of the newly developed β-lactams (cefiderocol) and β-lactam/β-lactamase inhibitor combinations (ceftazidime/avibactam, ceftolozane/tazobactam, aztreonam/avibactam, cefepime/taniborbactam, cefepime/zidebactam, imipenem/relebactam, meropenem/vaborbactam, meropenem/nacubactam and meropenem/xeruborbactam) against the most clinically relevant mechanisms of mutational and transferable β-lactam resistance in Pseudomonas aeruginosa.
methodsWe screened a collection of 61 P. aeruginosa PAO1 derivatives. Eighteen isolates displayed the most relevant mechanisms of mutational resistance to β-lactams. The other 43 constructs expressed transferable β-lactamases from genes cloned in pUCP-24. MICs were determined by reference broth microdilution.
resultsCefiderocol and imipenem/relebactam exhibited excellent in vitro activity against all of the mutational resistance mechanisms studied. Aztreonam/avibactam, cefepime/taniborbactam, cefepime/zidebactam, meropenem/vaborbactam, meropenem/nacubactam and meropenem/xeruborbactam proved to be more vulnerable to mutational events, especially to overexpression of efflux operons. The agents exhibiting the widest spectrum of activity against transferable β-lactamases were aztreonam/avibactam and cefepime/zidebactam, followed by cefepime/taniborbactam, cefiderocol, meropenem/xeruborbactam and meropenem/nacubactam. However, some MBLs, particularly NDM enzymes, may affect their activity. Combined production of certain enzymes (e.g. NDM-1) with increased MexAB-OprM-mediated efflux and OprD deficiency results in resistance to almost all agents tested, including last options such as aztreonam/avibactam and cefiderocol.
conclusionsCefiderocol and new β-lactam/β-lactamase inhibitor combinations show promising and complementary in vitro activity against mutational and transferable P. aeruginosa β-lactam resistance. However, the combined effects of efflux pumps, OprD deficiency and efficient β-lactamases could still result in the loss of all therapeutic options. Resistance surveillance, judicious use of new agents and continued drug development efforts are encouraged.
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