ArticleAntimicrobial agents and chemotherapy2014
Avibactam and class C β-lactamases: mechanism of inhibition, conservation of the binding pocket, and implications for resistance.
Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers, 2 of them syntheses that pooled it.
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Who cites it
96 citing papers in PubMed, 2 syntheses or guidelines pooled it, 184 citations in OpenAlex.
- Tackling the Antibiotic Resistance Caused by Class AInternational journal of molecular sciences · 2018Pooled it
- Pharmacological aspects and spectrum of action of ceftazidime-avibactam: a systematic review.Infection · 2018Pooled it
- NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Aztreonam-avibactam at the frontline: A dual-agent approach to metallo-β-lactamase resistance.The Journal of antibiotics · 2026Review
- Comparison of laboratory-developed methods for aztreonam plus ceftazidime-avibactam antimicrobial susceptibility testing for metallo-beta-lactamase-producing Enterobacterales.Journal of clinical microbiology · 2026Article
- Ceftazidime-avibactam resistance evolution inAntimicrobial agents and chemotherapy · 2026Article
- Synergistic Potential of Repurposing non-β-lactam Compounds as Class A serine β-lactamases Inhibitor: Insights from MolecularDocking, Molecular Dynamics Simulations and Antimicrobial Potentiation.Scientific reports · 2026Article
- Structural perspectives on clinical β-lactamase inhibitors: From mechanism to resistance.Journal of microbiology (Seoul, Korea) · 2026Review
- Cefepime and New Cefepime/Beta-Lactamase Inhibitor Combination for the Treatment of Gram-Negative Bacteria: Chemical Structure and Mechanism of Action, Microbiological Target, Clinical Use and PK/PD Characteristics.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Unravelling the triad of penicillin-binding proteins, β-lactamase activity, and mRNA dynamics in Pseudomonas aeruginosa AmpC induction.The Journal of antimicrobial chemotherapy · 2026Article
- Integrated machine learning, molecular dynamics, and density functional theory approaches for identifying potential inhibitor targeting TEM 𝛽-lactamase inFrontiers in bioinformatics · 2026Article
- Amphiphilic nebramine analogs synergize with β-lactam/β-lactamase inhibitor combinations, including cefepime-taniborbactam and meropenem-xeruborbactam against metallo-β-lactamase-carryingRSC medicinal chemistry · 2025Article
- A model-based evaluation of the pharmacokinetics-pharmacodynamics (PKPD) of avibactam in combination with ceftazidime.JAC-antimicrobial resistance · 2025Article
- β-Lactamase diversity inAntimicrobial agents and chemotherapy · 2025Article
- A New Insight into Phage Combination Therapeutic Approaches Against Drug-Resistant Mixed Bacterial Infections.PHAGE (New Rochelle, N.Y.) · 2024Review
- Characterization of acquired β-lactamases inMicrobiology spectrum · 2024Article
- Emergence of high-level aztreonam-avibactam and cefiderocol resistance following treatment of an NDM-producingJAC-antimicrobial resistance · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
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36 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Avibactam is a novel non-β-lactam β-lactamase inhibitor that inhibits a wide range of β-lactamases. These include class A, class C, and some class D enzymes, which erode the activity of β-lactam drugs in multidrug-resistant pathogens like Pseudomonas aeruginosa and Enterobacteriaceae spp. Avibactam is currently in clinical development in combination with the β-lactam antibiotics ceftazidime, ceftaroline fosamil, and aztreonam. Avibactam has the potential to be the first β-lactamase inhibitor that might provide activity against class C-mediated resistance, which represents a growing concern in both hospital- and community-acquired infections. Avibactam has an unusual mechanism of action: it is a covalent inhibitor that acts via ring opening, but in contrast to other currently used β-lactamase inhibitors, this reaction is reversible. Here, we present a high-resolution structure of avibactam bound to a class C β-lactamase, AmpC, from P. aeruginosa that provided insight into the mechanism of both acylation and recyclization in this enzyme class and highlighted the differences observed between class A and class C inhibition. Furthermore, variants resistant to avibactam that identified the residues important for inhibition were isolated. Finally, the structural information was used to predict effective inhibition by sequence analysis and functional studies of class C β-lactamases from a large and diverse set of contemporary clinical isolates (P. aeruginosa and several Enterobacteriaceae spp.) obtained from recent infections to understand any preexisting variability in the binding pocket that might affect inhibition by avibactam.
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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.