ArticleAntimicrobial agents and chemotherapy2020
Structural Basis and Binding Kinetics of Vaborbactam in Class A β-Lactamase Inhibition.
Article in Antimicrobial agents and chemotherapy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Genomic and molecular characterisation of a KPC-producing Klebsiella pneumoniae clinical isolate resistant to meropenem-vaborbactam, imipenem-relebactam, and ceftazidime-avibactam.BMC genomic data · 2026Article
- Aminoglycosides enhance meropenem/vaborbactam activity against KPC-producingAntimicrobial agents and chemotherapy · 2026Article
- Reclaiming the Microbial Battlefield: Adjuvant Strategies to Overcome Antibiotic Resistance.Microorganisms · 2026Review
- Phosphate sensitivity of KPC-2: a hidden variable in β-lactamase kinetics.Antimicrobial agents and chemotherapy · 2026Article
- Structural perspectives on clinical β-lactamase inhibitors: From mechanism to resistance.Journal of microbiology (Seoul, Korea) · 2026Review
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Covalent Irreversible Inhibitors of Tetracycline Destructases.ACS infectious diseases · 2025Article
- Adverse Event Signals Associated with Beta-Lactamase Inhibitors: Disproportionality Analysis of USFDA Adverse Event Reporting System.Journal of xenobiotics · 2025Article
- Therapeutic drug monitoring (TDM) of β-lactam/β-lactamase inhibitor (BL/BLI) drug combinations: insights from a pharmacometric simulation study.The Journal of antimicrobial chemotherapy · 2025Article
- Trends on Potential Boron-containing Drugs by Advancements in Ligand-protein Crystals Complexes.Current medicinal chemistry · 2025Review
- Time-resolved crystallography of boric acid binding to the active site serine of the β-lactamase CTX-M-14 and subsequent 1,2-diol esterification.Communications chemistry · 2024Article
- Meropenem/Vaborbactam-A Mechanistic Review for Insight into Future Development of Combinational Therapies.Antibiotics (Basel, Switzerland) · 2024Review
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Recent Developments to Cope the Antibacterial Resistance via β-Lactamase Inhibition.Molecules (Basel, Switzerland) · 2022Review
- Boron-based hybrids as novel scaffolds for the development of drugs with neuroprotective properties.RSC medicinal chemistry · 2021Article
- Assessing the Potency of β-Lactamase Inhibitors with Diverse Inactivation Mechanisms against the PenA1 Carbapenemase fromACS infectious diseases · 2021Article
- Article
- QPX7728, An Ultra-Broad-Spectrum B-Lactamase Inhibitor for Intravenous and Oral Therapy: Overview of Biochemical and Microbiological Characteristics.Frontiers in microbiology · 2021Review
- Activity of Aztreonam in Combination with Avibactam, Clavulanate, Relebactam, and Vaborbactam against Multidrug-Resistant Stenotrophomonas maltophilia.Antimicrobial agents and chemotherapy · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Class A β-lactamases are a major cause of β-lactam resistance in Gram-negative bacteria. The recently FDA-approved cyclic boronate vaborbactam is a reversible covalent inhibitor of class A β-lactamases, including CTX-M extended-spectrum β-lactamase and KPC carbapenemase, both frequently observed in the clinic. Intriguingly, vaborbactam displayed different binding kinetics and cell-based activity for these two enzymes, despite their similarity. A 1.0-Å crystal structure of CTX-M-14 demonstrated that two catalytic residues, K73 and E166, are positively charged and neutral, respectively. Meanwhile, a 1.25-Å crystal structure of KPC-2 revealed a more compact binding mode of vaborbactam versus CTX-M-14, as well as alternative conformations of W105. Together with kinetic analysis of W105 mutants, the structures demonstrate the influence of this residue and the unusual conformation of the β3 strand on the inactivation rate, as well as the stability of the reversible covalent bond with S70. Furthermore, studies of KPC-2 S130G mutant shed light on the different impacts of S130 in the binding of vaborbactam versus avibactam, another recently approved β-lactamase inhibitor. Taken together, these new data provide valuable insights into the inhibition mechanism of vaborbactam and future development of cyclic boronate inhibitors.
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