ArticleAntimicrobial agents and chemotherapy2024
Structural role of K224 in taniborbactam inhibition of NDM-1.
Article in Antimicrobial agents and chemotherapy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Boron-Based Bioisosteres in Medicinal Chemistry: Advances in Heterocycles and Therapeutic.ChemMedChem · 2026Review
- Cefepime 2.0: Upgrading β-Lactamase Inhibitor Use.Microorganisms · 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
- Spectrum of cefepime-taniborbactam coverage against 190 β-lactamases defined in engineered isogenicAntimicrobial agents and chemotherapy · 2025Article
- Impact of porin deletions on cefepime-taniborbactam activity againstAntimicrobial 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
- Breakthrough Advances in Beta-Lactamase Inhibitors: New Synthesized Compounds and Mechanisms of Action Against Drug-Resistant Bacteria.Pharmaceuticals (Basel, Switzerland) · 2025Review
- New antibiotics targeting Gram-negative bacilli.Le infezioni in medicina · 2025Review
- Review
- The metallo-β-lactamases strike back: emergence of taniborbactam escape variants.Antimicrobial agents and chemotherapy · 2024Review
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Taniborbactam (TAN; VNRX-5133) is a novel bicyclic boronic acid β-lactamase inhibitor (BLI) being developed in combination with cefepime (FEP). TAN inhibits both serine and some metallo-β-lactamases. Previously, the substitution R228L in VIM-24 was shown to increase activity against oxyimino-cephalosporins like FEP and ceftazidime (CAZ). We hypothesized that substitutions at K224, the homologous position in NDM-1, could impact FEP/TAN resistance. To evaluate this, a library of codon-optimized NDM K224X clones for minimum inhibitory concentration (MIC) measurements was constructed; steady-state kinetics and molecular docking simulations were next performed. Surprisingly, our investigation revealed that the addition of TAN restored FEP susceptibility only for NDM-1, as the MICs for the other 19 K224X variants remained comparable to those of FEP alone. Moreover, compared to NDM-1, all K224X variants displayed significantly lower MICs for imipenem, tebipenem, and cefiderocol (32-, 133-, and 33-fold lower, respectively). In contrast, susceptibility to CAZ was mostly unaffected. Kinetic assays with the K224I variant, the only variant with hydrolytic activity to FEP comparable to NDM-1, confirmed that the inhibitory capacity of TAN was modestly compromised (IC
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