ArticleAntimicrobial agents and chemotherapy2024
Structural basis of metallo-β-lactamase resistance to taniborbactam.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 30 citations in OpenAlex.
- The global epidemiology and treatment of metallo-β-lactamase-producing gram-negative pathogens.JAC-antimicrobial resistance · 2026Review
- Lanthipeptides fromMicrobiology spectrum · 2026Article
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Phenotypic and genotypic characterization of HMB-3, a metallo-beta-lactamase from Pseudomonas asiatica.The Journal of antimicrobial chemotherapy · 2026Article
- Clinically Significant Carbapenemases in Gram-Negative Pathogens: Molecular Diversity and Advances in β-Lactamase Inhibitor Therapy.Antibiotics (Basel, Switzerland) · 2026Review
- 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
- Clinical and molecular characterization of NDM-9 and NDM-13 producing multidrug-resistant Escherichia coli strains in China.BMC microbiology · 2026Article
- Article
- Light-Activated Metal-Dependent Protein Degradation: A Heterobifunctional Ruthenium(II) Photosensitizer Targeting New Delhi Metallo-β-lactamase 1.Journal of the American Chemical Society · 2025Article
- Structural insights into the activity of carbapenemases: understanding the mechanism of action of current inhibitors and informing the design of new carbapenem adjuvants.RSC medicinal chemistry · 2025Review
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- The global resistance problem and the clinical antibacterial pipeline.Nature reviews. Microbiology · 2025Review
- Cefiderocol "under siege"? Understanding the rise of NDM-mediated resistance to novel agents.Chemical science · 2025Article
- The emerging concern of IMP variants being resistant to the only IMP-type metallo-β-lactamase inhibitor, xeruborbactam.Antimicrobial agents and chemotherapy · 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
- Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors.Communications chemistry · 2025Article
- The NitroSpeed Taniborbactam NP test as a rapid test for detection of β-lactamase-mediated susceptibility to taniborbactam.FEMS microbiology letters · 2025Article
- Quantification of β-Lactamase Inhibition Using a Luminescent Whole-Cell Biosensor.Methods in molecular biology (Clifton, N.J.) · 2025Article
- New antibiotics targeting Gram-negative bacilli.Le infezioni in medicina · 2025Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
The design of inhibitors against metallo-β-lactamases (MBLs), the largest family of carbapenemases, has been a strategic goal in designing novel antimicrobial therapies. In this regard, the development of bicyclic boronates, such as taniborbactam (TAN) and xeruborbactam, is a major achievement that may help in overcoming the threat of MBL-producing and carbapenem-resistant Gram-negative pathogens. Of concern, a recent report has shown that New Delhi MBL-9 (NDM-9) escapes the inhibitory action of TAN by a single amino acid substitution with respect to New Delhi MBL-1 (NDM-1), the most widely disseminated MBL. Here, we report a docking and computational analysis that identifies that "escape variants" against TAN can arise by disruption of the electrostatic interaction of negative charges in the active site loops of MBLs with the N-(2-aminoethyl)cyclohexylamine side chain of TAN. These changes result in non-productive binding modes of TAN that preclude reaction with the MBLs, a phenomenon that is not restricted to NDM-9. This analysis demonstrates that single amino acid substitutions in non-essential residues in MBL loops can unexpectedly elicit resistance to TAN.
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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.