ArticleACS infectious diseases2017
Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity.
Article in ACS infectious diseases, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 67 citations in OpenAlex.
- The global epidemiology and treatment of metallo-β-lactamase-producing gram-negative pathogens.JAC-antimicrobial resistance · 2026Review
- Characteristics ofOne health (Amsterdam, Netherlands) · 2026Article
- Clinically Significant Carbapenemases in Gram-Negative Pathogens: Molecular Diversity and Advances in β-Lactamase Inhibitor Therapy.Antibiotics (Basel, Switzerland) · 2026Review
- Structural and functional characterization of the New Delhi metallo beta-lactamase-1 (NDM-1) D254A mutant: a biochemical, microbiological and bioinformatics study.World journal of microbiology & biotechnology · 2025Article
- Inhibitor Affinity Differs among Clinical Variants of IMP Metallo-ACS infectious diseases · 2025Article
- Morin combined with meropenem is a potent inhibitor of NDM-1 against NDM-1-producing E. coli.Scientific reports · 2025Article
- Article
- Zinc-dependent β-lactam resistance at a cost.Nature microbiology · 2025Article
- Metalation of Extracytoplasmic Proteins and Bacterial Cell Envelope Homeostasis.Annual review of microbiology · 2024Review
- Probing metalloenzyme dynamics in living systems: Contemporary advances in fluorescence imaging tools and applications.Current opinion in chemical biology · 2024Review
- Evolutionary trajectories of beta-lactamase NDM and DLST cluster inPathogens and global health · 2024Article
- Structural role of K224 in taniborbactam inhibition of NDM-1.Antimicrobial agents and chemotherapy · 2024Article
- Involvement of the non-active site Residues in the Catalytic Activity of NDM-4 Metallo beta-lactamase.The protein journal · 2023Article
- Distinct Inhibition Modes of New Delhi Metallo-β-lactamase-1 Revealed by NMR Spectroscopy.JACS Au · 2023Article
- The Effects of One-Point Mutation on the New Delhi Metallo Beta-Lactamase-1 Resistance toward Carbapenem Antibiotics and β-Lactamase Inhibitors: An In Silico Systematic Approach.International journal of molecular sciences · 2022Article
- Metallo-β-lactamases and a tug-of-war for the available zinc at the host-pathogen interface.Current opinion in chemical biology · 2022Review
- Enzyme Inhibitors: The Best Strategy to Tackle Superbug NDM-1 and Its Variants.International journal of molecular sciences · 2021Review
- Trade-Offs between Antibacterial Resistance and Fitness Cost in the Production of Metallo-β-Lactamases by Enteric Bacteria Manifest as Sporadic Emergence of Carbapenem Resistance in a Clinical Setting.Antimicrobial agents and chemotherapy · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Visualizing the Dynamic Metalation State of New Delhi Metallo-β-lactamase-1 in Bacteria Using a Reversible Fluorescent Probe.Journal of the American Chemical Society · 2021Article
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Authors and funding
16 authors at 5 institutions in 1 country.
Funding
Abstract
Use and misuse of antibiotics have driven the evolution of serine β-lactamases to better recognize new generations of β-lactam drugs, but the selective pressures driving evolution of metallo-β-lactamases are less clear. Here, we present evidence that New Delhi metallo-β-lactamase (NDM) is evolving to overcome the selective pressure of zinc(II) scarcity. Studies of NDM-1, NDM-4 (M154L), and NDM-12 (M154L, G222D) demonstrate that the point mutant M154L, contained in 50% of clinical NDM variants, selectively enhances resistance to the penam ampicillin at low zinc(II) concentrations relevant to infection sites. Each of the clinical variants is shown to be progressively more thermostable and to bind zinc(II) more tightly than NDM-1, but a selective enhancement of penam turnover at low zinc(II) concentrations indicates that most of the improvement derives from catalysis rather than stability. X-ray crystallography of NDM-4 and NDM-12, as well as bioinorganic spectroscopy of dizinc(II), zinc(II)/cobalt(II), and dicobalt(II) metalloforms probe the mechanism of enhanced resistance and reveal perturbations of the dinuclear metal cluster that underlie improved catalysis. These studies support the proposal that zinc(II) scarcity, rather than changes in antibiotic structure, is driving the evolution of new NDM variants in clinical settings.
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