ArticlePathogens (Basel, Switzerland)2025
Diversity in the Common Fold: Structural Insights into Class D β-Lactamases from Gram-Negative Pathogens.
Article in Pathogens (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- β-lactamase genes in clinical isolates of Capnocytophaga canimorsus and description of a novel class D β-lactamase, OXA-1422.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Article
- The Novel Carbapenem, JDB/PQ-1-219, Has Potent Broad Spectrum Activity against Multi-Drug ResistantACS infectious diseases · 2026Article
- Genetic and biochemical characterization of OXA-1054, a carbapenem-hydrolyzing class D β-lactamase conferring broad-spectrum β-lactam resistance inAntimicrobial agents and chemotherapy · 2026Article
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Authors and funding
2 authors.
Funding
Abstract
Class D β-lactamases (DBLs) represent a major threat to antibiotic efficacy by hydrolyzing β-lactam drugs, including last-resort carbapenems, thereby driving antimicrobial resistance in Gram-negative bacteria. The enzymes share a structurally conserved two-domain α/β architecture with seven active-site motifs and three flexible extended loops (the P-loop, Ω-loop, and newly designated B-loop) that surround the active site. While each of these loops is known to influence enzyme function, their coordinated roles have not been fully elucidated. To investigate the significance of their interplay, we compared the sequences and crystal structures of 40 DBLs from clinically relevant Gram-negative pathogens and performed molecular dynamics simulations on selected representatives. Combined structural and dynamical analyses revealed a strong correlation between B-loop architecture and carbapenemase activity in the pathogens
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