ArticleAntimicrobial agents and chemotherapy2025
Active site loops of membrane-anchored metallo-β-lactamases from environmental bacteria determine cephalosporinase activity.
Article in Antimicrobial agents and chemotherapy, 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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3 citing papers in PubMed.
- Phylogenetic Relationships and Structural Conservation ofInternational journal of molecular sciences · 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
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Abstract
Antimicrobial resistance is a significant global public health threat that limits treatment options for bacterial infections. This situation is aggravated by the environmental spread of β-lactamase genes. In particular, metallo-β-lactamases (MBLs) hydrolyze almost all available β-lactam antibiotics, including late-generation cephalosporins and carbapenems. Among MBLs, the New Delhi metallo-β-lactamase (NDM-1) of subclass B1 has shown the most ominous dissemination. NDM variants are the only MBLs of clinical importance that are membrane-anchored, a sub-cellular localization that endows them with high stability under conditions of metal limitation. However, antibiotic resistance predates modern antibiotic usage, and environmental bacteria serve as reservoirs for resistance genes. Here, we report the biochemical and structural characterization of two membrane-bound MBLs: CJO-1 and CIM-2, from
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