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The metallo-β-lactamases strike back: emergence of taniborbactam escape variants
Pranita D Tamma1, Jose M Munita2
1Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Abstract:
Metallo-β-lactamases (MBLs) have evolved relatively rapidly to become an international public health threat. There are no clinically available β-lactamase inhibitors with activity against MBLs. This may change with the introduction of cefepime-taniborbactam. Herein, we review three manuscripts (S. I. Drusin, C. Le Terrier, L. Poirel, R. A. Bonomo, et al., Antimicrob Agents Chemother 68:e01168-23, 2024, https://doi.org/10.1128/aac.01168-23; C. Le Terrier, C. Viguier, P. Nordmann, A. J. Vila, and L. Poirel, Antimicrob Agents Chemother 68:e00991-23, 2024, https://doi.org/10.1128/aac.00991-23; D. Ono, M. F. Mojica, C. R. Bethel, Y. Ishii, et al., Antimicrob Agents Chemother 68:e01332-23, 2024, https://doi.org/10.1128/aac.01332-23) in which investigators describe elegant experiments to explore MBL/taniborbactam interactions and modifications to MBLs, in response, to reduce the affinity of taniborbactam. Challenges with MBL inhibition will not disappear; rather, they will evolve commensurate with advancements in medicinal chemistry.
Insights
Metallo-β-lactamases (MBLs) are a growing threat, but cefepime-taniborbactam shows promise. Research explores MBL-inhibitor interactions and MBL evolution against new drugs.
Area of Science:
- Microbiology
- Medicinal Chemistry
- Public Health
Background:
- Metallo-β-lactamases (MBLs) represent a significant and evolving international public health concern due to their resistance to existing antibiotics.
- Currently, there are no clinically approved β-lactamase inhibitors effective against MBLs, highlighting a critical unmet medical need.
Approach:
- This review examines three recent studies investigating the interactions between MBLs and taniborbactam, a novel inhibitor.
- The studies employed elegant experimental designs to understand MBL-taniborbactam binding and the adaptive modifications MBLs undergo to evade inhibition.
Key Points:
- Taniborbactam demonstrates potential as a therapeutic agent against MBL-producing bacteria.
- MBLs exhibit adaptive evolution, modifying their structure to reduce the binding affinity of taniborbactam.
- Understanding these molecular interactions is crucial for developing next-generation MBL inhibitors.
Conclusions:
- Cefepime-taniborbactam offers a potential new treatment option for infections caused by MBL-producing bacteria.
- The challenge of MBL inhibition is dynamic, requiring ongoing research and development in medicinal chemistry to stay ahead of bacterial resistance.
- Continued investigation into MBL evolution and inhibitor interactions is essential for combating antimicrobial resistance.
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