金属-β-内酰胺酶(MBL)已经相对迅速地发展成为国际公共卫生威胁。没有临床上可用的具有针对MBL的活性的β-内酰胺酶抑制剂。这可能随着头孢吡肟-坦尼博巴坦的引入而改变。在这里,我们回顾了三份手稿(S.I.Drusin,C.LeTerrier,L.Poirel,R.A.Bonomo,etal.,AntimicrobAgentsChemother68:e01168-23,2024,https://doi.org/10.1128/aac.01168-23;C.LeTerrier,C.Viguier,P.Nordmann,A.J.Vila,和L.Poirel,AntimicrobAgentsChemother68:e00991-23,2024,https://doi.org/10.1128/aac.00991-23;D.Ono,M.F.Mojica,C.R.Bethel,Y.Ishii,etal.,AntimicrobAgentsChemother68:e01332-23,2024,https://doi.org/10.1128/aac.01332-23),其中研究人员描述了探索MBL/taniborbaptam相互作用和对MBL的修改的优雅实验,作为回应,降低坦尼巴坦的亲和力。MBL抑制的挑战不会消失;相反,它们将随着药物化学的进步而发展。
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.