School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia.
Department of Chemistry, Maynooth University, Maynooth, Co. Kildare, Ireland.
J Inorg Biochem. 2022 Jan;226:111637. doi: 10.1016/j.jinorgbio.2021.111637. Epub 2021 Oct 24.
Resistance to β-lactam antibiotics, including the "last-resort" carbapenems, has emerged as a major threat to global health. A major resistance mechanism employed by pathogens involves the use of metallo-β-lactamases (MBLs), zinc-dependent enzymes that inactivate most of the β-lactam antibiotics used to treat infections. Variants of MBLs are frequently discovered in clinical environments. However, an increasing number of such enzymes have been identified in microorganisms that are less impacted by human activities. Here, an MBL from Lysobacter antibioticus, isolated from the rhizosphere, has been shown to be highly active toward numerous β-lactam antibiotics. Its activity is higher than that of some of the most effective MBLs linked to hospital-acquired antibiotic resistance and thus poses an interesting system to investigate evolutionary pressures that drive the emergence of such biocatalysts.
β-内酰胺类抗生素（包括“最后手段”的碳青霉烯类抗生素）耐药性的出现，已成为全球健康的主要威胁。病原体采用的主要耐药机制涉及使用金属β-内酰胺酶（MBLs），这是一种锌依赖性酶，能使大多数用于治疗感染的β-内酰胺类抗生素失活。MBLs 的变体经常在临床环境中被发现。然而，越来越多的此类酶已在受人类活动影响较小的微生物中被鉴定出来。在这里，从根际分离到的抗生菌 Lysobacter 中的一种 MBL 被证明对许多β-内酰胺类抗生素具有很高的活性。其活性高于一些与医院获得性抗生素耐药性相关的最有效的 MBLs，因此，它构成了一个有趣的系统，可以研究推动此类生物催化剂出现的进化压力。
