编码青霉素结合蛋白2的mrdA单突变导致产ndm的大肠杆菌耐药的体外进化

IF 4.5 2区 医学 Q2 MICROBIOLOGY
Christi L McElheny, Erika L Butcher, Akito Kawai, Robert M Q Shanks, Ryan K Shields, Yohei Doi
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引用次数: 0

摘要

Durlobactam是一种重氮比环辛烷β-内酰胺酶抑制剂,通过与青霉素结合蛋白2 (PBP2)结合而表现出直接的抗菌活性。我们将新德里金属β-内酰胺酶产生大肠杆菌突变株暴露于不断增加的杜氯巴坦浓度中,其杜氯巴坦最低抑制浓度为2µg/mL,比基线增加了16倍。耐药归因于mrdA基因的点突变,导致ppbp2中的V522I取代。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
In vitro evolution of durlobactam resistance in NDM-producing Escherichia coli due to a single mutation in mrdA encoding penicillin-binding protein 2.

Durlobactam, a diazabicyclooctane β-lactamase inhibitor, exhibits direct antibacterial activity by binding to penicillin-binding protein 2 (PBP2). We generated a mutant strain of New Delhi metallo-β-lactamase-producing Escherichia coli with a durlobactam minimum inhibitory concentration of 2 µg/mL, representing a 16-fold increase from baseline, by exposing it to increasing concentrations of durlobactam. Resistance was attributed to a point mutation in the mrdA gene, resulting in a V522I substitution in PBP2.

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来源期刊
CiteScore
10.00
自引率
8.20%
发文量
762
审稿时长
3 months
期刊介绍: Antimicrobial Agents and Chemotherapy (AAC) features interdisciplinary studies that build our understanding of the underlying mechanisms and therapeutic applications of antimicrobial and antiparasitic agents and chemotherapy.
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