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Identification and characterization of CIM-1, a carbapenemase that adds to the family of resistance factors against last resort antibiotics
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Identification and characterization of CIM-1, a carbapenemase that adds to the family of resistance factors against last resort antibiotics
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Journal Article
Identification and characterization of CIM-1, a carbapenemase that adds to the family of resistance factors against last resort antibiotics
2024
Overview
The increasing rate of carbapenem-resistant bacteria within healthcare environments is an issue of great concern that needs urgent attention. This resistance is driven by metallo-β-lactamases (MBLs), which can catalyse the hydrolysis of almost all clinically available β-lactams and are resistant to all the clinically utilized β-lactamase inhibitors. In this study, an uncharacterized MBL is identified in a multidrug resistant isolate of the opportunistic pathogen,
Chryseobacterium indologenes
. Sequence analysis predicts this MBL (CIM-1) to be a lipoprotein with an atypical lipobox. Characterization of CIM-1 reveals it to be a high-affinity carbapenemase with a broad spectrum of activity that includes all cephalosporins and carbapenems. Results also shown that CIM-1 is potentially a membrane-associated MBL with an uncharacterized lipobox. Using prediction tools, we also identify more potentially lipidated MBLs with non-canonical lipoboxes highlighting the necessity of further investigation of lipidated MBLs.
An uncharacterized metallo-β-lactamase identified in a multidrug-resistant
Chryseobacterium indologenes
has an atypical lipobox and is potentially lipidated. It has a high-affinity for β-lactams including the last-resort antibiotics, carbapenems.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 38/70
/ 38/77
/ 38/90
/ 42/44
/ 45/22
/ 45/23
/ 82/16
/ 82/29
/ 82/58
/ 82/80
/ 82/83
/ Affinity
/ Anti-Bacterial Agents - pharmacology
/ Bacterial Proteins - genetics
/ Biomedical and Life Sciences
