Abstract
Carbapenems are typically the treatment of choice for drug-resistant Acinetobacter baumannii; however, the emergence of carbapenem-resistant strains has elevated this pathogen to the World Health Organization’s critical priority pathogen list. Since carbapenem resistance is frequently mediated by carbapenemases, particularly oxacillinases and metallo-beta-lactamases, antibody-based carbapenemase detection tests can be developed for rapid and affordable diagnosis of the infection. However, the development of such tests requires the availability of high-quality target proteins for generating specific antibodies, their characterization, and assay optimization. In this study, we reported a streamlined workflow to obtain a purified preparation of the tagless and functionally active recombinant OXA-23 enzyme, which is one of the major factors responsible for carbapenem resistance in Acinetobacter baumannii. The recombinant protein was expressed in the heterologous expression host Escherichia coli using auto-induction and purified using a single step of chromatography, followed by the removal of the affinity tag using TEV protease. The simple protocol reported here is expected to facilitate the production of other carbapenemases and similar proteins for the development of diagnostics and therapeutics to support the fight against antimicrobial-resistant bacteria.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
