Production of recombinant OXA-23 carbapenemase: a target for developing antibody-based diagnostics against carbapenem-resistant Acinetobacter baumannii
Journal of Applied Biology and Biotechnology, ISSN: 2347-212X, Vol: 13, Issue: 1, Page: 291-298
2025
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Article Description
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.
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