Abstract
Escherichia coli RclA and Staphylococcus aureus MerA are part of the Group I flavoprotein disulfide reductase (FDR) family and have been implicated in the contribution to bacterial pathogenesis by defending against the host immune response. Fusobacterium nucleatum is a pathogenic, anaerobic Gram-negative bacterial species commonly found in the human oral cavity and gastrointestinal tract. In this study, we discovered that the F. nucleatum protein FN0820, belonging to the Group I FDR family, exhibited a higher activity of a Cu2+-dependent NADH oxidase than E. coli RclA. Moreover, FN0820 decreased the dissolved oxygen level in the solution with higher NADH oxidase activity. We found that L-tryptophan and its analog 5-hydroxytryptophan inhibit the FN0820 activities of NADH oxidase and the concomitant reduction of oxygen. Our results have implications for develo** new treatment strategies against pathogens that defend the host immune response with Group I FDRs.
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Acknowledgements
This research was supported by the Bio & Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science & ICT (MSIT) (grant NRF-2019M3E5D6063871). This research was also supported by the Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry and Fisheries (IPET), funded by the Ministry of Agriculture, Food and Rural Affairs (MAFRA) (321036053HD020).
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YB and NCH designed the research. YB, JR, and JHP conceived and performed the experiments. SJ, IJ and NCH provided expertise and feedback. YB, JR, and NCH wrote the manuscript, and NCH secured funding.
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Shin, H., Baek, Y., Lee, D. et al. Structural and Functional Analyses of the Flavoprotein Disulfide Reductase FN0820 of Fusobacterium nucleatum. J Microbiol. 61, 1033–1041 (2023). https://doi.org/10.1007/s12275-023-00095-9
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DOI: https://doi.org/10.1007/s12275-023-00095-9