| Title | Structural and Functional Analyses of the Flavoprotein Disulfide Reductase FN0820 of Fusobacterium nucleatum |
|---|---|
| Author | Hyunwoo Shin1, Yeongjin Baek1, Dukwon Lee1, Yongbin Xu2, Yonghoon Kwon1, Inseong Jo3*, and Nam‑Chul Ha1,4* |
| Address | 1Department of Agricultural Biotechnology and Research Institute of Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Republic of Korea, 2Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, People’s Republic of China, 3Infectious Diseases Therapeutic Research Center, Korea Research Institute of Chemical Technology (KRICT), Daejeon 34114, Republic of Korea, 4Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Republic of Korea |
| Bibliography | Journal of Microbiology, 61(12),1033-1041, 2023, |
| DOI | 10.1007/s12275-023-00095-9 |
| Key Words | Fusobacterium · RclA · Flavoprotein disulfide reductase · Oxygen reduction · 5-hydroxytryptophan · L-tryptophan |
| 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 developing new treatment strategies against pathogens that defend the host immune response with Group I FDRs. |