AI Article Synopsis
- Escherichia coli RclA and Staphylococcus aureus MerA are proteins in the Group I flavoprotein disulfide reductase family that help bacteria survive the host immune system.
- The study focused on Fusobacterium nucleatum's FN0820 protein, which showed greater Cu-dependent NADH oxidase activity than E. coli RclA and lowered oxygen levels in solution.
- L-tryptophan and 5-hydroxytryptophan were found to inhibit FN0820's NADH oxidase activity, suggesting potential new treatments targeting bacterial defenses involving Group I FDRs.
Article 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 Cu-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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s12275-023-00095-9 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!