Structural and Functional Analyses of the Flavoprotein Disulfide Reductase FN0820 of Fusobacterium nucleatum

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-neg...

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Bibliographic Details
Published in:The journal of microbiology 2023, 61(12), , pp.1033-1041
Main Authors: Shin, Hyunwoo, Baek, Yeongjin, Lee, Dukwon, Xu, Yongbin, Kwon, Yonghoon, Jo, Inseong, Ha, Nam-Chul
Format: Article
Language:English
Subjects:
Bacteria - metabolism
Biomedical and Life Sciences
Copper
Defence mechanisms
Dissolved oxygen
Disulfide reductase
E coli
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Flavoproteins - chemistry
Flavoproteins - metabolism
Fusobacterium nucleatum
Gastrointestinal system
Gastrointestinal tract
Humans
Immune response
Immune system
Immunity
Life Sciences
Microbial Physiology and Biochemistry
Microbiology
Mouth
NADH
NADH oxidase
Nicotinamide adenine dinucleotide
Oral cavity
Oxidase
Pathogenesis
Reductases
Staphylococcus aureus
Structure-function relationships
Tryptophan
생물학
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Summary: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 2+ -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.
ISSN:1225-8873
1976-3794
DOI:10.1007/s12275-023-00095-9