Characterization of thioredoxin-thioredoxin reductase system in Filifactor alocis.
Filifactor alocis
H2O2‐induced oxidative stress
peroxiredoxin
thioredoxin
thioredoxin reductase
Journal
Molecular oral microbiology
ISSN: 2041-1014
Titre abrégé: Mol Oral Microbiol
Pays: Denmark
ID NLM: 101524770
Informations de publication
Date de publication:
20 Oct 2024
20 Oct 2024
Historique:
revised:
24
09
2024
received:
14
05
2024
accepted:
25
09
2024
medline:
21
10
2024
pubmed:
21
10
2024
entrez:
21
10
2024
Statut:
aheadofprint
Résumé
Filifactor alocis is a newly appreciated member of the periodontal community with a strong periodontal disease correlation. Little is known about the survival mechanisms by which F. alocis copes with oxidative stress and establishes the infection within the local inflammatory microenvironment of the periodontal pocket. The aim of this study is to investigate if F. alocis putative peroxiredoxin/AhpC protein FA768 may constitute an alkyl hydroperoxide reductase system utilizing putative thioredoxin reductase protein FA608, and putative thioredoxin/glutaredoxin homolog FA1411/FA455. FA768, FA608, FA1411 and FA455 proteins from F. alocis were expressed and purified from Escherichia coli. Insulin and 5,5-dithio-bis-2-nitrobenzoic acid (DTNB) reduction assays were performed to determine if purified FA1411 and FA455 proteins could be a substrate for FA608. The peroxidase activity of FA768 was examined by measuring its ability to reduce hydrogen peroxide (H In this study, we have demonstrated the existence of a functioning thioredoxin-dependent alkyl hydroperoxide system in F. alocis. This system is comprised of a thioredoxin reductase (FA608), a thioredoxin/glutaredoxin homolog (FA1411/FA455), and a typical 2-cysteine peroxiredoxin/AhpC (FA768). FA608, together with FA1411/FA455, can function as a thioredoxin reductase system to reduce insulin, DTNB, and FA768. FA455 is a glutaredoxin-like protein with thioredoxin functions in F. alocis. Both the FA768/FA608/FA1411 and FA768/FA608/FA455 reductase systems were NADPH-dependent and exhibited specificity for broad hydroperoxide substrates H This is the first study of a thioredoxin dependent alkyl hydroperoxide system from a periodontal pathogen. This system is proposed to protect F. alocis against oxidative stress due to the likely absence of a catalase or an additional peroxiredoxin homolog.
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Public Health Services
ID : DE030411
Organisme : Public Health Services
ID : DE025852
Organisme : NIDCR NIH HHS
ID : DE029825
Pays : United States
Informations de copyright
© 2024 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.
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