{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T16:37:25Z","timestamp":1780331845028,"version":"3.54.1"},"reference-count":55,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2024,10,20]],"date-time":"2024-10-20T00:00:00Z","timestamp":1729382400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000072","name":"National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["DE029825"],"award-info":[{"award-number":["DE029825"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Oral Microbiology"],"published-print":{"date-parts":[[2025,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Introduction<\/jats:title>\n                    <jats:p>\n                      <jats:italic>Filifactor alocis<\/jats:italic>\n                      is a newly appreciated member of the periodontal community with a strong periodontal disease correlation. Little is known about the survival mechanisms by which\n                      <jats:italic>F.\u00a0alocis<\/jats:italic>\n                      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\n                      <jats:italic>F.\u00a0alocis<\/jats:italic>\n                      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.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      FA768, FA608, FA1411 and FA455 proteins from\n                      <jats:italic>F.\u00a0alocis<\/jats:italic>\n                      were expressed and purified from\n                      <jats:italic>Escherichia coli<\/jats:italic>\n                      . Insulin and 5,5\u2010dithio\u2010bis\u20102\u2010nitrobenzoic 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\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      ) with FA608 and FA1411\/FA455 provided as the reducing systems. Further, the hydroperoxide substrate specificity of FA768 was analyzed by monitoring the NADPH oxidation in the presence of different peroxides, including H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      , cumyl hydroperoxide (CHP), and tert\u2010butyl hydroperoxide (t\u2010BHP).\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      In this study, we have demonstrated the existence of a functioning thioredoxin\u2010dependent alkyl hydroperoxide system in\n                      <jats:italic>F.\u00a0alocis<\/jats:italic>\n                      . This system is comprised of a thioredoxin reductase (FA608), a thioredoxin\/glutaredoxin homolog (FA1411\/FA455), and a typical 2\u2010cysteine 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\u2010like protein with thioredoxin functions in\n                      <jats:italic>F.\u00a0alocis<\/jats:italic>\n                      . Both the FA768\/FA608\/FA1411 and FA768\/FA608\/FA455 reductase systems were NADPH\u2010dependent and exhibited specificity for broad hydroperoxide substrates H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      , CHP, and t\u2010BHP.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>\n                      This is the first study of a thioredoxin dependent alkyl hydroperoxide system from a periodontal pathogen. This system is proposed to protect\n                      <jats:italic>F.\u00a0alocis<\/jats:italic>\n                      against oxidative stress due to the likely absence of a catalase or an additional peroxiredoxin homolog.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/omi.12486","type":"journal-article","created":{"date-parts":[[2024,10,21]],"date-time":"2024-10-21T02:33:42Z","timestamp":1729478022000},"page":"50-63","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Characterization of thioredoxin\u2013thioredoxin reductase system in\n                    <i>Filifactor alocis<\/i>"],"prefix":"10.1111","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-1768-9954","authenticated-orcid":false,"given":"Arunima","family":"Mishra","sequence":"first","affiliation":[{"name":"Division of Microbiology &amp; Molecular Genetics, School of Medicine Loma Linda University  Loma 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