{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T17:51:31Z","timestamp":1785779491475,"version":"3.56.0"},"reference-count":47,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T00:00:00Z","timestamp":1782777600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T00:00:00Z","timestamp":1782777600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2026,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Borrelia burgdorferi<\/jats:italic>\n                    <\/jats:styled-content>\n                    (\n                    <jats:italic>Bb<\/jats:italic>\n                    ), the etiological agent of Lyme disease, lacks the genes for de novo riboflavin biosynthesis and depends on host\u2010derived riboflavin to generate flavin cofactors FMN and FAD. Riboflavin salvage by\n                    <jats:italic>Bb<\/jats:italic>\n                    has demonstrated importance to infection and metabolic homeostasis, though the critical roles of flavin cofactors to central metabolism are not well defined. Here, we demonstrate that riboflavin availability directly controls glycolytic flux through regulation of intracellular redox balance. Disruption of riboflavin uptake by deletion of gene\n                    <jats:italic>bb0318<\/jats:italic>\n                    encoding the putative ATPase component of the riboflavin transporter resulted in impaired glycolysis as indicated by reduced intracellular pyruvate and a perturbed NADH\/NAD\n                    <jats:sup>+<\/jats:sup>\n                    ratio driven by faulty NAD\n                    <jats:sup>+<\/jats:sup>\n                    regeneration. We identified coenzyme A disulfide reductase (CoADR) as a key flavin\u2010dependent mediator of glycolytic flux. A \u0394\n                    <jats:italic>cdr<\/jats:italic>\n                    mutant mimicked the glycolytic dysregulation of the \u0394\n                    <jats:italic>bb0318<\/jats:italic>\n                    mutant, but was not rescued by exogenous riboflavin, placing\n                    <jats:italic>Bb<\/jats:italic>\n                    CoADR downstream of riboflavin salvage. Biochemical analyses of recombinant\n                    <jats:italic>Bb<\/jats:italic>\n                    CoADR demonstrated FAD\u2010dependent NADH oxidase activity. Targeted mutagenesis of predicted FAD\u2010binding residues impaired cofactor binding and NADH oxidase activity, further confirming the dependence of\n                    <jats:italic>Bb<\/jats:italic>\n                    CoADR on FAD. Together, this work reveals a direct link between riboflavin acquisition and core metabolic processes driven by\n                    <jats:italic>Bb<\/jats:italic>\n                    CoADR\u2010mediated flavin\u2010dependent redox metabolism.\n                  <\/jats:p>","DOI":"10.1111\/mmi.70090","type":"journal-article","created":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T08:03:55Z","timestamp":1782893035000},"page":"208-219","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Riboflavin Salvage Supports Glycolysis in\n                    <i>Borrelia burgdorferi<\/i>\n                    Through Flavin\u2010Dependent\n                    <scp>NAD<\/scp>\n                    <sup>+<\/sup>\n                    Regeneration"],"prefix":"10.1111","volume":"126","author":[{"given":"Anna M.","family":"Schulz","sequence":"first","affiliation":[{"name":"Division of Immunity and Pathogenesis, Burnett School of Biomedical Sciences, College of Medicine University of Central Florida  Orlando Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grace E.","family":"Easterling","sequence":"additional","affiliation":[{"name":"Division of Immunity and Pathogenesis, Burnett School of Biomedical Sciences, College of Medicine University of Central Florida  Orlando Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaditya","family":"Balasubramaniyan","sequence":"additional","affiliation":[{"name":"Division of Immunity and Pathogenesis, Burnett School of Biomedical Sciences, College of Medicine University of Central Florida  Orlando Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3130-3795","authenticated-orcid":false,"given":"Mollie W.","family":"Jewett","sequence":"additional","affiliation":[{"name":"Division of Immunity and Pathogenesis, Burnett School of Biomedical Sciences, College of Medicine University of Central Florida  Orlando Florida USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,6,30]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1080\/10942912.2015.1076459"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0079-6603(04)78003-4"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.3389\/fbioe.2020.570828"},{"key":"e_1_2_11_5_1","first-page":"521","article-title":"Isolation and Cultivation of Lyme Disease Spirochetes","volume":"57","author":"Barbour A. 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