{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,25]],"date-time":"2026-10-25T05:29:32Z","timestamp":1792906172788,"version":"4.5.0"},"reference-count":83,"publisher":"National Academy of Sciences","issue":"33","license":[{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100018777","name":"IU | College of Arts and Sciences, Indiana University Bloomington","doi-asserted-by":"publisher","award":["startup"],"award-info":[{"award-number":["startup"]}],"id":[{"id":"10.13039\/100018777","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-10-IAHU-03"],"award-info":[{"award-number":["ANR-10-IAHU-03"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["1R35 GM161411"],"award-info":[{"award-number":["1R35 GM161411"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,8,18]]},"abstract":"<jats:p>\n                    Viruses with large DNA genomes often carry auxiliary metabolic genes that reprogram host physiology, yet their contributions to host redox and membrane homeostasis remain poorly understood. Here, we report the finding and functional reconstitution of viral homologs of vitamin K epoxide reductase (VKOR) encoded by giant viruses. Using phylogenetic and genomic context analysis, we find that viral VKOR genes are frequently located adjacent to \u03b3-carboxylase-like epoxidase and fatty acid desaturase domains, consistent with a putative modular redox pathway for membrane lipid modification. To investigate their function, we expressed viral VKORs in an\n                    <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                    strain lacking disulfide bond\u2013forming enzymes and examined both their membrane topology and activity. Remarkably, a minimal set of residue substitutions enabled proper membrane insertion and restored bacterial motility, demonstrating that viral VKORs are catalytically competent electron shuttles. Structural modeling supports their integration into the endoplasmic reticulum\u2013like environment in the host. Finally, we show that VKORs and \u03b3-carboxylase-like epoxidase-desaturases from\n                    <jats:italic toggle=\"yes\">Fadolivirus<\/jats:italic>\n                    and\n                    <jats:italic toggle=\"yes\">Yasminevirus<\/jats:italic>\n                    giant viruses are expressed during infection of\n                    <jats:italic toggle=\"yes\">Vermamoeba vermiformis<\/jats:italic>\n                    , where they may couple vitamin K epoxidation to desaturation-driven lipid remodeling. These findings expand the known functional repertoire of giant viruses and highlight a viral strategy for manipulating host redox metabolism and membrane composition.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2610764123","type":"journal-article","created":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T19:09:16Z","timestamp":1786388956000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":1,"title":["Giant viruses encode vitamin K\u2013based redox modules for lipid modification"],"prefix":"10.1073","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-3556-5288","authenticated-orcid":false,"given":"Rebecca","family":"Collins","sequence":"first","affiliation":[{"name":"Department of Biology, Indiana 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