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We previously showed that their W protein, a key player in the evasion of the host antiviral response, forms highly flexible, curved fibrils in vitro. Here, we show that the cysteine oxidation state acts as a molecular switch controlling the formation of either amorphous aggregates or flexible fibrils, and that residues 2 to 29 are essential for fibrillation. We also uncover that the HeV W protein (W\n                    <jats:sup>HeV<\/jats:sup>\n                    ) can also self\u2010assemble in cellula. W\n                    <jats:sup>HeV<\/jats:sup>\n                    forms distinct types of nuclear condensates that exhibit different dependencies on the cysteine redox state. While deletion of residues 2\u201329 prevents formation of nuclear filaments, cysteine\u2010to\u2010serine substitution mainly impairs the formation of non\u2010filamentous condensates. Both infection and W\n                    <jats:sup>HeV<\/jats:sup>\n                    ectopic expression trigger oxidative stress, presumably favorable to W\n                    <jats:sup>HeV<\/jats:sup>\n                    condensation. Finally, we show that impaired ability to form redox\u2010sensitive, non\u2010filamentous condensates is associated with a reduced W ability to inhibit the NF\u2010\u03baB pathway, while it conversely enhances W ability to repress the interferon response pathway by enhancing W binding to STAT1.\n                  <\/jats:p>","DOI":"10.1002\/advs.202523465","type":"journal-article","created":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T22:12:19Z","timestamp":1784326339000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Cysteine Redox State Governs the Condensation Pathway of Hendra Virus W Protein and Differentially Impacts Type I IFN and NF\u2010\u03baB Signaling"],"prefix":"10.1002","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0061-2405","authenticated-orcid":false,"given":"Frank","family":"Gondelaud","sequence":"first","affiliation":[{"name":"Laboratoire Architecture Et Fonction des 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