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We describe here a novel flavivirus inhibition mechanism that results in interferon-mediated obstruction of tick-borne encephalitis virus particle assembly and involves release of malfunctioning membrane-associated capsid (C) particles. This mechanism is controlled by the activity of the interferon-induced protein viperin, a broad-spectrum antiviral interferon-stimulated gene. Through analysis of the viperin-interactome, we identified the Golgi brefeldin A-resistant guanine nucleotide exchange factor 1 (GBF1) as the cellular protein targeted by viperin. Viperin-induced antiviral activity, as well as C-particle release, was stimulated by GBF1 inhibition and knockdown and reduced by elevated levels of GBF1. Our results suggest that viperin targets flavivirus virulence by inducing the secretion of unproductive noninfectious virus particles via a GBF1-dependent mechanism. This as-yet-undescribed antiviral mechanism allows potential therapeutic intervention.<\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            The interferon response can target viral infection on almost every level; however, very little is known about the interference of flavivirus assembly. We show here that interferon, through the action of viperin, can disturb the assembly of tick-borne encephalitis virus. The viperin protein is highly induced after viral infection and exhibit broad-spectrum antiviral activity. However, the mechanism of action is still elusive and appears to vary between the different viruses, indicating that cellular targets utilized by several viruses might be involved. In this study, we show that viperin induces capsid particle release by interacting and inhibiting the function of the cellular protein Golgi brefeldin A-resistant guanine nucleotide exchange factor 1 (GBF1). GBF1 is a key protein in the cellular secretory pathway and is essential in the life cycle of many viruses, also targeted by viperin, implicating GBF1 as a novel putative drug target.\n          <\/jats:p>","DOI":"10.1128\/jvi.01751-17","type":"journal-article","created":{"date-parts":[[2017,10,19]],"date-time":"2017-10-19T00:25:30Z","timestamp":1508372730000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":53,"title":["Viperin Targets Flavivirus Virulence by Inducing Assembly of Noninfectious Capsid Particles"],"prefix":"10.1128","volume":"92","author":[{"given":"Kirstin","family":"Vonderstein","sequence":"first","affiliation":[{"name":"Department of Clinical Microbiology, Virology, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emma","family":"Nilsson","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Virology, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philipp","family":"Hubel","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biochemistry, Martinsried, Munich, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lars\u00e5rd","family":"Nyg\u00e5rd Skalman","sequence":"additional","affiliation":[{"name":"Department of Medical Biochemistry and Biophysics, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Integrative Medical Biology, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arunkumar","family":"Upadhyay","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Virology, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jenny","family":"Pasto","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Virology, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas","family":"Pichlmair","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Biochemistry, Martinsried, Munich, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Lundmark","sequence":"additional","affiliation":[{"name":"Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Department of Medical Biochemistry and Biophysics, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Integrative Medical Biology, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6553-0940","authenticated-orcid":false,"given":"Anna K.","family":"\u00d6verby","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Virology, Ume\u00e5 University, Ume\u00e5, Sweden"},{"name":"Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 University, Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1089\/vim.2004.17.498"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-immunol-032713-120231"},{"key":"e_1_3_3_4_2","first-page":"21","volume-title":"Molecular virology and control of flaviviruses","author":"Roby JA","year":"2012","unstructured":"Roby JA, Funk A, Khromykh AA. 2012. 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