Kirchhoff, Frank

[["dc.bibliographiccitation.artnumber","2104.e10"],["dc.bibliographiccitation.firstpage","2092"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Braun, Elisabeth"],["dc.contributor.author","Hotter, Dominik"],["dc.contributor.author","Koepke, Lennart"],["dc.contributor.author","Zech, Fabian"],["dc.contributor.author","Groß, Rüdiger"],["dc.contributor.author","Sparrer, Konstantin M.J."],["dc.contributor.author","Müller, Janis A."],["dc.contributor.author","Pfaller, Christian K."],["dc.contributor.author","Heusinger, Elena"],["dc.contributor.author","Wombacher, Rebecka"],["dc.contributor.author","Sutter, Kathrin"],["dc.contributor.author","Dittmer, Ulf"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Simmons, Graham"],["dc.contributor.author","Jakobsen, Martin R."],["dc.contributor.author","Conzelmann, Karl-Klaus"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Münch, Jan"],["dc.contributor.author","Fackler, Oliver T."],["dc.contributor.author","Kirchhoff, Frank"],["dc.contributor.author","Sauter, Daniel"],["dc.date.accessioned","2019-07-09T11:51:46Z"],["dc.date.available","2019-07-09T11:51:46Z"],["dc.date.issued","2019"],["dc.description.abstract","Guanylate-binding protein (GBP) 5 is an interferon (IFN)-inducible cellular factor reducing HIV-1 infectivity by an incompletely understood mechanism. Here, we show that this activity is shared by GBP2, but not by other members of the human GBP family. GBP2/5 decrease the activity of the cellular proprotein convertase furin, which mediates conversion of the HIV-1 envelope protein (Env) precursor gp160 into mature gp120 and gp41. Because this process primes HIV-1 Env for membrane fusion, viral particles produced in the presence of GBP2/5 are poorly infectious due to increased incorporation of non-functional gp160. Furin activity is critical for the processing of envelope glycoproteins of many viral pathogens. Consistently, GBP2/5 also inhibit Zika, measles, and influenza A virus replication and decrease infectivity of viral particles carrying glycoproteins of Marburg and murine leukemia viruses. Collectively, our results show that GPB2/5 exert broad antiviral activity by suppressing the activity of the virus-dependency factor furin."],["dc.identifier.doi","10.1016/j.celrep.2019.04.063"],["dc.identifier.pmid","31091448"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16188"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60006"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","599"],["dc.title","Guanylate-Binding Proteins 2 and 5 Exert Broad Antiviral Activity by Inhibiting Furin-Mediated Processing of Viral Envelope Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]