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dc.contributor.authorGeiger, Florian
dc.contributor.authorAcker, Julia
dc.contributor.authorPapa, Guido
dc.contributor.authorWang, Xinyu
dc.contributor.authorArter, William E
dc.contributor.authorSaar, Kadi L
dc.contributor.authorErkamp, Nadia A
dc.contributor.authorQi, Runzhang
dc.contributor.authorBravo, Jack PK
dc.contributor.authorStrauss, Sebastian
dc.contributor.authorKrainer, Georg
dc.contributor.authorBurrone, Oscar R
dc.contributor.authorJungmann, Ralf
dc.contributor.authorKnowles, Tuomas PJ
dc.contributor.authorEngelke, Hanna
dc.contributor.authorBorodavka, Alexander
dc.date.accessioned2021-09-15T17:26:38Z
dc.date.available2021-09-15T17:26:38Z
dc.date.issued2021-09-15
dc.date.submitted2021-01-12
dc.identifier.issn0261-4189
dc.identifier.issn1460-2075
dc.identifier.otherembj2021107711
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/328086
dc.descriptionFunder: Deutsche Forschungsgemeinschaft (DFG); Id: http://dx.doi.org/10.13039/501100001659
dc.description.abstractAbstract: RNA viruses induce the formation of subcellular organelles that provide microenvironments conducive to their replication. Here we show that replication factories of rotaviruses represent protein‐RNA condensates that are formed via liquid–liquid phase separation of the viroplasm‐forming proteins NSP5 and rotavirus RNA chaperone NSP2. Upon mixing, these proteins readily form condensates at physiologically relevant low micromolar concentrations achieved in the cytoplasm of virus‐infected cells. Early infection stage condensates could be reversibly dissolved by 1,6‐hexanediol, as well as propylene glycol that released rotavirus transcripts from these condensates. During the early stages of infection, propylene glycol treatments reduced viral replication and phosphorylation of the condensate‐forming protein NSP5. During late infection, these condensates exhibited altered material properties and became resistant to propylene glycol, coinciding with hyperphosphorylation of NSP5. Some aspects of the assembly of cytoplasmic rotavirus replication factories mirror the formation of other ribonucleoprotein granules. Such viral RNA‐rich condensates that support replication of multi‐segmented genomes represent an attractive target for developing novel therapeutic approaches.
dc.languageen
dc.subjectEMBO23
dc.subjectEMBO40
dc.subjectArticle
dc.subjectArticles
dc.subjectbiomolecular condensates
dc.subjectmicrofluidics
dc.subjectRNP granules
dc.subjectviral genome assembly
dc.titleLiquid–liquid phase separation underpins the formation of replication factories in rotaviruses
dc.typeArticle
dc.date.updated2021-09-15T17:26:38Z
prism.publicationNameThe EMBO Journal
dc.identifier.doi10.17863/CAM.75543
dcterms.dateAccepted2021-08-27
rioxxterms.versionofrecord10.15252/embj.2021107711
rioxxterms.versionAO
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidAcker, Julia [0000-0002-6422-6514]
dc.contributor.orcidPapa, Guido [0000-0002-5215-0014]
dc.contributor.orcidArter, William E [0000-0002-3615-1885]
dc.contributor.orcidJungmann, Ralf [0000-0003-4607-3312]
dc.contributor.orcidEngelke, Hanna [0000-0001-9529-9436]
dc.contributor.orcidBorodavka, Alexander [0000-0002-5729-2687]


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