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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorCALMELS, Christina
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorVENTURA, Michel
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorAKNIN, Cindy
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorMETIFIOT, Mathieu
dc.contributor.authorANDREOLA, Marie-Line
dc.date.accessioned2023-11-08T09:30:07Z
dc.date.available2023-11-08T09:30:07Z
dc.date.issued2017-06-02
dc.identifier.issn2045-2322en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184677
dc.description.abstractEnMosquito- and tick-borne pathogens including Chikungunya, Dengue, Japanese encephalitis, West Nile, Yellow fever and Zika virus, represent a new economic and public health challenge. In the absence of effective vaccines and specific therapies, only supportive regimens are administrated for most of these infections. Thus, the development of a targeted therapy is mandatory to stop the rapid progression of these pathogens and preoccupant associated burdens such as Guillain-Barre syndrome, microcephaly. For this, it is essential to develop biochemical tools to help study and target key viral enzymes involved in replication such as helicase complexes, methyl-transferases and RNA-dependent RNA polymerases. Here, we show that a highly purified ZIKV polymerase domain is active in vitro. Importantly, we show that this isolated domain is capable of de novo synthesis of the viral genome and efficient elongation without terminal nucleotide transferase activity. Altogether, this isolated polymerase domain will be a precious tool to screen and optimize specific nucleoside and non-nucleoside inhibitors to fight against Zika infections.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enCatalysis
dc.subject.enHumans
dc.subject.enModels
dc.subject.enMolecular
dc.subject.enProtein Binding
dc.subject.enProtein Conformation
dc.subject.enProtein Domains
dc.subject.enProtein Interaction Domains and Motifs
dc.subject.enRNA
dc.subject.enViral
dc.subject.enRNA-Dependent RNA Polymerase
dc.subject.enTranscription
dc.subject.enGenetic
dc.subject.enVirus Replication
dc.subject.enZika Virus
dc.subject.enZika Virus Infection
dc.title.enDe novo RNA synthesis catalyzed by the Zika Virus RNA polymerase domain.
dc.title.alternativeSci Repen_US
dc.typeArticle de revueen_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed28577343en_US
bordeaux.journalScientific Reportsen_US
bordeaux.page2697en_US
bordeaux.volume7en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue1en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04274777
hal.version1
hal.date.transferred2023-11-08T09:30:09Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Scientific%20Reports&rft.date=2017-06-02&rft.volume=7&rft.issue=1&rft.spage=2697&rft.epage=2697&rft.eissn=2045-2322&rft.issn=2045-2322&rft.au=CALMELS,%20Christina&VENTURA,%20Michel&AKNIN,%20Cindy&METIFIOT,%20Mathieu&ANDREOLA,%20Marie-Line&rft.genre=article


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