Initiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virus

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dc.citation.articleNumbere1005523en_US
dc.citation.issueNumber4en_US
dc.citation.journalTitlePLoS Pathogensen_US
dc.citation.volumeNumber12en_US
dc.contributor.authorCollier, Aaron M.en_US
dc.contributor.authorLyytinen, Outi L.en_US
dc.contributor.authorGuo, Yusong R.en_US
dc.contributor.authorToh, Yukimatsuen_US
dc.contributor.authorPoranen, Minna M.en_US
dc.contributor.authorTao, Yizhi Janeen_US
dc.date.accessioned2016-11-10T22:23:40Zen_US
dc.date.available2016-11-10T22:23:40Zen_US
dc.date.issued2016en_US
dc.description.abstractDuring the replication cycle of double-stranded (ds) RNA viruses, the viral RNA-dependent RNA polymerase (RdRP) replicates and transcribes the viral genome from within the viral capsid. How the RdRP molecules are packaged within the virion and how they function within the confines of an intact capsid are intriguing questions with answers that most likely vary across the different dsRNA virus families. In this study, we have determined a 2.4 Å resolution structure of an RdRP from the human picobirnavirus (hPBV). In addition to the conserved polymerase fold, the hPBV RdRP possesses a highly flexible 24 amino acid loop structure located near the C-terminus of the protein that is inserted into its active site. In vitro RNA polymerization assays and site-directed mutagenesis showed that: (1) the hPBV RdRP is fully active using both ssRNA and dsRNA templates; (2) the insertion loop likely functions as an assembly platform for the priming nucleotide to allow de novo initiation; (3) RNA transcription by the hPBV RdRP proceeds in a semi-conservative manner; and (4) the preference of virus-specific RNA during transcription is dictated by the lower melting temperature associated with the terminal sequences. Co-expression of the hPBV RdRP and the capsid protein (CP) indicated that, under the conditions used, the RdRP could not be incorporated into the recombinant capsids in the absence of the viral genome. Additionally, the hPBV RdRP exhibited higher affinity towards the conserved 5'-terminal sequence of the viral RNA, suggesting that the RdRP molecules may be encapsidated through their specific binding to the viral RNAs during assembly.en_US
dc.identifier.citationCollier, Aaron M., Lyytinen, Outi L., Guo, Yusong R., et al.. "Initiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virus." <i>PLoS Pathogens,</i> 12, no. 4 (2016) Public Library of Science: http://dx.doi.org/10.1371/journal.ppat.1005523.en_US
dc.identifier.doihttp://dx.doi.org/10.1371/journal.ppat.1005523en_US
dc.identifier.urihttps://hdl.handle.net/1911/92700en_US
dc.language.isoengen_US
dc.publisherPublic Library of Scienceen_US
dc.rightsThis is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0en_US
dc.titleInitiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virusen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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