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Article: In situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus

TitleIn situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus
Authors
Issue Date2017
Citation
Nature, 2017, v. 541, n. 7635, p. 112-116 How to Cite?
AbstractPackaging of the genome into a protein capsid and its subsequent delivery into a host cell are two fundamental processes in the life cycle of a virus. Unlike double-stranded DNA viruses, which pump their genome into a preformed capsid, single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the genome; however, the structural basis of this co-assembly is poorly understood. MS2 infects Escherichia coli via the host sex pilus' (F-pilus); it was the first fully sequenced organism and is a model system for studies of translational gene regulation, RNA-protein interactions, and RNA virus assembly. Its positive-sense ssRNA genome of 3,569 bases is enclosed in a capsid with one maturation protein monomer and 89 coat protein dimers arranged in a T = 3 icosahedral lattice. The maturation protein is responsible for attaching the virus to an F-pilus and delivering the viral genome into the host during infection, but how the genome is organized and delivered is not known. Here we describe the MS2 structure at 3.6 Å resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconstruction. We traced approximately 80% of the backbone of the viral genome, built atomic models for 16 RNA stem-loops, and identified three conserved motifs of RNA-coat protein interactions among 15 of these stem-loops with diverse sequences. The stem-loop at the 3′ end of the genome interacts extensively with the maturation protein, which, with just a six-helix bundle and a six-stranded β-sheet, forms a genome-delivery apparatus and joins 89 coat protein dimers to form a capsid. This atomic description of genome-capsid interactions in a spherical ssRNA virus provides insight into genome delivery via the host sex pilus and mechanisms underlying ssRNA-capsid co-assembly, and inspires speculation about the links between nucleoprotein complexes and the origins of viruses.
Persistent Identifierhttp://hdl.handle.net/10722/285955
ISSN
2023 Impact Factor: 50.5
2023 SCImago Journal Rankings: 18.509
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorDai, Xinghong-
dc.contributor.authorLi, Zhihai-
dc.contributor.authorLai, Mason-
dc.contributor.authorShu, Sara-
dc.contributor.authorDu, Yushen-
dc.contributor.authorZhou, Z. Hong-
dc.contributor.authorSun, Ren-
dc.date.accessioned2020-08-18T04:57:05Z-
dc.date.available2020-08-18T04:57:05Z-
dc.date.issued2017-
dc.identifier.citationNature, 2017, v. 541, n. 7635, p. 112-116-
dc.identifier.issn0028-0836-
dc.identifier.urihttp://hdl.handle.net/10722/285955-
dc.description.abstractPackaging of the genome into a protein capsid and its subsequent delivery into a host cell are two fundamental processes in the life cycle of a virus. Unlike double-stranded DNA viruses, which pump their genome into a preformed capsid, single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the genome; however, the structural basis of this co-assembly is poorly understood. MS2 infects Escherichia coli via the host sex pilus' (F-pilus); it was the first fully sequenced organism and is a model system for studies of translational gene regulation, RNA-protein interactions, and RNA virus assembly. Its positive-sense ssRNA genome of 3,569 bases is enclosed in a capsid with one maturation protein monomer and 89 coat protein dimers arranged in a T = 3 icosahedral lattice. The maturation protein is responsible for attaching the virus to an F-pilus and delivering the viral genome into the host during infection, but how the genome is organized and delivered is not known. Here we describe the MS2 structure at 3.6 Å resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconstruction. We traced approximately 80% of the backbone of the viral genome, built atomic models for 16 RNA stem-loops, and identified three conserved motifs of RNA-coat protein interactions among 15 of these stem-loops with diverse sequences. The stem-loop at the 3′ end of the genome interacts extensively with the maturation protein, which, with just a six-helix bundle and a six-stranded β-sheet, forms a genome-delivery apparatus and joins 89 coat protein dimers to form a capsid. This atomic description of genome-capsid interactions in a spherical ssRNA virus provides insight into genome delivery via the host sex pilus and mechanisms underlying ssRNA-capsid co-assembly, and inspires speculation about the links between nucleoprotein complexes and the origins of viruses.-
dc.languageeng-
dc.relation.ispartofNature-
dc.titleIn situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1038/nature20589-
dc.identifier.pmid27992877-
dc.identifier.pmcidPMC5701785-
dc.identifier.scopuseid_2-s2.0-85016149843-
dc.identifier.volume541-
dc.identifier.issue7635-
dc.identifier.spage112-
dc.identifier.epage116-
dc.identifier.eissn1476-4687-
dc.identifier.isiWOS:000396119500040-
dc.identifier.f1000727122609-
dc.identifier.issnl0028-0836-

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