Dual Role of a Viral Polymerase in Viral Genome Replication and Particle Self-Assembly

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dc.contributor.author Sun, Xiaoyu
dc.contributor.author Ilca, Serban L.
dc.contributor.author Huiskonen, Juha T.
dc.contributor.author Poranen, Minna M.
dc.date.accessioned 2018-12-18T13:22:01Z
dc.date.available 2018-12-18T13:22:01Z
dc.date.issued 2018
dc.identifier.citation Sun , X , Ilca , S L , Huiskonen , J T & Poranen , M M 2018 , ' Dual Role of a Viral Polymerase in Viral Genome Replication and Particle Self-Assembly ' , mBio , vol. 9 , no. 5 , ARTN e01242-18 . https://doi.org/10.1128/mBio.01242-18
dc.identifier.other PURE: 120281874
dc.identifier.other PURE UUID: c2ed6107-3477-4f63-907e-454cbf571a99
dc.identifier.other WOS: 000449472200049
dc.identifier.other ORCID: /0000-0002-9468-8787/work/51799082
dc.identifier.other ORCID: /0000-0002-4775-3670/work/51805283
dc.identifier.other Scopus: 85054354835
dc.identifier.uri http://hdl.handle.net/10138/277636
dc.description.abstract Double-stranded RNA (dsRNA) viruses package several RNA-dependent RNA polymerases (RdRp) together with their dsRNA genome into an icosahedral protein capsid known as the polymerase complex. This structure is highly conserved among dsRNA viruses but is not found in any other virus group. RdRp subunits typically interact directly with the main capsid proteins, close to the 5-fold symmetric axes, and perform viral genome replication and transcription within the icosahedral protein shell. In this study, we utilized Pseudomonas phage Phi 6, a well-established virus self-assembly model, to probe the potential roles of the RdRp in dsRNA virus assembly. We demonstrated that Phi 6 RdRp accelerates the polymerase complex self-assembly process and contributes to its conformational stability and integrity. We highlight the role of specific amino acid residues on the surface of the RdRp in its incorporation during the self-assembly reaction. Substitutions of these residues reduce RdRp incorporation into the polymerase complex during the self-assembly reaction. Furthermore, we determined that the overall transcription efficiency of the Phi 6 polymerase complex increased when the number of RdRp subunits exceeded the number of genome segments. These results suggest a mechanism for RdRp recruitment in the polymerase complex and highlight its novel role in virion assembly, in addition to the canonical RNA transcription and replication functions. IMPORTANCE Double-stranded RNA viruses infect a wide spectrum of hosts, including animals, plants, fungi, and bacteria. Yet genome replication mechanisms of these viruses are conserved. During the infection cycle, a proteinaceous capsid, the polymerase complex, is formed. An essential component of this capsid is the viral RNA polymerase that replicates and transcribes the enclosed viral genome. The polymerase complex structure is well characterized for many double-stranded RNA viruses. However, much less is known about the hierarchical molecular interactions that take place in building up such complexes. Using the bacteriophage Phi 6 self-assembly system, we obtained novel insights into the processes that mediate polymerase subunit incorporation into the polymerase complex for generation of functional structures. The results presented pave the way for the exploitation and engineering of viral self-assembly processes for biomedical and synthetic biology applications. An understanding of viral assembly processes at the molecular level may also facilitate the development of antivirals that target viral capsid assembly. en
dc.format.extent 14
dc.language.iso eng
dc.relation.ispartof mBio
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject Pseudomonas phage phi6
dc.subject RNA-dependent RNA polymerase
dc.subject bacteriophage assembly
dc.subject cystovirus
dc.subject double-stranded RNA virus
dc.subject virus assembly
dc.subject RNA BACTERIOPHAGE PHI-6
dc.subject SINGLE-STRANDED RNA
dc.subject PSEUDOMONAS PHAGE PHI-6
dc.subject PROTEIN P7
dc.subject DSRNA BACTERIOPHAGE-PHI-6
dc.subject MINUS-STRAND
dc.subject CRYO-EM
dc.subject CRYOELECTRON MICROSCOPY
dc.subject ELECTRON-MICROSCOPY
dc.subject PURIFIED PROTEIN
dc.subject 1183 Plant biology, microbiology, virology
dc.title Dual Role of a Viral Polymerase in Viral Genome Replication and Particle Self-Assembly en
dc.type Article
dc.contributor.organization Molecular and Translational Virology
dc.contributor.organization Molecular and Integrative Biosciences Research Programme
dc.contributor.organization Helsinki Institute of Life Science HiLIFE
dc.contributor.organization General Microbiology
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1128/mBio.01242-18
dc.relation.issn 2150-7511
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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