Involvement of a Nonstructural Protein in Poliovirus Capsid Assembly

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dc.contributor.authorAdeyemi, Oluwapelumi O.
dc.contributor.authorSherry, Lee
dc.contributor.authorWard, Joseph C
dc.contributor.authorPierce, Danielle M
dc.contributor.authorHerod, Morgan R
dc.contributor.authorRowlands, David J
dc.contributor.authorStonehouse, Nicola J
dc.date.accessioned2021-08-24T10:20:32Z
dc.date.available2021-08-24T10:20:32Z
dc.date.issued2019
dc.description.abstractVirus capsid proteins must perform a number of roles. These include self-assembly and maintaining stability under challenging environmental conditions, while retaining the conformational flexibility necessary to uncoat and deliver the viral genome into a host cell. Fulfilling these roles could place conflicting constraints on the innate abilities encoded within the protein sequences. In a previous study, we identified a number of mutations within the capsid-coding sequence of poliovirus (PV) that were established in the population during selection for greater thermostability by sequential treatment at progressively higher temperatures. Two mutations in the VP1 protein acquired at an early stage were maintained throughout this selection procedure. One of these mutations prevented virion assembly when introduced into a wild-type (wt) infectious clone. Here we show, by sequencing beyond the capsid-coding region of the heat-selected virions, that two mutations had arisen within the coding region of the 2A protease. Both mutations were maintained throughout the selection process. Introduction of these mutations into a wt infectious clone by site-directed mutagenesis considerably reduced replication. However, they permitted a low level of assembly of infectious virions containing the otherwise lethal mutation in VP1. The 2Apro mutations were further shown to slow the kinetics of viral polyprotein processing, and we suggest that this delay improves the correct folding of the mutant capsid precursor protein to permit virion assembly.en_US
dc.description.sponsorshipO.O.A. was funded for part of this study by the Tertiary Education Trust Fund (TETfund), Nigeria.en_US
dc.identifier.citationAdeyemi O.O., Sherry L., Ward J.C., Pierce D.M., Herod M.R., Rowlands D.J., Stonehouse N.J. (2019). Involvement of a nonstructural protein in poliovirus capsid assembly. Journal of Virology. 93(5); e01447-18en_US
dc.identifier.urihttps://uilspace.unilorin.edu.ng/handle/20.500.12484/6250
dc.language.isoenen_US
dc.publisherAmerican Society for Microbiology, USAen_US
dc.titleInvolvement of a Nonstructural Protein in Poliovirus Capsid Assemblyen_US
dc.typeArticleen_US

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