About: Infectious Bursal Disease Virus: Ribonucleoprotein Complexes of a Double-Stranded RNA Virus

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Infectious Bursal Disease Virus: Ribonucleoprotein Complexes of a Double-Stranded RNA Virus
Creator	Luque, Daniel Rodríguez, José Carrascosa, José Castón, José Rejas, María Saugar, Irene
Source	Elsevier; Medline; PMC
abstract	Abstract Genome-binding proteins with scaffolding and/or regulatory functions are common in living organisms and include histones in eukaryotic cells, histone-like proteins in some double-stranded DNA (dsDNA) viruses, and the nucleocapsid proteins of single-stranded RNA viruses. dsRNA viruses nevertheless lack these ribonucleoprotein (RNP) complexes and are characterized by sharing an icosahedral T =2 core involved in the metabolism and insulation of the dsRNA genome. The birnaviruses, with a bipartite dsRNA genome, constitute a well-established exception and have a single-shelled T =13 capsid only. Moreover, as in many negative single-stranded RNA viruses, the genomic dsRNA is bound to a nucleocapsid protein (VP3) and the RNA-dependent RNA polymerase (VPg). We used electron microscopy and functional analysis to characterize these RNP complexes of infectious bursal disease virus, the best characterized member of the Birnaviridae family. Mild disruption of viral particles revealed that VP3, the most abundant core protein, present at ∼450 copies per virion, is found in filamentous material tightly associated with the dsRNA. We developed a method to purify RNP and VPg–dsRNA complexes. Analysis of these complexes showed that they are linear molecules containing a constant amount of protein. Sensitivity assays to nucleases indicated that VP3 renders the genomic dsRNA less accessible for RNase III without introducing genome compaction. Additionally, we found that these RNP complexes are functionally competent for RNA synthesis in a capsid-independent manner, in contrast to most dsRNA viruses.
has issue date	2009-02-27(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2008.11.029
bibo:pmid	19063900
has license	els-covid
sha1sum (hex)	b045dde70d5ae1b3b0c8cfc27b06d9c7ad99e50f
schema:url	https://doi.org/10.1016/j.jmb.2008.11.029
resource representing a document's title	Infectious Bursal Disease Virus: Ribonucleoprotein Complexes of a Double-Stranded RNA Virus
has PubMed Central identifier	PMC7173181
has PubMed identifier	19063900
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:b045dde70d5ae1b3b0c8cfc27b06d9c7ad99e50f#body_text
is schema:about of	named entity 'VP3' named entity 'RNase III' named entity 'filamentous' named entity 'complexes' named entity 'bound' named entity 'RNP' named entity 'dsRNA' named entity 'Birnaviridae' named entity 'ribonucleoprotein' named entity 'complexes' named entity 'complexes' named entity 'functional analysis' named entity 'negative' named entity 'histone-like' named entity 'bipartite' named entity 'disruption' named entity 'viruses' named entity 'dsRNA' named entity 'viruses' named entity 'viruses' named entity 'organisms' named entity 'exception' named entity 'RNP' named entity 'renders' named entity 'VP3' named entity 'Sensitivity' named entity 'VP3' named entity 'viral particles' named entity 'histone-like' named entity 'Genome' named entity 'single-stranded RNA' named entity 'virion' named entity 'scaffolding' named entity 'dsRNA' named entity 'living organisms' named entity 'RNP' named entity 'VPg' named entity 'dsRNA' named entity 'nucleocapsid proteins' named entity 'Ribonucleoprotein Complexes' named entity 'capsid proteins' named entity 'RNP' named entity 'stoichiometry' named entity 'ethidium bromide' named entity 'molecule' named entity '1 mM' named entity 'glycerol' named entity 'ethidium bromide' named entity 'dsRNA-binding protein' named entity 'JEOL' named entity 'moonlighting protein' named entity 'incubation' named entity 'substrate' named entity 'VPg' named entity 'RNA synthesis' named entity 'RNP' named entity 'VPg' named entity 'VPg' named entity 'proline' named entity 'capsid' named entity 'protein kinase' named entity 'negative control' named entity 'aqueous' named entity 'dsRNA' named entity 'IBDV' named entity 'IBDV' named entity 'RNase III' named entity 'scaffolding protein' named entity 'BSA' named entity 'Moonlighting proteins' named entity 'capsid' named entity 'VP3' named entity 'RNP' named entity 'dsRNA' named entity 'IBDV' named entity 'Molecular Dynamics'

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