About: The PRRSV replicase: Exploring the multifunctionality of an intriguing set of nonstructural proteins

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About: The PRRSV replicase: Exploring the multifunctionality of an intriguing set of nonstructural proteins Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The PRRSV replicase: Exploring the multifunctionality of an intriguing set of nonstructural proteins
Creator	Fang, Ying Snijder, Eric
Source	Elsevier; Medline; PMC
abstract	Abstract Our knowledge about the structure and function of the nonstructural proteins (nsps) encoded by the arterivirus replicase gene has advanced in recent years. The continued characterization of the nsps of the arterivirus prototype equine arteritis virus has not only corroborated several important functional predictions, but also revealed various novel features of arteriviral replication. For porcine reproductive and respiratory syndrome virus (PRRSV), based on bioinformatics predictions and experimental studies, a processing map for the pp1a and pp1ab replicase polyproteins has been developed. Crystal structures have been resolved for two of the PRRSV nonstructural proteins that possess proteinase activity (nsp1α and nsp4). The functional characterization of the key enzymes for arterivirus RNA synthesis, the nsp9 RNA polymerase and nsp10 helicase, has been initiated. In addition, progress has been made on nsp functions relating to the regulation of subgenomic mRNAs synthesis (nsp1), the induction of replication-associated membrane rearrangements (nsp2 and nsp3), and an intriguing replicative endoribonuclease (nsp11) for which the natural substrate remains to be identified. The role of nsps in viral pathogenesis and host immunity is also being explored, and specific nsps (including nsp1α/β, nsp2, nsp4, nsp7, and nsp11) have been implicated in the modulation of host immune responses to PRRSV infection. The nsp3–8 region was identified as containing major virulence factors, although mechanistic information is scarce. The biological significance of PRRSV nsps in virus-host interactions and the technical advancements in engineering the PRRSV genome by reverse genetics are also reflected in recent developments in the area of vaccines and diagnostic assays.
has issue date	2010-12-31(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2010.07.030
bibo:pmid	20696193
has license	els-covid
sha1sum (hex)	9d02563440cffe40a3cd47fcdf3e2a5d7f3b9acb
schema:url	https://doi.org/10.1016/j.virusres.2010.07.030
resource representing a document's title	The PRRSV replicase: Exploring the multifunctionality of an intriguing set of nonstructural proteins
has PubMed Central identifier	PMC7114499
has PubMed identifier	20696193
schema:publication	Virus Research
resource representing a document's body	covid:9d02563440cffe40a3cd47fcdf3e2a5d7f3b9acb#body_text
is schema:about of	named entity 'developments' named entity 'RNA' named entity 'area' named entity 'features' named entity 'host' named entity 'region' named entity 'studies' named entity 'reverse genetics' named entity 'reproductive' covid:arg/9d02563440cffe40a3cd47fcdf3e2a5d7f3b9acb named entity 'continued' named entity 'endoribonuclease' named entity 'initiated' named entity 'encoded' named entity 'advanced' named entity 'mRNAs' named entity 'virus' named entity 'polymerase' named entity 'porcine' named entity 'replication' named entity 'substrate' named entity 'major' named entity 'induction' named entity 'genome' named entity 'immunity' named entity 'replicase' named entity 'infection' named entity 'virulence factors' named entity 'RNA synthesis' named entity 'gene' named entity 'nsp2' named entity 'proteinase' named entity 'nonstructural proteins' named entity 'viral pathogenesis' named entity 'RNA polymerase' named entity 'nonstructural proteins' named entity 'arterivirus' named entity 'experimental studies' named entity 'nsp4' named entity 'nonstructural proteins' named entity 'recombinant' named entity 'RNA' named entity 'host immune responses' named entity 'upregulation' named entity 'PRRSV' named entity 'antiviral' named entity 'N-terminal' named entity 'host immunity' named entity 'nsp2' named entity 'substrates' named entity 'minus-strand' named entity 'Asp' named entity 'nsp2' named entity 'infection' named entity 'proof of principle' named entity 'EAV' named entity 'proteolysis' named entity 'replicase' named entity 'nucleus' named entity 'nsp5' named entity 'IFN' named entity 'serum samples' named entity 'EAV' named entity 'nsp2' named entity 'reverse genetics' named entity 'immunoprecipitated' named entity 'animal models' named entity 'nsp2' named entity 'molecular basis' named entity 'viruses' named entity 'epitopes' named entity 'nuclear localization signals' named entity 'antibody response' named entity 'base pairs' named entity 'minus strand' named entity 'mRNAs' named entity 'phage' named entity 'recombinant' named entity 'cytoplasm' named entity 'ISGs'

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