About: Coronavirus Nsp10, a Critical Co-factor for Activation of Multiple Replicative Enzymes

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About: Coronavirus Nsp10, a Critical Co-factor for Activation of Multiple Replicative Enzymes Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Coronavirus Nsp10, a Critical Co-factor for Activation of Multiple Replicative Enzymes
Creator	Canard, Bruno Decroly, Etienne Imbert, Isabelle Betzi, Stéphane Bouvet, Mickaël Guillemot, Jean-Claude Lugari, Adrien Lécine, Patrick Morelli, Xavier Pfefferle, Susanne Snijder, Eric Posthuma, Clara Zevenhoven, Jessika Drosten,
Source	Medline; PMC
abstract	The RNA-synthesizing machinery of the severe acute respiratory syndrome Coronavirus (SARS-CoV) is composed of 16 non-structural proteins (nsp1–16) encoded by ORF1a/1b. The 148-amino acid nsp10 subunit contains two zinc fingers and is known to interact with both nsp14 and nsp16, stimulating their respective 3′-5′ exoribonuclease and 2′-O-methyltransferase activities. Using alanine-scanning mutagenesis, in cellulo bioluminescence resonance energy transfer experiments, and in vitro pulldown assays, we have now identified the key residues on the nsp10 surface that interact with nsp14. The functional consequences of mutations introduced at these positions were first evaluated biochemically by monitoring nsp14 exoribonuclease activity. Disruption of the nsp10-nsp14 interaction abrogated the nsp10-driven activation of the nsp14 exoribonuclease. We further showed that the nsp10 surface interacting with nsp14 overlaps with the surface involved in the nsp10-mediated activation of nsp16 2′-O-methyltransferase activity, suggesting that nsp10 is a major regulator of SARS-CoV replicase function. In line with this notion, reverse genetics experiments supported an essential role of the nsp10 surface that interacts with nsp14 in SARS-CoV replication, as several mutations that abolished the interaction in vitro yielded a replication-negative viral phenotype. In contrast, mutants in which the nsp10-nsp16 interaction was disturbed proved to be crippled but viable. These experiments imply that the nsp10 surface that interacts with nsp14 and nsp16 and possibly other subunits of the viral replication complex may be a target for the development of antiviral compounds against pathogenic coronaviruses.
has issue date	2014-07-29(xsd:dateTime)
bibo:doi	10.1074/jbc.m114.577353
bibo:pmid	25074927
has license	bronze-oa
sha1sum (hex)	c808733cdd3d3bbd4da5c98546b0bf1809b3cc30
schema:url	https://doi.org/10.1074/jbc.m114.577353
resource representing a document's title	Coronavirus Nsp10, a Critical Co-factor for Activation of Multiple Replicative Enzymes
has PubMed Central identifier	PMC4162180
has PubMed identifier	25074927
schema:publication	Journal of Biological Chemistry
resource representing a document's body	covid:c808733cdd3d3bbd4da5c98546b0bf1809b3cc30#body_text
is schema:about of	named entity 'plays' named entity 'SARS-CoV' named entity 'stimulates' named entity 'Enzymes' named entity 'Multiple' named entity 'NSP14' named entity 'MULTIPLE' named entity 'ENZYMES' named entity 'ROLE' named entity 'CRITICAL' named entity 'RESULTS' named entity 'CRITICAL' named entity 'CORONAVIRUS' named entity 'FACTOR' named entity 'ACTIVATION' named entity 'BACKGROUND' named entity 'REPLICATION' named entity 'ACTIVITIES' named entity 'DEMONSTRATED' named entity 'SARS-COV' named entity 'SURFACE' named entity 'MAPPED' named entity 'BINDS' named entity 'PLAYS' named entity 'INTERACTING' covid:arg/c808733cdd3d3bbd4da5c98546b0bf1809b3cc30 named entity 'binds' named entity 'SARS-CoV' named entity 'Enzymes' named entity 'mRNAs' named entity 'plasmid DNA' named entity 'SARS-CoV' named entity 'coronaviruses' named entity 'RNA genome' named entity 'virus' named entity 'active site' named entity 'protein' named entity 'BHK' named entity 'phenotypes' named entity 'ExoN' named entity 'Nidovirales' named entity 'phenotype' named entity 'viral genome' named entity 'Lys' named entity 'PMSF' named entity 'Exonuclease' named entity 'SARS' named entity 'Thr' named entity 'antibodies' named entity 'oligo' named entity 'ExoN' named entity 'virus' named entity 'eukaryotic cell' named entity 'virus replication' named entity 'polyadenylated' named entity 'wild-type' named entity 'cDNA clones' named entity 'eukaryotic cells' named entity 'Tyr' named entity 'guanylyltransferase' named entity 'cell culture' named entity 'PCR amplification' named entity 'titer' named entity 'antiviral drug' named entity 'plasmid' named entity 'hexamers' named entity 'phenotype' named entity 'South Dakota State University'

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