About: In Vitro Reconstitution of SARS-Coronavirus mRNA Cap Methylation

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	In Vitro Reconstitution of SARS-Coronavirus mRNA Cap Methylation
Creator	Snijder, E Bouvet, M Debarnot, C Imbert, I Selisko, B
Source	Medline; PMC
abstract	SARS-coronavirus (SARS-CoV) genome expression depends on the synthesis of a set of mRNAs, which presumably are capped at their 5′ end and direct the synthesis of all viral proteins in the infected cell. Sixteen viral non-structural proteins (nsp1 to nsp16) constitute an unusually large replicase complex, which includes two methyltransferases putatively involved in viral mRNA cap formation. The S-adenosyl-L-methionine (AdoMet)-dependent (guanine-N7)-methyltransferase (N7-MTase) activity was recently attributed to nsp14, whereas nsp16 has been predicted to be the AdoMet-dependent (nucleoside-2′O)-methyltransferase. Here, we have reconstituted complete SARS-CoV mRNA cap methylation in vitro. We show that mRNA cap methylation requires a third viral protein, nsp10, which acts as an essential trigger to complete RNA cap-1 formation. The obligate sequence of methylation events is initiated by nsp14, which first methylates capped RNA transcripts to generate cap-0 (7Me)GpppA-RNAs. The latter are then selectively 2′O-methylated by the 2′O-MTase nsp16 in complex with its activator nsp10 to give rise to cap-1 (7Me)GpppA(2′OMe)-RNAs. Furthermore, sensitive in vitro inhibition assays of both activities show that aurintricarboxylic acid, active in SARS-CoV infected cells, targets both MTases with IC(50) values in the micromolar range, providing a validated basis for anti-coronavirus drug design.
has issue date	2010-04-22(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1000863
bibo:pmid	20421945
has license	cc-by
sha1sum (hex)	5484795b90c22596ead5f0b9ccf08d95a3e6f5c2
schema:url	https://doi.org/10.1371/journal.ppat.1000863
resource representing a document's title	In Vitro Reconstitution of SARS-Coronavirus mRNA Cap Methylation
has PubMed Central identifier	PMC2858705
has PubMed identifier	20421945
schema:publication	PLoS Pathog
resource representing a document's body	covid:5484795b90c22596ead5f0b9ccf08d95a3e6f5c2#body_text
is schema:about of	named entity 'cap' named entity 'cap' named entity 'inhibition' named entity 'mRNA' named entity 'cell' named entity '7Me' named entity 'methylation' named entity 'linear phase' named entity 'co-factor' named entity 'methylated' named entity 'coronaviruses' named entity 'mechanism of action' named entity 'replicase' named entity 'co-substrate' named entity 'protein' named entity 'Novagen' named entity 'ampicillin' named entity 'New England Biolabs' named entity 'methylated' named entity 'genome' named entity 'exonuclease' named entity 'adenosine' named entity 'protein' named entity 'protein' named entity 'dependent' named entity 'methylates' named entity 'coronavirus' named entity 'SARS-CoV' named entity 'AdoMet' named entity 'mRNA' named entity 'cap formation' named entity 'genome expression' named entity 'SARS-CoV' named entity 'methylation' named entity 'methyltransferase' named entity 'coronavirus' named entity 'viral protein' named entity 'mRNA' named entity 'active site' named entity '0.45' named entity 'mRNA' named entity 'protein' named entity 'RNA' named entity 'RNA' named entity 'binding site' named entity 'chitin' named entity 'SARS-CoV' named entity 'strep-tag' named entity 'RNA' named entity 'bioinformatics' named entity 'methylation' named entity 'GTP' named entity 'proximal' named entity 'SARS' named entity 'protein-protein interactions' named entity 'endoplasmic reticulum' named entity 'co-expressed' named entity 'flaviviruses' named entity 'ribavirin' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'DTT' named entity 'IPTG' named entity 'TLC' named entity 'RNA' named entity 'RNA' named entity 'mRNA' named entity '1.2' named entity 'trypsin' named entity 'guanine' named entity 'methyl' named entity 'nucleotide' named entity 'RNA' named entity 'cleavage' named entity 'mRNAs' named entity 'AdoMet' named entity 'membrane-bound'

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