SrasV1, PubMed, Corpus, bibRecord, 001705

In vitro reconstitution of SARS-coronavirus mRNA cap methylation.

Identifieur interne : 001705 ( PubMed/Corpus ); précédent : 001704; suivant : 001706

In vitro reconstitution of SARS-coronavirus mRNA cap methylation.

Auteurs : Mickaël Bouvet ; Claire Debarnot ; Isabelle Imbert ; Barbara Selisko ; Eric J. Snijder ; Bruno Canard ; Etienne Decroly

Source :

PLoS pathogens [ 1553-7374 ] ; 2010.

RBID : pubmed:20421945

English descriptors

KwdEn :
- Exoribonucleases (chemistry), Exoribonucleases (genetics), Exoribonucleases (metabolism), Gene Expression Regulation, Viral, In Vitro Techniques, Methylation, RNA Caps (chemistry), RNA Caps (genetics), RNA Caps (metabolism), RNA, Messenger, SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), tRNA Methyltransferases.
MESH :
- chemical , chemistry : Exoribonucleases, RNA Caps, Viral Nonstructural Proteins.
- chemical , genetics : Exoribonucleases, RNA Caps, Viral Nonstructural Proteins.
- chemical , metabolism : Exoribonucleases, RNA Caps, Viral Nonstructural Proteins.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Gene Expression Regulation, Viral, In Vitro Techniques, Methylation, RNA, Messenger, tRNA Methyltransferases.

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.

DOI: 10.1371/journal.ppat.1000863
PubMed: 20421945

Links to Exploration step

pubmed:20421945

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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In vitro reconstitution of SARS-coronavirus mRNA cap methylation.

In vitro reconstitution of SARS-coronavirus mRNA cap methylation.

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