SARS-CoV ORF1b-encoded nonstructural proteins 12-16: replicative enzymes as antiviral targets.
Identifieur interne : 001B30 ( PubMed/Corpus ); précédent : 001B29; suivant : 001B31SARS-CoV ORF1b-encoded nonstructural proteins 12-16: replicative enzymes as antiviral targets.
Auteurs : Lorenzo Subissi ; Isabelle Imbert ; François Ferron ; Axelle Collet ; Bruno Coutard ; Etienne Decroly ; Bruno CanardSource :
- Antiviral research [ 1872-9096 ] ; 2014.
English descriptors
- KwdEn :
- Antiviral Agents (pharmacology), Humans, Methyltransferases (antagonists & inhibitors), Methyltransferases (metabolism), RNA Helicases (antagonists & inhibitors), RNA Helicases (metabolism), RNA Replicase (antagonists & inhibitors), RNA Replicase (metabolism), Ribonucleases (antagonists & inhibitors), Ribonucleases (metabolism), SARS Virus (enzymology), SARS Virus (physiology), Viral Nonstructural Proteins (antagonists & inhibitors), Viral Nonstructural Proteins (metabolism), Virus Replication.
- MESH :
- chemical , antagonists & inhibitors : Methyltransferases, RNA Helicases, RNA Replicase, Ribonucleases, Viral Nonstructural Proteins.
- chemical , metabolism : Methyltransferases, RNA Helicases, RNA Replicase, Ribonucleases, Viral Nonstructural Proteins.
- chemical , pharmacology : Antiviral Agents.
- enzymology : SARS Virus.
- physiology : SARS Virus.
- Humans, Virus Replication.
Abstract
The SARS (severe acute respiratory syndrome) pandemic caused ten years ago by the SARS-coronavirus (SARS-CoV) has stimulated a number of studies on the molecular biology of coronaviruses. This research has provided significant new insight into many mechanisms used by the coronavirus replication-transcription complex (RTC). The RTC directs and coordinates processes in order to replicate and transcribe the coronavirus genome, a single-stranded, positive-sense RNA of outstanding length (∼27-32kilobases). Here, we review the up-to-date knowledge on SARS-CoV replicative enzymes encoded in the ORF1b, i.e., the main RNA-dependent RNA polymerase (nsp12), the helicase/triphosphatase (nsp13), two unusual ribonucleases (nsp14, nsp15) and RNA-cap methyltransferases (nsp14, nsp16). We also review how these enzymes co-operate with other viral co-factors (nsp7, nsp8, and nsp10) to regulate their activity. These last ten years of research on SARS-CoV have considerably contributed to unravel structural and functional details of one of the most fascinating replication/transcription machineries of the RNA virus world. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10years of research on highly pathogenic human coronaviruses".
DOI: 10.1016/j.antiviral.2013.11.006
PubMed: 24269475
Links to Exploration step
pubmed:24269475Le document en format XML
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<front><div type="abstract" xml:lang="en">The SARS (severe acute respiratory syndrome) pandemic caused ten years ago by the SARS-coronavirus (SARS-CoV) has stimulated a number of studies on the molecular biology of coronaviruses. This research has provided significant new insight into many mechanisms used by the coronavirus replication-transcription complex (RTC). The RTC directs and coordinates processes in order to replicate and transcribe the coronavirus genome, a single-stranded, positive-sense RNA of outstanding length (∼27-32kilobases). Here, we review the up-to-date knowledge on SARS-CoV replicative enzymes encoded in the ORF1b, i.e., the main RNA-dependent RNA polymerase (nsp12), the helicase/triphosphatase (nsp13), two unusual ribonucleases (nsp14, nsp15) and RNA-cap methyltransferases (nsp14, nsp16). We also review how these enzymes co-operate with other viral co-factors (nsp7, nsp8, and nsp10) to regulate their activity. These last ten years of research on SARS-CoV have considerably contributed to unravel structural and functional details of one of the most fascinating replication/transcription machineries of the RNA virus world. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10years of research on highly pathogenic human coronaviruses". </div>
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