The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein.
Identifieur interne : 001994 ( PubMed/Checkpoint ); précédent : 001993; suivant : 001995The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein.
Auteurs : Isabelle Imbert [France] ; Eric J. Snijder ; Maria Dimitrova ; Jean-Claude Guillemot ; Patrick Lécine ; Bruno CanardSource :
- Virus research [ 0168-1702 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Dimérisation, Humains, Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), RNA replicase (), RNA replicase (métabolisme), Réplication virale, Techniques de double hybride, Transcription génétique, Virus du SRAS (métabolisme).
- MESH :
- génétique : Protéines virales non structurales.
- métabolisme : Protéines virales non structurales, RNA replicase, Virus du SRAS.
- Animaux, Cellules Vero, Dimérisation, Humains, Protéines virales non structurales, RNA replicase, Réplication virale, Techniques de double hybride, Transcription génétique.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, Dimerization, Humans, RNA Replicase (chemistry), RNA Replicase (metabolism), SARS Virus (metabolism), Transcription, Genetic, Two-Hybrid System Techniques, Vero Cells, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Replication.
- MESH :
- chemical , chemistry : RNA Replicase, Viral Nonstructural Proteins.
- chemical , genetics : Viral Nonstructural Proteins.
- chemical , metabolism : RNA Replicase, Viral Nonstructural Proteins.
- metabolism : SARS Virus.
- Animals, Chlorocebus aethiops, Dimerization, Humans, Transcription, Genetic, Two-Hybrid System Techniques, Vero Cells, Virus Replication.
Abstract
Many genetic and mechanistic features distinguish the coronavirus replication machinery from that encoded by most other RNA viruses. The coronavirus replication/transcription complex is an assembly of viral and, most probably, cellular proteins that mediate the synthesis of both the unusually large (approximately 30 kb) RNA genome and an extensive set of subgenomic mRNAs. The viral components of the complex are encoded by the giant replicase gene, which is expressed in the form of two polyproteins (pp1a and pp1ab) that are processed into 16 cleavage products (nonstructural proteins 1-16). Using the combination of yeast two-hybrid screening and GST pull-down assays, we have now analyzed all potential interactions between SARS-Coronavirus nonstructural proteins, which may contribute to the structure and/or function of the viral replication/transcription complex. We demonstrate the existence of a complex network of interactions involving all 16 nonstructural proteins. Our results both confirmed previously described associations and identified novel heterodimerizations. The interaction map thus provides a sum of the interactions that may occur at some point during coronavirus RNA synthesis and provides a framework for future research.
DOI: 10.1016/j.virusres.2007.11.017
PubMed: 18255185
Affiliations:
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The coronavirus replication/transcription complex is an assembly of viral and, most probably, cellular proteins that mediate the synthesis of both the unusually large (approximately 30 kb) RNA genome and an extensive set of subgenomic mRNAs. The viral components of the complex are encoded by the giant replicase gene, which is expressed in the form of two polyproteins (pp1a and pp1ab) that are processed into 16 cleavage products (nonstructural proteins 1-16). Using the combination of yeast two-hybrid screening and GST pull-down assays, we have now analyzed all potential interactions between SARS-Coronavirus nonstructural proteins, which may contribute to the structure and/or function of the viral replication/transcription complex. We demonstrate the existence of a complex network of interactions involving all 16 nonstructural proteins. Our results both confirmed previously described associations and identified novel heterodimerizations. The interaction map thus provides a sum of the interactions that may occur at some point during coronavirus RNA synthesis and provides a framework for future research.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18255185</PMID><DateCompleted><Year>2008</Year><Month>06</Month><Day>30</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1702</ISSN><JournalIssue CitedMedium="Print"><Volume>133</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>May</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>The SARS-Coronavirus PLnc domain of nsp3 as a replication/transcription scaffolding protein.</ArticleTitle><Pagination><MedlinePgn>136-48</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virusres.2007.11.017</ELocationID><Abstract><AbstractText>Many genetic and mechanistic features distinguish the coronavirus replication machinery from that encoded by most other RNA viruses. The coronavirus replication/transcription complex is an assembly of viral and, most probably, cellular proteins that mediate the synthesis of both the unusually large (approximately 30 kb) RNA genome and an extensive set of subgenomic mRNAs. The viral components of the complex are encoded by the giant replicase gene, which is expressed in the form of two polyproteins (pp1a and pp1ab) that are processed into 16 cleavage products (nonstructural proteins 1-16). Using the combination of yeast two-hybrid screening and GST pull-down assays, we have now analyzed all potential interactions between SARS-Coronavirus nonstructural proteins, which may contribute to the structure and/or function of the viral replication/transcription complex. We demonstrate the existence of a complex network of interactions involving all 16 nonstructural proteins. Our results both confirmed previously described associations and identified novel heterodimerizations. The interaction map thus provides a sum of the interactions that may occur at some point during coronavirus RNA synthesis and provides a framework for future research.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Imbert</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'Ingénieurs de Luminy-Case 925, Marseille Cedex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Snijder</LastName><ForeName>Eric J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Dimitrova</LastName><ForeName>Maria</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Guillemot</LastName><ForeName>Jean-Claude</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Lécine</LastName><ForeName>Patrick</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>02</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber><NameOfSubstance UI="D012324">RNA 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