The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing.
Identifieur interne : 000C03 ( PubMed/Corpus ); précédent : 000C02; suivant : 000C04The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing.
Auteurs : E J Snijder ; E. Decroly ; J. ZiebuhrSource :
- Advances in virus research [ 1557-8399 ] ; 2016.
English descriptors
- KwdEn :
- Acid Anhydride Hydrolases (genetics), Acid Anhydride Hydrolases (metabolism), Animals, Gene Expression Regulation, Viral, Humans, Methyltransferases (genetics), Methyltransferases (metabolism), Protein Domains, RNA Helicases (genetics), RNA Helicases (metabolism), RNA, Viral (biosynthesis), RNA, Viral (genetics), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (pathology), Severe Acute Respiratory Syndrome (virology), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Replication.
- MESH :
- chemical , biosynthesis : RNA, Viral.
- chemical , genetics : Acid Anhydride Hydrolases, Methyltransferases, RNA Helicases, RNA, Viral, Viral Nonstructural Proteins.
- chemical , metabolism : Acid Anhydride Hydrolases, Methyltransferases, RNA Helicases, Viral Nonstructural Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- pathology : Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Gene Expression Regulation, Viral, Humans, Protein Domains, Virus Replication.
Abstract
Coronaviruses are animal and human pathogens that can cause lethal zoonotic infections like SARS and MERS. They have polycistronic plus-stranded RNA genomes and belong to the order Nidovirales, a diverse group of viruses for which common ancestry was inferred from the common principles underlying their genome organization and expression, and from the conservation of an array of core replicase domains, including key RNA-synthesizing enzymes. Coronavirus genomes (~26-32 kilobases) are the largest RNA genomes known to date and their expansion was likely enabled by acquiring enzyme functions that counter the commonly high error frequency of viral RNA polymerases. The primary functions that direct coronavirus RNA synthesis and processing reside in nonstructural protein (nsp) 7 to nsp16, which are cleavage products of two large replicase polyproteins translated from the coronavirus genome. Significant progress has now been made regarding their structural and functional characterization, stimulated by technical advances like improved methods for bioinformatics and structural biology, in vitro enzyme characterization, and site-directed mutagenesis of coronavirus genomes. Coronavirus replicase functions include more or less universal activities of plus-stranded RNA viruses, like an RNA polymerase (nsp12) and helicase (nsp13), but also a number of rare or even unique domains involved in mRNA capping (nsp14, nsp16) and fidelity control (nsp14). Several smaller subunits (nsp7-nsp10) act as crucial cofactors of these enzymes and contribute to the emerging "nsp interactome." Understanding the structure, function, and interactions of the RNA-synthesizing machinery of coronaviruses will be key to rationalizing their evolutionary success and the development of improved control strategies.
DOI: 10.1016/bs.aivir.2016.08.008
PubMed: 27712628
Links to Exploration step
pubmed:27712628Le document en format XML
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Electronic address: e.j.snijder@lumc.nl.</nlm:affiliation></affiliation></author><author><name sortKey="Decroly, E" sort="Decroly, E" uniqKey="Decroly E" first="E" last="Decroly">E. Decroly</name><affiliation><nlm:affiliation>Aix-Marseille Université, AFMB UMR 7257, Marseille, France; CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Ziebuhr, J" sort="Ziebuhr, J" uniqKey="Ziebuhr J" first="J" last="Ziebuhr">J. Ziebuhr</name><affiliation><nlm:affiliation>Institute of Medical Virology, Justus Liebig University Giessen, Giessen, Germany. 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They have polycistronic plus-stranded RNA genomes and belong to the order Nidovirales, a diverse group of viruses for which common ancestry was inferred from the common principles underlying their genome organization and expression, and from the conservation of an array of core replicase domains, including key RNA-synthesizing enzymes. Coronavirus genomes (~26-32 kilobases) are the largest RNA genomes known to date and their expansion was likely enabled by acquiring enzyme functions that counter the commonly high error frequency of viral RNA polymerases. The primary functions that direct coronavirus RNA synthesis and processing reside in nonstructural protein (nsp) 7 to nsp16, which are cleavage products of two large replicase polyproteins translated from the coronavirus genome. Significant progress has now been made regarding their structural and functional characterization, stimulated by technical advances like improved methods for bioinformatics and structural biology, in vitro enzyme characterization, and site-directed mutagenesis of coronavirus genomes. Coronavirus replicase functions include more or less universal activities of plus-stranded RNA viruses, like an RNA polymerase (nsp12) and helicase (nsp13), but also a number of rare or even unique domains involved in mRNA capping (nsp14, nsp16) and fidelity control (nsp14). Several smaller subunits (nsp7-nsp10) act as crucial cofactors of these enzymes and contribute to the emerging "nsp interactome." Understanding the structure, function, and interactions of the RNA-synthesizing machinery of coronaviruses will be key to rationalizing their evolutionary success and the development of improved control strategies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27712628</PMID><DateCompleted><Year>2017</Year><Month>01</Month><Day>11</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-8399</ISSN><JournalIssue CitedMedium="Internet"><Volume>96</Volume><PubDate><Year>2016</Year></PubDate></JournalIssue><Title>Advances in virus research</Title><ISOAbbreviation>Adv. Virus Res.</ISOAbbreviation></Journal><ArticleTitle>The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing.</ArticleTitle><Pagination><MedlinePgn>59-126</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0065-3527(16)30047-1</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/bs.aivir.2016.08.008</ELocationID><Abstract><AbstractText>Coronaviruses are animal and human pathogens that can cause lethal zoonotic infections like SARS and MERS. They have polycistronic plus-stranded RNA genomes and belong to the order Nidovirales, a diverse group of viruses for which common ancestry was inferred from the common principles underlying their genome organization and expression, and from the conservation of an array of core replicase domains, including key RNA-synthesizing enzymes. Coronavirus genomes (~26-32 kilobases) are the largest RNA genomes known to date and their expansion was likely enabled by acquiring enzyme functions that counter the commonly high error frequency of viral RNA polymerases. The primary functions that direct coronavirus RNA synthesis and processing reside in nonstructural protein (nsp) 7 to nsp16, which are cleavage products of two large replicase polyproteins translated from the coronavirus genome. Significant progress has now been made regarding their structural and functional characterization, stimulated by technical advances like improved methods for bioinformatics and structural biology, in vitro enzyme characterization, and site-directed mutagenesis of coronavirus genomes. Coronavirus replicase functions include more or less universal activities of plus-stranded RNA viruses, like an RNA polymerase (nsp12) and helicase (nsp13), but also a number of rare or even unique domains involved in mRNA capping (nsp14, nsp16) and fidelity control (nsp14). Several smaller subunits (nsp7-nsp10) act as crucial cofactors of these enzymes and contribute to the emerging "nsp interactome." Understanding the structure, function, and interactions of the RNA-synthesizing machinery of coronaviruses will be key to rationalizing their evolutionary success and the development of improved control strategies.</AbstractText><CopyrightInformation>© 2016 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Snijder</LastName><ForeName>E J</ForeName><Initials>EJ</Initials><AffiliationInfo><Affiliation>Leiden University Medical Center, Leiden, The Netherlands. Electronic address: e.j.snijder@lumc.nl.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Decroly</LastName><ForeName>E</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, Marseille, France; CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ziebuhr</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Medical Virology, Justus Liebig University Giessen, Giessen, Germany. Electronic address: john.ziebuhr@viro.med.uni-giessen.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>BB/G012067/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>09</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Adv Virus Res</MedlineTA><NlmUniqueID>0370441</NlmUniqueID><ISSNLinking>0065-3527</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012367">RNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural 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