The coronavirus nucleocapsid protein is ADP-ribosylated
Identifieur interne : 000B55 ( Main/Exploration ); précédent : 000B54; suivant : 000B56The coronavirus nucleocapsid protein is ADP-ribosylated
Auteurs : Matthew E. Grunewald ; Anthony R. Fehr ; Jeremiah Athmer ; Stanley PerlmanSource :
- Virology [ 0042-6822 ] ; 2017.
Descripteurs français
- KwdFr :
- Animaux, Coronavirus (génétique), Coronavirus (métabolisme), Domaines protéiques, Humains, Lignée cellulaire, Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Régulation de l'expression des gènes viraux (physiologie).
- MESH :
- génétique : Coronavirus, Protéines nucléocapside, Protéines virales non structurales.
- métabolisme : Coronavirus, Protéines nucléocapside, Protéines virales non structurales.
- physiologie : Régulation de l'expression des gènes viraux.
- Animaux, Domaines protéiques, Humains, Lignée cellulaire.
English descriptors
- KwdEn :
- ADP-Ribosylation (physiology), Animals, Cell Line, Coronavirus (genetics), Coronavirus (metabolism), Gene Expression Regulation, Viral (physiology), Humans, Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Domains, Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , genetics : Nucleocapsid Proteins, Viral Nonstructural Proteins.
- genetics : Coronavirus.
- metabolism : Coronavirus, Nucleocapsid Proteins, Viral Nonstructural Proteins.
- physiology : ADP-Ribosylation, Gene Expression Regulation, Viral.
- Animals, Cell Line, Humans, Protein Domains.
Abstract
ADP-ribosylation is a common post-translational modification, although how it modulates RNA virus infection is not well understood. While screening for ADP-ribosylated proteins during coronavirus (CoV) infection, we detected a ~55 kDa ADP-ribosylated protein in mouse hepatitis virus (MHV)-infected cells and in virions, which we identified as the viral nucleocapsid (N) protein. The N proteins of porcine epidemic diarrhea virus (PEDV), severe acute respiratory syndrome (SARS)-CoV and Middle East respiratory syndrome (MERS)-CoV were also ADP-ribosylated. ADP-ribosylation of N protein was also observed in cells exogenously expressing N protein by transduction using Venezuelan equine encephalitis virus replicon particles (VRPs). However, plasmid-derived N protein was not ADP-ribosylated following transient transfection but was ADP-ribosylated after MHV infection, indicating that this modification requires virus infection. In conclusion, we have identified a novel post-translation modification of the CoV N protein that may play a regulatory role for this important structural protein.
Url:
DOI: 10.1016/j.virol.2017.11.020
PubMed: 29199039
PubMed Central: 5871557
Affiliations:
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Fehr</name></author><author><name sortKey="Athmer, Jeremiah" sort="Athmer, Jeremiah" uniqKey="Athmer J" first="Jeremiah" last="Athmer">Jeremiah Athmer</name></author><author><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">29199039</idno><idno type="pmc">5871557</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5871557</idno><idno type="RBID">PMC:5871557</idno><idno type="doi">10.1016/j.virol.2017.11.020</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">001183</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001183</idno><idno type="wicri:Area/Pmc/Curation">001183</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001183</idno><idno type="wicri:Area/Pmc/Checkpoint">000697</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000697</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:29199039</idno><idno type="wicri:Area/PubMed/Corpus">000A62</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A62</idno><idno type="wicri:Area/PubMed/Curation">000A62</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000A62</idno><idno type="wicri:Area/PubMed/Checkpoint">000739</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000739</idno><idno type="wicri:Area/Ncbi/Merge">001C70</idno><idno type="wicri:Area/Ncbi/Curation">001C70</idno><idno type="wicri:Area/Ncbi/Checkpoint">001C70</idno><idno type="wicri:doubleKey">0042-6822:2017:Grunewald M:the:coronavirus:nucleocapsid</idno><idno type="wicri:Area/Main/Merge">000B58</idno><idno type="wicri:Area/Main/Curation">000B55</idno><idno type="wicri:Area/Main/Exploration">000B55</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The coronavirus nucleocapsid protein is ADP-ribosylated</title><author><name sortKey="Grunewald, Matthew E" sort="Grunewald, Matthew E" uniqKey="Grunewald M" first="Matthew E." last="Grunewald">Matthew E. Grunewald</name></author><author><name sortKey="Fehr, Anthony R" sort="Fehr, Anthony R" uniqKey="Fehr A" first="Anthony R." last="Fehr">Anthony R. Fehr</name></author><author><name sortKey="Athmer, Jeremiah" sort="Athmer, Jeremiah" uniqKey="Athmer J" first="Jeremiah" last="Athmer">Jeremiah Athmer</name></author><author><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ADP-Ribosylation (physiology)</term><term>Animals</term><term>Cell Line</term><term>Coronavirus (genetics)</term><term>Coronavirus (metabolism)</term><term>Gene Expression Regulation, Viral (physiology)</term><term>Humans</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Domains</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Coronavirus (génétique)</term><term>Coronavirus (métabolisme)</term><term>Domaines protéiques</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (métabolisme)</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>Régulation de l'expression des gènes viraux (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Coronavirus</term><term>Protéines nucléocapside</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term><term>Nucleocapsid Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term><term>Protéines nucléocapside</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Régulation de l'expression des gènes viraux</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>ADP-Ribosylation</term><term>Gene Expression Regulation, Viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Protein Domains</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Domaines protéiques</term><term>Humains</term><term>Lignée cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>ADP-ribosylation is a common post-translational modification, although how it modulates RNA virus infection is not well understood. While screening for ADP-ribosylated proteins during coronavirus (CoV) infection, we detected a ~55 kDa ADP-ribosylated protein in mouse hepatitis virus (MHV)-infected cells and in virions, which we identified as the viral nucleocapsid (N) protein. The N proteins of porcine epidemic diarrhea virus (PEDV), severe acute respiratory syndrome (SARS)-CoV and Middle East respiratory syndrome (MERS)-CoV were also ADP-ribosylated. ADP-ribosylation of N protein was also observed in cells exogenously expressing N protein by transduction using Venezuelan equine encephalitis virus replicon particles (VRPs). However, plasmid-derived N protein was not ADP-ribosylated following transient transfection but was ADP-ribosylated after MHV infection, indicating that this modification requires virus infection. In conclusion, we have identified a novel post-translation modification of the CoV N protein that may play a regulatory role for this important structural protein.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Atasheva, S" uniqKey="Atasheva S">S. Atasheva</name></author><author><name sortKey="Akhrymuk, M" uniqKey="Akhrymuk M">M. Akhrymuk</name></author><author><name sortKey="Frolova, E I" uniqKey="Frolova E">E.I. Frolova</name></author><author><name sortKey="Frolov, I" uniqKey="Frolov I">I. Frolov</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Atasheva, S" uniqKey="Atasheva S">S. Atasheva</name></author><author><name sortKey="Frolova, E I" uniqKey="Frolova E">E.I. Frolova</name></author><author><name sortKey="Frolov, I" uniqKey="Frolov I">I. Frolov</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bailey, O T" uniqKey="Bailey O">O.T. 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