The coronavirus nucleocapsid protein is ADP-ribosylated.
Identifieur interne : 000A62 ( PubMed/Corpus ); précédent : 000A61; suivant : 000A63The coronavirus nucleocapsid protein is ADP-ribosylated.
Auteurs : Matthew E. Grunewald ; Anthony R. Fehr ; Jeremiah Athmer ; Stanley PerlmanSource :
- Virology [ 1096-0341 ] ; 2018.
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 ~55kDa 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.
DOI: 10.1016/j.virol.2017.11.020
PubMed: 29199039
Links to Exploration step
pubmed:29199039Le document en format XML
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Fehr</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Athmer, Jeremiah" sort="Athmer, Jeremiah" uniqKey="Athmer J" first="Jeremiah" last="Athmer">Jeremiah Athmer</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States. 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Grunewald</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Fehr, Anthony R" sort="Fehr, Anthony R" uniqKey="Fehr A" first="Anthony R" last="Fehr">Anthony R. Fehr</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Athmer, Jeremiah" sort="Athmer, Jeremiah" uniqKey="Athmer J" first="Jeremiah" last="Athmer">Jeremiah Athmer</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States. Electronic address: Stanley-Perlman@uiowa.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Virology</title><idno type="eISSN">1096-0341</idno><imprint><date when="2018" type="published">2018</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="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="metabolism" xml:lang="en"><term>Coronavirus</term><term>Nucleocapsid Proteins</term><term>Viral Nonstructural Proteins</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></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 ~55kDa 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29199039</PMID><DateCompleted><Year>2018</Year><Month>04</Month><Day>20</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0341</ISSN><JournalIssue CitedMedium="Internet"><Volume>517</Volume><PubDate><Year>2018</Year><Month>04</Month></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>The coronavirus nucleocapsid protein is ADP-ribosylated.</ArticleTitle><Pagination><MedlinePgn>62-68</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0042-6822(17)30399-9</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virol.2017.11.020</ELocationID><Abstract><AbstractText>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 ~55kDa 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.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Grunewald</LastName><ForeName>Matthew E</ForeName><Initials>ME</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fehr</LastName><ForeName>Anthony R</ForeName><Initials>AR</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Athmer</LastName><ForeName>Jeremiah</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Perlman</LastName><ForeName>Stanley</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA 52242, United States. Electronic address: Stanley-Perlman@uiowa.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>T32 AI007260</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 NS036592</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 AI007533</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI129269</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>F32 AI113973</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI060699</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 AI007511</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 GM007337</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>12</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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