Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.
Identifieur interne : 000A98 ( PubMed/Curation ); précédent : 000A97; suivant : 000A99Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.
Auteurs : Yingying Cong [Pays-Bas] ; Franziska Kriegenburg [Pays-Bas] ; Cornelis A M. De Haan [Pays-Bas] ; Fulvio Reggiori [Pays-Bas]Source :
- Scientific reports [ 2045-2322 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Nucleocapsid Proteins.
- Animals, Cell Line, Mice, Protein Binding, Protein Multimerization.
Abstract
Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs.
DOI: 10.1038/s41598-017-06062-w
PubMed: 28720894
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Deusinglaan 1, 9713 AV, Groningen, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen</wicri:regionArea></affiliation></author><author><name sortKey="Kriegenburg, Franziska" sort="Kriegenburg, Franziska" uniqKey="Kriegenburg F" first="Franziska" last="Kriegenburg">Franziska Kriegenburg</name><affiliation wicri:level="1"><nlm:affiliation>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen</wicri:regionArea></affiliation></author><author><name sortKey="De Haan, Cornelis A M" sort="De Haan, Cornelis A M" uniqKey="De Haan C" first="Cornelis A M" last="De Haan">Cornelis A M. De Haan</name><affiliation wicri:level="1"><nlm:affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht</wicri:regionArea></affiliation></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name><affiliation wicri:level="1"><nlm:affiliation>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen, The Netherlands. f.m.reggiori@umcg.nl.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen</wicri:regionArea></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Mice</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Multimerization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Multimérisation de protéines</term><term>Protéines nucléocapside (métabolisme)</term><term>Souris</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Mice</term><term>Protein Binding</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Multimérisation de protéines</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28720894</PMID><DateCompleted><Year>2019</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>23</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>1</Issue><PubDate><Year>2017</Year><Month>07</Month><Day>18</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.</ArticleTitle><Pagination><MedlinePgn>5740</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-017-06062-w</ELocationID><Abstract><AbstractText>Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cong</LastName><ForeName>Yingying</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kriegenburg</LastName><ForeName>Franziska</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Haan</LastName><ForeName>Cornelis A M</ForeName><Initials>CAM</Initials><AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reggiori</LastName><ForeName>Fulvio</ForeName><Initials>F</Initials><Identifier Source="ORCID">0000-0003-2652-2686</Identifier><AffiliationInfo><Affiliation>Department of Cell Biology, University Medical Center Groningen, University of Groningen, A. 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