Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.
Identifieur interne : 000E60 ( Main/Exploration ); précédent : 000E59; suivant : 000E61Coronavirus 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
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000A98
- to stream PubMed, to step Curation: 000A98
- to stream PubMed, to step Checkpoint: 000B44
- to stream Ncbi, to step Merge: 002E30
- to stream Ncbi, to step Curation: 002E30
- to stream Ncbi, to step Checkpoint: 002E30
- to stream Main, to step Merge: 000E62
- to stream Main, to step Curation: 000E60
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.</title><author><name sortKey="Cong, Yingying" sort="Cong, Yingying" uniqKey="Cong Y" first="Yingying" last="Cong">Yingying Cong</name><affiliation wicri:level="3"><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><placeName><settlement type="city">Groningue</settlement><region nuts="2" type="province">Groningue (province)</region></placeName></affiliation></author><author><name sortKey="Kriegenburg, Franziska" sort="Kriegenburg, Franziska" uniqKey="Kriegenburg F" first="Franziska" last="Kriegenburg">Franziska Kriegenburg</name><affiliation wicri:level="3"><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><placeName><settlement type="city">Groningue</settlement><region nuts="2" type="province">Groningue (province)</region></placeName></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="4"><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><placeName><settlement type="city">Utrecht</settlement><region nuts="2" type="province">Utrecht (province)</region></placeName><orgName type="university">Université d'Utrecht</orgName></affiliation></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name><affiliation wicri:level="3"><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><placeName><settlement type="city">Groningue</settlement><region nuts="2" type="province">Groningue (province)</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28720894</idno><idno type="pmid">28720894</idno><idno type="doi">10.1038/s41598-017-06062-w</idno><idno type="wicri:Area/PubMed/Corpus">000A98</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A98</idno><idno type="wicri:Area/PubMed/Curation">000A98</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000A98</idno><idno type="wicri:Area/PubMed/Checkpoint">000B44</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000B44</idno><idno type="wicri:Area/Ncbi/Merge">002E30</idno><idno type="wicri:Area/Ncbi/Curation">002E30</idno><idno type="wicri:Area/Ncbi/Checkpoint">002E30</idno><idno type="wicri:Area/Main/Merge">000E62</idno><idno type="wicri:Area/Main/Curation">000E60</idno><idno type="wicri:Area/Main/Exploration">000E60</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.</title><author><name sortKey="Cong, Yingying" sort="Cong, Yingying" uniqKey="Cong Y" first="Yingying" last="Cong">Yingying Cong</name><affiliation wicri:level="3"><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><placeName><settlement type="city">Groningue</settlement><region nuts="2" type="province">Groningue (province)</region></placeName></affiliation></author><author><name sortKey="Kriegenburg, Franziska" sort="Kriegenburg, Franziska" uniqKey="Kriegenburg F" first="Franziska" last="Kriegenburg">Franziska Kriegenburg</name><affiliation wicri:level="3"><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><placeName><settlement type="city">Groningue</settlement><region nuts="2" type="province">Groningue (province)</region></placeName></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="4"><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><placeName><settlement type="city">Utrecht</settlement><region nuts="2" type="province">Utrecht (province)</region></placeName><orgName type="university">Université d'Utrecht</orgName></affiliation></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name><affiliation wicri:level="3"><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><placeName><settlement type="city">Groningue</settlement><region nuts="2" type="province">Groningue (province)</region></placeName></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><affiliations><list><country><li>Pays-Bas</li></country><region><li>Groningue (province)</li><li>Utrecht (province)</li></region><settlement><li>Groningue</li><li>Utrecht</li></settlement><orgName><li>Université d'Utrecht</li></orgName></list><tree><country name="Pays-Bas"><region name="Groningue (province)"><name sortKey="Cong, Yingying" sort="Cong, Yingying" uniqKey="Cong Y" first="Yingying" last="Cong">Yingying Cong</name></region><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><name sortKey="Kriegenburg, Franziska" sort="Kriegenburg, Franziska" uniqKey="Kriegenburg F" first="Franziska" last="Kriegenburg">Franziska Kriegenburg</name><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000E60 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000E60 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:28720894
|texte= Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:28720894" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |