Recognition of the Murine Coronavirus Genomic RNA Packaging Signal Depends on the Second RNA-Binding Domain of the Nucleocapsid Protein
Identifieur interne : 001588 ( Main/Exploration ); précédent : 001587; suivant : 001589Recognition of the Murine Coronavirus Genomic RNA Packaging Signal Depends on the Second RNA-Binding Domain of the Nucleocapsid Protein
Auteurs : Lili Kuo ; Cheri A. Koetzner ; Kelley R. Hurst ; Paul S. MastersSource :
- Journal of Virology [ 0022-538X ] ; 2014.
Descripteurs français
- KwdFr :
- ARN viral (génétique), ARN viral (métabolisme), Animaux, Assemblage viral, Génome viral, Infections à Coronaviridae (médecine vétérinaire), Infections à Coronaviridae (virologie), Liaison aux protéines, Lignée cellulaire, Maladies des rongeurs (virologie), Protéines nucléocapside (), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Souris, Structure tertiaire des protéines, Virus de l'hépatite murine (), Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (physiologie).
- MESH :
- génétique : ARN viral, Protéines nucléocapside, Virus de l'hépatite murine.
- médecine vétérinaire : Infections à Coronaviridae.
- métabolisme : ARN viral, Protéines nucléocapside.
- physiologie : Virus de l'hépatite murine.
- virologie : Infections à Coronaviridae, Maladies des rongeurs.
- Animaux, Assemblage viral, Génome viral, Liaison aux protéines, Lignée cellulaire, Protéines nucléocapside, Souris, Structure tertiaire des protéines, Virus de l'hépatite murine.
English descriptors
- KwdEn :
- Animals, Cell Line, Coronaviridae Infections (veterinary), Coronaviridae Infections (virology), Genome, Viral, Mice, Murine hepatitis virus (chemistry), Murine hepatitis virus (genetics), Murine hepatitis virus (physiology), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Binding, Protein Structure, Tertiary, RNA, Viral (genetics), RNA, Viral (metabolism), Rodent Diseases (virology), Virus Assembly.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Murine hepatitis virus.
- genetics : Murine hepatitis virus, Nucleocapsid Proteins, RNA, Viral.
- chemical , metabolism : Nucleocapsid Proteins, RNA, Viral.
- physiology : Murine hepatitis virus.
- veterinary : Coronaviridae Infections.
- virology : Coronaviridae Infections, Rodent Diseases.
- Animals, Cell Line, Genome, Viral, Mice, Protein Binding, Protein Structure, Tertiary, Virus Assembly.
Abstract
The coronavirus nucleocapsid (N) protein forms a helical ribonucleoprotein with the viral positive-strand RNA genome and binds to the principal constituent of the virion envelope, the membrane (M) protein, to facilitate assembly and budding. Besides these structural roles, N protein associates with a component of the replicase-transcriptase complex, nonstructural protein 3, at a critical early stage of infection. N protein has also been proposed to participate in the replication and selective packaging of genomic RNA and the transcription and translation of subgenomic mRNA. Coronavirus N proteins contain two structurally distinct RNA-binding domains, an unusual characteristic among RNA viruses. To probe the functions of these domains in the N protein of the model coronavirus mouse hepatitis virus (MHV), we constructed mutants in which each RNA-binding domain was replaced by its counterpart from the N protein of severe acute respiratory syndrome coronavirus (SARS-CoV). Mapping of revertants of the resulting chimeric viruses provided evidence for extensive intramolecular interactions between the two RNA-binding domains. Through analysis of viral RNA that was packaged into virions we identified the second of the two RNA-binding domains as a principal determinant of MHV packaging signal recognition. As expected, the interaction of N protein with M protein was not affected in either of the chimeric viruses. Moreover, the SARS-CoV N substitutions did not alter the fidelity of leader-body junction formation during subgenomic mRNA synthesis. These results more clearly delineate the functions of N protein and establish a basis for further exploration of the mechanism of genomic RNA packaging.
Url:
DOI: 10.1128/JVI.03866-13
PubMed: 24501403
PubMed Central: 3993769
Affiliations:
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Le document en format XML
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Masters</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24501403</idno><idno type="pmc">3993769</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3993769</idno><idno type="RBID">PMC:3993769</idno><idno type="doi">10.1128/JVI.03866-13</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000C82</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000C82</idno><idno type="wicri:Area/Pmc/Curation">000C82</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000C82</idno><idno type="wicri:Area/Pmc/Checkpoint">000861</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000861</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:24501403</idno><idno type="wicri:Area/PubMed/Corpus">001054</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001054</idno><idno type="wicri:Area/PubMed/Curation">001054</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001054</idno><idno type="wicri:Area/PubMed/Checkpoint">000F43</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000F43</idno><idno type="wicri:Area/Ncbi/Merge">002824</idno><idno type="wicri:Area/Ncbi/Curation">002824</idno><idno type="wicri:Area/Ncbi/Checkpoint">002824</idno><idno type="wicri:doubleKey">0022-538X:2014:Kuo L:recognition:of:the</idno><idno type="wicri:Area/Main/Merge">001592</idno><idno type="wicri:Area/Main/Curation">001588</idno><idno type="wicri:Area/Main/Exploration">001588</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Recognition of the Murine Coronavirus Genomic RNA Packaging Signal Depends on the Second RNA-Binding Domain of the Nucleocapsid Protein</title><author><name sortKey="Kuo, Lili" sort="Kuo, Lili" uniqKey="Kuo L" first="Lili" last="Kuo">Lili Kuo</name></author><author><name sortKey="Koetzner, Cheri A" sort="Koetzner, Cheri A" uniqKey="Koetzner C" first="Cheri A." last="Koetzner">Cheri A. Koetzner</name></author><author><name sortKey="Hurst, Kelley R" sort="Hurst, Kelley R" uniqKey="Hurst K" first="Kelley R." last="Hurst">Kelley R. Hurst</name></author><author><name sortKey="Masters, Paul S" sort="Masters, Paul S" uniqKey="Masters P" first="Paul S." last="Masters">Paul S. Masters</name></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Coronaviridae Infections (veterinary)</term><term>Coronaviridae Infections (virology)</term><term>Genome, Viral</term><term>Mice</term><term>Murine hepatitis virus (chemistry)</term><term>Murine hepatitis virus (genetics)</term><term>Murine hepatitis virus (physiology)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>RNA, Viral (genetics)</term><term>RNA, Viral (metabolism)</term><term>Rodent Diseases (virology)</term><term>Virus Assembly</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (génétique)</term><term>ARN viral (métabolisme)</term><term>Animaux</term><term>Assemblage viral</term><term>Génome viral</term><term>Infections à Coronaviridae (médecine vétérinaire)</term><term>Infections à Coronaviridae (virologie)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Maladies des rongeurs (virologie)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (métabolisme)</term><term>Souris</term><term>Structure tertiaire des protéines</term><term>Virus de l'hépatite murine ()</term><term>Virus de l'hépatite murine (génétique)</term><term>Virus de l'hépatite murine (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term><term>Nucleocapsid Proteins</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN viral</term><term>Protéines nucléocapside</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" qualifier="médecine vétérinaire" xml:lang="fr"><term>Infections à Coronaviridae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="veterinary" xml:lang="en"><term>Coronaviridae Infections</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à Coronaviridae</term><term>Maladies des rongeurs</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronaviridae Infections</term><term>Rodent Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Genome, Viral</term><term>Mice</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Assemblage viral</term><term>Génome viral</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines nucléocapside</term><term>Souris</term><term>Structure tertiaire des protéines</term><term>Virus de l'hépatite murine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>ABSTRACT</title><p>The coronavirus nucleocapsid (N) protein forms a helical ribonucleoprotein with the viral positive-strand RNA genome and binds to the principal constituent of the virion envelope, the membrane (M) protein, to facilitate assembly and budding. Besides these structural roles, N protein associates with a component of the replicase-transcriptase complex, nonstructural protein 3, at a critical early stage of infection. N protein has also been proposed to participate in the replication and selective packaging of genomic RNA and the transcription and translation of subgenomic mRNA. Coronavirus N proteins contain two structurally distinct RNA-binding domains, an unusual characteristic among RNA viruses. To probe the functions of these domains in the N protein of the model coronavirus mouse hepatitis virus (MHV), we constructed mutants in which each RNA-binding domain was replaced by its counterpart from the N protein of severe acute respiratory syndrome coronavirus (SARS-CoV). Mapping of revertants of the resulting chimeric viruses provided evidence for extensive intramolecular interactions between the two RNA-binding domains. Through analysis of viral RNA that was packaged into virions we identified the second of the two RNA-binding domains as a principal determinant of MHV packaging signal recognition. As expected, the interaction of N protein with M protein was not affected in either of the chimeric viruses. Moreover, the SARS-CoV N substitutions did not alter the fidelity of leader-body junction formation during subgenomic mRNA synthesis. These results more clearly delineate the functions of N protein and establish a basis for further exploration of the mechanism of genomic RNA packaging.</p><p><bold>IMPORTANCE</bold> This work describes the interactions of the two RNA-binding domains of the nucleocapsid protein of a model coronavirus, mouse hepatitis virus. The main finding is that the second of the two domains plays an essential role in recognizing the RNA structure that allows the selective packaging of genomic RNA into assembled virions.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Hurst, Kelley R" sort="Hurst, Kelley R" uniqKey="Hurst K" first="Kelley R." last="Hurst">Kelley R. Hurst</name><name sortKey="Koetzner, Cheri A" sort="Koetzner, Cheri A" uniqKey="Koetzner C" first="Cheri A." last="Koetzner">Cheri A. Koetzner</name><name sortKey="Kuo, Lili" sort="Kuo, Lili" uniqKey="Kuo L" first="Lili" last="Kuo">Lili Kuo</name><name sortKey="Masters, Paul S" sort="Masters, Paul S" uniqKey="Masters P" first="Paul S." last="Masters">Paul S. Masters</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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