The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.
Identifieur interne : 001926 ( PubMed/Corpus ); précédent : 001925; suivant : 001927The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.
Auteurs : Shaun Tylor ; Anton Andonov ; Todd Cutts ; Jingxin Cao ; Elsey Grudesky ; Gary Van Domselaar ; Xuguang Li ; Runtao HeSource :
- Canadian journal of microbiology [ 0008-4166 ] ; 2009.
English descriptors
- KwdEn :
- Amino Acid Motifs (genetics), Amino Acid Sequence, Animals, Arginine (chemistry), Chlorocebus aethiops, Humans, Molecular Sequence Data, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), SARS Virus (physiology), Serine (chemistry), Transfection, Vero Cells, Virus Replication.
- MESH :
- chemical , chemistry : Arginine, Nucleocapsid Proteins, Serine.
- genetics : Amino Acid Motifs, Nucleocapsid Proteins, SARS Virus.
- chemical , metabolism : Nucleocapsid Proteins, SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Humans, Molecular Sequence Data, Transfection, Vero Cells, Virus Replication.
Abstract
The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.
DOI: 10.1139/w08-139
PubMed: 19370068
Links to Exploration step
pubmed:19370068Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.</title><author><name sortKey="Tylor, Shaun" sort="Tylor, Shaun" uniqKey="Tylor S" first="Shaun" last="Tylor">Shaun Tylor</name><affiliation><nlm:affiliation>National Microbiology Laboratory, Health Canada, 1015 Arlington St, Winnipeg, MB R3E3R2, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name></author><author><name sortKey="Cutts, Todd" sort="Cutts, Todd" uniqKey="Cutts T" first="Todd" last="Cutts">Todd Cutts</name></author><author><name sortKey="Cao, Jingxin" sort="Cao, Jingxin" uniqKey="Cao J" first="Jingxin" last="Cao">Jingxin Cao</name></author><author><name sortKey="Grudesky, Elsey" sort="Grudesky, Elsey" uniqKey="Grudesky E" first="Elsey" last="Grudesky">Elsey Grudesky</name></author><author><name sortKey="Van Domselaar, Gary" sort="Van Domselaar, Gary" uniqKey="Van Domselaar G" first="Gary" last="Van Domselaar">Gary Van Domselaar</name></author><author><name sortKey="Li, Xuguang" sort="Li, Xuguang" uniqKey="Li X" first="Xuguang" last="Li">Xuguang Li</name></author><author><name sortKey="He, Runtao" sort="He, Runtao" uniqKey="He R" first="Runtao" last="He">Runtao He</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19370068</idno><idno type="pmid">19370068</idno><idno type="doi">10.1139/w08-139</idno><idno type="wicri:Area/PubMed/Corpus">001926</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001926</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.</title><author><name sortKey="Tylor, Shaun" sort="Tylor, Shaun" uniqKey="Tylor S" first="Shaun" last="Tylor">Shaun Tylor</name><affiliation><nlm:affiliation>National Microbiology Laboratory, Health Canada, 1015 Arlington St, Winnipeg, MB R3E3R2, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name></author><author><name sortKey="Cutts, Todd" sort="Cutts, Todd" uniqKey="Cutts T" first="Todd" last="Cutts">Todd Cutts</name></author><author><name sortKey="Cao, Jingxin" sort="Cao, Jingxin" uniqKey="Cao J" first="Jingxin" last="Cao">Jingxin Cao</name></author><author><name sortKey="Grudesky, Elsey" sort="Grudesky, Elsey" uniqKey="Grudesky E" first="Elsey" last="Grudesky">Elsey Grudesky</name></author><author><name sortKey="Van Domselaar, Gary" sort="Van Domselaar, Gary" uniqKey="Van Domselaar G" first="Gary" last="Van Domselaar">Gary Van Domselaar</name></author><author><name sortKey="Li, Xuguang" sort="Li, Xuguang" uniqKey="Li X" first="Xuguang" last="Li">Xuguang Li</name></author><author><name sortKey="He, Runtao" sort="He, Runtao" uniqKey="He R" first="Runtao" last="He">Runtao He</name></author></analytic><series><title level="j">Canadian journal of microbiology</title><idno type="ISSN">0008-4166</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (genetics)</term><term>Amino Acid Sequence</term><term>Animals</term><term>Arginine (chemistry)</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Molecular Sequence Data</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (physiology)</term><term>Serine (chemistry)</term><term>Transfection</term><term>Vero Cells</term><term>Virus Replication</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arginine</term><term>Nucleocapsid Proteins</term><term>Serine</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Motifs</term><term>Nucleocapsid Proteins</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Molecular Sequence Data</term><term>Transfection</term><term>Vero Cells</term><term>Virus Replication</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19370068</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0008-4166</ISSN><JournalIssue CitedMedium="Print"><Volume>55</Volume><Issue>3</Issue><PubDate><Year>2009</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Canadian journal of microbiology</Title><ISOAbbreviation>Can. J. Microbiol.</ISOAbbreviation></Journal><ArticleTitle>The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.</ArticleTitle><Pagination><MedlinePgn>254-60</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1139/w08-139</ELocationID><Abstract><AbstractText>The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tylor</LastName><ForeName>Shaun</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>National Microbiology Laboratory, Health Canada, 1015 Arlington St, Winnipeg, MB R3E3R2, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Andonov</LastName><ForeName>Anton</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Cutts</LastName><ForeName>Todd</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Cao</LastName><ForeName>Jingxin</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Grudesky</LastName><ForeName>Elsey</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Van Domselaar</LastName><ForeName>Gary</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xuguang</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>He</LastName><ForeName>Runtao</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Canada</Country><MedlineTA>Can J Microbiol</MedlineTA><NlmUniqueID>0372707</NlmUniqueID><ISSNLinking>0008-4166</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>452VLY9402</RegistryNumber><NameOfSubstance UI="D012694">Serine</NameOfSubstance></Chemical><Chemical><RegistryNumber>94ZLA3W45F</RegistryNumber><NameOfSubstance UI="D001120">Arginine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="Y">Amino Acid Motifs</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001120" MajorTopicYN="N">Arginine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012694" MajorTopicYN="N">Serine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="Y">Virus Replication</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>4</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>4</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>7</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19370068</ArticleId><ArticleId IdType="pii">w08-139</ArticleId><ArticleId IdType="doi">10.1139/w08-139</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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