Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus.
Identifieur interne : 002D95 ( PubMed/Checkpoint ); précédent : 002D94; suivant : 002D96Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus.
Auteurs : Runtao He [Canada] ; Andrew Leeson ; Melissa Ballantine ; Anton Andonov ; Lindsay Baker ; Frederick Dobie ; Yan Li ; Nathalie Bastien ; Heinz Feldmann ; Ute Strocher ; Steven Theriault ; Todd Cutts ; Jingxin Cao ; Timothy F. Booth ; Frank A. Plummer ; Shaun Tyler ; Xuguang LiSource :
- Virus research [ 0168-1702 ] ; 2004.
Descripteurs français
- KwdFr :
- Assemblage viral, Cartographie d'interactions entre protéines, Conformation des protéines, Délétion de séquence, Liaison aux protéines, Protéines de la matrice virale (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Protéines virales (métabolisme), Sites de fixation, Techniques de double hybride, Virus du SRAS (métabolisme), Virus du SRAS (physiologie).
- MESH :
- métabolisme : Protéines de la matrice virale, Protéines nucléocapside, Protéines virales, Virus du SRAS.
- physiologie : Virus du SRAS.
- Assemblage viral, Cartographie d'interactions entre protéines, Conformation des protéines, Délétion de séquence, Liaison aux protéines, Protéines nucléocapside, Sites de fixation, Techniques de double hybride.
English descriptors
- KwdEn :
- Binding Sites, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Binding, Protein Conformation, Protein Interaction Mapping, SARS Virus (metabolism), SARS Virus (physiology), Sequence Deletion, Two-Hybrid System Techniques, Viral Matrix Proteins (metabolism), Viral Proteins (metabolism), Virus Assembly.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemical , metabolism : Nucleocapsid Proteins, Viral Matrix Proteins, Viral Proteins.
- metabolism : SARS Virus.
- physiology : SARS Virus.
- Binding Sites, Protein Binding, Protein Conformation, Protein Interaction Mapping, Sequence Deletion, Two-Hybrid System Techniques, Virus Assembly.
Abstract
The human coronavirus, associated with severe acute respiratory syndrome (SARS-CoV), was identified and molecularly characterized in 2003. Sequence analysis of the virus indicates that there is only 20% amino acid (aa) identity with known coronaviruses. Previous studies indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly. Yet, little sequence homology between the newly identified SARS-CoV and those previously studied coronaviruses suggests that determination of protein-protein interaction and identification of amino acid sequences, responsible for such interaction in SARS-CoV, are necessary for the elucidation of the molecular mechanism of SARS-CoV replication and rationalization of anti-SARS therapeutic intervention. In this study, we employed mammalian two-hybrid system to investigate possible interactions between SARS-CoV nucleocapsid (N) and the membrane (M) proteins. We found that interaction of the N and M proteins takes place in vivo and identified that a stretch of amino acids (168-208) in the N protein may be critical for such protein-protein interactions. Importantly, the same region has been found to be required for multimerization of the N protein (He et al., 2004) suggesting this region may be crucial in maintaining correct conformation of the N protein for self-interaction and interaction with the M protein.
DOI: 10.1016/j.virusres.2004.05.002
PubMed: 15351485
Affiliations:
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Booth</name></author><author><name sortKey="Plummer, Frank A" sort="Plummer, Frank A" uniqKey="Plummer F" first="Frank A" last="Plummer">Frank A. Plummer</name></author><author><name sortKey="Tyler, Shaun" sort="Tyler, Shaun" uniqKey="Tyler S" first="Shaun" last="Tyler">Shaun Tyler</name></author><author><name sortKey="Li, Xuguang" sort="Li, Xuguang" uniqKey="Li X" first="Xuguang" last="Li">Xuguang Li</name></author></analytic><series><title level="j">Virus research</title><idno type="ISSN">0168-1702</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Interaction Mapping</term><term>SARS Virus (metabolism)</term><term>SARS Virus (physiology)</term><term>Sequence Deletion</term><term>Two-Hybrid System Techniques</term><term>Viral Matrix Proteins (metabolism)</term><term>Viral Proteins (metabolism)</term><term>Virus Assembly</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Assemblage viral</term><term>Cartographie d'interactions entre protéines</term><term>Conformation des protéines</term><term>Délétion de séquence</term><term>Liaison aux protéines</term><term>Protéines de la matrice virale (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (métabolisme)</term><term>Protéines virales (métabolisme)</term><term>Sites de fixation</term><term>Techniques de double hybride</term><term>Virus du SRAS (métabolisme)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Viral Matrix Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de la matrice virale</term><term>Protéines nucléocapside</term><term>Protéines virales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Interaction Mapping</term><term>Sequence Deletion</term><term>Two-Hybrid System Techniques</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Assemblage viral</term><term>Cartographie d'interactions entre protéines</term><term>Conformation des protéines</term><term>Délétion de séquence</term><term>Liaison aux protéines</term><term>Protéines nucléocapside</term><term>Sites de fixation</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The human coronavirus, associated with severe acute respiratory syndrome (SARS-CoV), was identified and molecularly characterized in 2003. Sequence analysis of the virus indicates that there is only 20% amino acid (aa) identity with known coronaviruses. Previous studies indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly. Yet, little sequence homology between the newly identified SARS-CoV and those previously studied coronaviruses suggests that determination of protein-protein interaction and identification of amino acid sequences, responsible for such interaction in SARS-CoV, are necessary for the elucidation of the molecular mechanism of SARS-CoV replication and rationalization of anti-SARS therapeutic intervention. In this study, we employed mammalian two-hybrid system to investigate possible interactions between SARS-CoV nucleocapsid (N) and the membrane (M) proteins. We found that interaction of the N and M proteins takes place in vivo and identified that a stretch of amino acids (168-208) in the N protein may be critical for such protein-protein interactions. Importantly, the same region has been found to be required for multimerization of the N protein (He et al., 2004) suggesting this region may be crucial in maintaining correct conformation of the N protein for self-interaction and interaction with the M protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15351485</PMID><DateCompleted><Year>2005</Year><Month>03</Month><Day>11</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0168-1702</ISSN><JournalIssue CitedMedium="Print"><Volume>105</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus.</ArticleTitle><Pagination><MedlinePgn>121-5</MedlinePgn></Pagination><Abstract><AbstractText>The human coronavirus, associated with severe acute respiratory syndrome (SARS-CoV), was identified and molecularly characterized in 2003. Sequence analysis of the virus indicates that there is only 20% amino acid (aa) identity with known coronaviruses. Previous studies indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly. Yet, little sequence homology between the newly identified SARS-CoV and those previously studied coronaviruses suggests that determination of protein-protein interaction and identification of amino acid sequences, responsible for such interaction in SARS-CoV, are necessary for the elucidation of the molecular mechanism of SARS-CoV replication and rationalization of anti-SARS therapeutic intervention. In this study, we employed mammalian two-hybrid system to investigate possible interactions between SARS-CoV nucleocapsid (N) and the membrane (M) proteins. We found that interaction of the N and M proteins takes place in vivo and identified that a stretch of amino acids (168-208) in the N protein may be critical for such protein-protein interactions. Importantly, the same region has been found to be required for multimerization of the N protein (He et al., 2004) suggesting this region may be crucial in maintaining correct conformation of the N protein for self-interaction and interaction with the M protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>He</LastName><ForeName>Runtao</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>National Microbiology Laboratory, Health Canada, 1015 Arlington St., Winnipeg, Man., Canada R3E 3R2. runtao_he@hc-sc.gc.ca</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leeson</LastName><ForeName>Andrew</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Ballantine</LastName><ForeName>Melissa</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Andonov</LastName><ForeName>Anton</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Baker</LastName><ForeName>Lindsay</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Dobie</LastName><ForeName>Frederick</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Yan</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Bastien</LastName><ForeName>Nathalie</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Feldmann</LastName><ForeName>Heinz</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Strocher</LastName><ForeName>Ute</ForeName><Initials>U</Initials></Author><Author ValidYN="Y"><LastName>Theriault</LastName><ForeName>Steven</ForeName><Initials>S</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>Booth</LastName><ForeName>Timothy F</ForeName><Initials>TF</Initials></Author><Author ValidYN="Y"><LastName>Plummer</LastName><ForeName>Frank A</ForeName><Initials>FA</Initials></Author><Author ValidYN="Y"><LastName>Tyler</LastName><ForeName>Shaun</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xuguang</ForeName><Initials>X</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>108502-71-2</RegistryNumber><NameOfSubstance UI="C067997">M protein, Coronavirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025941" MajorTopicYN="N">Protein Interaction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017384" MajorTopicYN="N">Sequence Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014763" MajorTopicYN="N">Viral Matrix Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019065" MajorTopicYN="N">Virus Assembly</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>02</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>05</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>05</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>9</Month><Day>8</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>3</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>9</Month><Day>8</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId 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F. Booth</name><name sortKey="Cao, Jingxin" sort="Cao, Jingxin" uniqKey="Cao J" first="Jingxin" last="Cao">Jingxin Cao</name><name sortKey="Cutts, Todd" sort="Cutts, Todd" uniqKey="Cutts T" first="Todd" last="Cutts">Todd Cutts</name><name sortKey="Dobie, Frederick" sort="Dobie, Frederick" uniqKey="Dobie F" first="Frederick" last="Dobie">Frederick Dobie</name><name sortKey="Feldmann, Heinz" sort="Feldmann, Heinz" uniqKey="Feldmann H" first="Heinz" last="Feldmann">Heinz Feldmann</name><name sortKey="Leeson, Andrew" sort="Leeson, Andrew" uniqKey="Leeson A" first="Andrew" last="Leeson">Andrew Leeson</name><name sortKey="Li, Xuguang" sort="Li, Xuguang" uniqKey="Li X" first="Xuguang" last="Li">Xuguang Li</name><name sortKey="Li, Yan" sort="Li, Yan" uniqKey="Li Y" first="Yan" last="Li">Yan Li</name><name sortKey="Plummer, Frank A" sort="Plummer, Frank A" uniqKey="Plummer F" first="Frank A" last="Plummer">Frank A. Plummer</name><name sortKey="Strocher, Ute" sort="Strocher, Ute" uniqKey="Strocher U" first="Ute" last="Strocher">Ute Strocher</name><name sortKey="Theriault, Steven" sort="Theriault, Steven" uniqKey="Theriault S" first="Steven" last="Theriault">Steven Theriault</name><name sortKey="Tyler, Shaun" sort="Tyler, Shaun" uniqKey="Tyler S" first="Shaun" last="Tyler">Shaun Tyler</name></noCountry><country name="Canada"><noRegion><name sortKey="He, Runtao" sort="He, Runtao" uniqKey="He R" first="Runtao" last="He">Runtao He</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus.
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