Non-compact nucleocapsid protein multimers in influenza-virus-infected cells.
Identifieur interne : 000289 ( PubMed/Corpus ); précédent : 000288; suivant : 000290Non-compact nucleocapsid protein multimers in influenza-virus-infected cells.
Auteurs : E N Prokudina ; N P Semenova ; V M Chumakov ; T A GrigorievaSource :
- Archives of virology [ 0304-8608 ] ; 2007.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Viral (immunology), Antibody Affinity, Cell Line, Dogs, Electrophoresis, Polyacrylamide Gel, Influenza A Virus, H2N2 Subtype (immunology), Influenza A Virus, H3N2 Subtype (immunology), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (immunology), Nucleocapsid Proteins (metabolism), Orthomyxoviridae Infections (virology), Protein Conformation.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Nucleocapsid Proteins.
- immunology : Influenza A Virus, H2N2 Subtype, Influenza A Virus, H3N2 Subtype.
- chemical , metabolism : Nucleocapsid Proteins.
- virology : Orthomyxoviridae Infections.
- Animals, Antibody Affinity, Cell Line, Dogs, Electrophoresis, Polyacrylamide Gel, Protein Conformation.
Abstract
We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 degrees C and possessing properties of folded proteins, are post-translationally formed in influenza-virus-infected cells. In this study we demonstrate that, in addition to compact NP oligomers, incompletely folded NP multimers are detected intracellularly by SDS/PAGE carried out under weak dissociating conditions. In cells infected with avian, human A(H2N2), and human A(H3N2) viruses, NP multimers are detected in the stacking gel of SDS/PAGE as retarded and loose structures dissociating at +50 degrees C. NP multimers are more sensitive to proteolysis than NP oligomers, but they are more resistant to proteolysis than NP monomers. In contrast to compact NP oligomers, NP multimers possess a weak immunoreactivity to some monoclonal antibodies. Pulse-chase experiments have shown that NP multimers appear at early stages of NP synthesis and are partially converted post-translationally into faster-migrating compact NP oligomers. In the course of infection, the excess NP multimers not converted into compact NP oligomers accumulate in cells and degrade. Under weak dissociating conditions, intracellular NP multimers are relatively stable in avian, human A(H2N2) and human A(H3N2) viruses and unstable in human A(H1N1) viruses, dissociating into monomers. NP multimers presumably serve to bring nascent unfolded NP molecules into close contact with each other for further oligomerization, to protect NP monomers from proteolysis, and to serve as intermediates in the posttranslational folding of NP.
DOI: 10.1007/s00705-006-0911-z
PubMed: 17216139
Links to Exploration step
pubmed:17216139Le document en format XML
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Ivanovsky Institute of Virology, Moscow, Russia. prokudinaen@mail.ru</nlm:affiliation></affiliation></author><author><name sortKey="Semenova, N P" sort="Semenova, N P" uniqKey="Semenova N" first="N P" last="Semenova">N P Semenova</name></author><author><name sortKey="Chumakov, V M" sort="Chumakov, V M" uniqKey="Chumakov V" first="V M" last="Chumakov">V M Chumakov</name></author><author><name sortKey="Grigorieva, T A" sort="Grigorieva, T A" uniqKey="Grigorieva T" first="T A" last="Grigorieva">T A Grigorieva</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17216139</idno><idno type="pmid">17216139</idno><idno type="doi">10.1007/s00705-006-0911-z</idno><idno type="wicri:Area/PubMed/Corpus">000289</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000289</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Non-compact nucleocapsid protein multimers in influenza-virus-infected cells.</title><author><name sortKey="Prokudina, E N" sort="Prokudina, E N" uniqKey="Prokudina E" first="E N" last="Prokudina">E N Prokudina</name><affiliation><nlm:affiliation>The D.I. Ivanovsky Institute of Virology, Moscow, Russia. prokudinaen@mail.ru</nlm:affiliation></affiliation></author><author><name sortKey="Semenova, N P" sort="Semenova, N P" uniqKey="Semenova N" first="N P" last="Semenova">N P Semenova</name></author><author><name sortKey="Chumakov, V M" sort="Chumakov, V M" uniqKey="Chumakov V" first="V M" last="Chumakov">V M Chumakov</name></author><author><name sortKey="Grigorieva, T A" sort="Grigorieva, T A" uniqKey="Grigorieva T" first="T A" last="Grigorieva">T A Grigorieva</name></author></analytic><series><title level="j">Archives of virology</title><idno type="ISSN">0304-8608</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Viral (immunology)</term><term>Antibody Affinity</term><term>Cell Line</term><term>Dogs</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Influenza A Virus, H2N2 Subtype (immunology)</term><term>Influenza A Virus, H3N2 Subtype (immunology)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (immunology)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Orthomyxoviridae Infections (virology)</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A Virus, H2N2 Subtype</term><term>Influenza A Virus, H3N2 Subtype</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Antibody Affinity</term><term>Cell Line</term><term>Dogs</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Protein Conformation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 degrees C and possessing properties of folded proteins, are post-translationally formed in influenza-virus-infected cells. In this study we demonstrate that, in addition to compact NP oligomers, incompletely folded NP multimers are detected intracellularly by SDS/PAGE carried out under weak dissociating conditions. In cells infected with avian, human A(H2N2), and human A(H3N2) viruses, NP multimers are detected in the stacking gel of SDS/PAGE as retarded and loose structures dissociating at +50 degrees C. NP multimers are more sensitive to proteolysis than NP oligomers, but they are more resistant to proteolysis than NP monomers. In contrast to compact NP oligomers, NP multimers possess a weak immunoreactivity to some monoclonal antibodies. Pulse-chase experiments have shown that NP multimers appear at early stages of NP synthesis and are partially converted post-translationally into faster-migrating compact NP oligomers. In the course of infection, the excess NP multimers not converted into compact NP oligomers accumulate in cells and degrade. Under weak dissociating conditions, intracellular NP multimers are relatively stable in avian, human A(H2N2) and human A(H3N2) viruses and unstable in human A(H1N1) viruses, dissociating into monomers. NP multimers presumably serve to bring nascent unfolded NP molecules into close contact with each other for further oligomerization, to protect NP monomers from proteolysis, and to serve as intermediates in the posttranslational folding of NP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17216139</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2007</Year><Month>10</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0304-8608</ISSN><JournalIssue CitedMedium="Print"><Volume>152</Volume><Issue>5</Issue><PubDate><Year>2007</Year></PubDate></JournalIssue><Title>Archives of virology</Title><ISOAbbreviation>Arch. Virol.</ISOAbbreviation></Journal><ArticleTitle>Non-compact nucleocapsid protein multimers in influenza-virus-infected cells.</ArticleTitle><Pagination><MedlinePgn>981-8</MedlinePgn></Pagination><Abstract><AbstractText>We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 degrees C and possessing properties of folded proteins, are post-translationally formed in influenza-virus-infected cells. In this study we demonstrate that, in addition to compact NP oligomers, incompletely folded NP multimers are detected intracellularly by SDS/PAGE carried out under weak dissociating conditions. In cells infected with avian, human A(H2N2), and human A(H3N2) viruses, NP multimers are detected in the stacking gel of SDS/PAGE as retarded and loose structures dissociating at +50 degrees C. NP multimers are more sensitive to proteolysis than NP oligomers, but they are more resistant to proteolysis than NP monomers. In contrast to compact NP oligomers, NP multimers possess a weak immunoreactivity to some monoclonal antibodies. Pulse-chase experiments have shown that NP multimers appear at early stages of NP synthesis and are partially converted post-translationally into faster-migrating compact NP oligomers. In the course of infection, the excess NP multimers not converted into compact NP oligomers accumulate in cells and degrade. Under weak dissociating conditions, intracellular NP multimers are relatively stable in avian, human A(H2N2) and human A(H3N2) viruses and unstable in human A(H1N1) viruses, dissociating into monomers. NP multimers presumably serve to bring nascent unfolded NP molecules into close contact with each other for further oligomerization, to protect NP monomers from proteolysis, and to serve as intermediates in the posttranslational folding of NP.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Prokudina</LastName><ForeName>E N</ForeName><Initials>EN</Initials><AffiliationInfo><Affiliation>The D.I. Ivanovsky Institute of Virology, Moscow, Russia. prokudinaen@mail.ru</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Semenova</LastName><ForeName>N P</ForeName><Initials>NP</Initials></Author><Author ValidYN="Y"><LastName>Chumakov</LastName><ForeName>V M</ForeName><Initials>VM</Initials></Author><Author ValidYN="Y"><LastName>Grigorieva</LastName><ForeName>T A</ForeName><Initials>TA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>01</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>Austria</Country><MedlineTA>Arch Virol</MedlineTA><NlmUniqueID>7506870</NlmUniqueID><ISSNLinking>0304-8608</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000915" MajorTopicYN="N">Antibody Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004285" MajorTopicYN="N">Dogs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053121" MajorTopicYN="N">Influenza A Virus, H2N2 Subtype</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053122" MajorTopicYN="N">Influenza A Virus, H3N2 Subtype</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009976" MajorTopicYN="N">Orthomyxoviridae Infections</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>08</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>11</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>1</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>1</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17216139</ArticleId><ArticleId IdType="doi">10.1007/s00705-006-0911-z</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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