Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
Identifieur interne : 000024 ( Istex/Corpus ); précédent : 000023; suivant : 000025Non-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 ] ; 2007-05-01.
Abstract
Summary.: We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 °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 °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.
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DOI: 10.1007/s00705-006-0911-z
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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 °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><istex><corpusName>springer-journals</corpusName><author><json:item><name>E. N. Prokudina</name><affiliations><json:string>The D.I. Ivanovsky Institute of Virology, Moscow, Russia</json:string></affiliations></json:item><json:item><name>N. P. Semenova</name><affiliations><json:string>The D.I. Ivanovsky Institute of Virology, Moscow, Russia</json:string></affiliations></json:item><json:item><name>V. M. Chumakov</name><affiliations><json:string>The D.I. 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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 °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. 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N.</GivenName><FamilyName>Prokudina</FamilyName></AuthorName></Author><Author AffiliationIDS="A1"><AuthorName DisplayOrder="Western"><GivenName>N. P.</GivenName><FamilyName>Semenova</FamilyName></AuthorName></Author><Author AffiliationIDS="A1"><AuthorName DisplayOrder="Western"><GivenName>V. M.</GivenName><FamilyName>Chumakov</FamilyName></AuthorName></Author><Author AffiliationIDS="A1"><AuthorName DisplayOrder="Western"><GivenName>T. A.</GivenName><FamilyName>Grigorieva</FamilyName></AuthorName></Author><Affiliation ID="A1"><OrgName>The D.I. Ivanovsky Institute of Virology</OrgName><OrgAddress><City>Moscow</City><Country Code="RU">Russia</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary.</Heading><Para TextBreak="No">We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 °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 °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.</Para><Para TextBreak="No">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.</Para><Para TextBreak="No">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.</Para></Abstract></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Non-compact nucleocapsid protein multimers in influenza-virus-infected cells</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Non-compact nucleocapsid protein multimers in influenza-virus-infected cells</title></titleInfo><name type="personal"><namePart type="given">E. N.</namePart><namePart type="family">Prokudina</namePart><affiliation>The D.I. Ivanovsky Institute of Virology, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N. P.</namePart><namePart type="family">Semenova</namePart><affiliation>The D.I. Ivanovsky Institute of Virology, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V. M.</namePart><namePart type="family">Chumakov</namePart><affiliation>The D.I. Ivanovsky Institute of Virology, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">T. A.</namePart><namePart type="family">Grigorieva</namePart><affiliation>The D.I. Ivanovsky Institute of Virology, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Springer-Verlag</publisher><place><placeTerm type="text">Vienna</placeTerm></place><dateCreated encoding="w3cdtf">2006-08-28</dateCreated><dateIssued encoding="w3cdtf">2007-05-01</dateIssued><copyrightDate encoding="w3cdtf">2007</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary.: We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 °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 °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.</abstract><relatedItem type="host"><titleInfo><title>Archives of Virology</title><subTitle>Official Journal of the Virology Division of the International Union of Microbiological Societies</subTitle></titleInfo><titleInfo type="abbreviated"><title>Arch Virol</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2007-05-01</dateIssued><copyrightDate encoding="w3cdtf">2007</copyrightDate></originInfo><subject><genre>Journal-Subject-Group</genre><topic authority="SpringerSubjectCodes" authorityURI="B">Biomedicine</topic><topic authority="SpringerSubjectCodes" authorityURI="B22003">Virology</topic><topic authority="SpringerSubjectCodes" authorityURI="B16003">Medical Microbiology</topic><topic authority="SpringerSubjectCodes" authorityURI="H33096">Infectious Diseases</topic></subject><identifier type="ISSN">0304-8608</identifier><identifier type="eISSN">1432-8798</identifier><identifier type="JournalID">705</identifier><identifier type="JournalSPIN">30024806</identifier><identifier type="IssueArticleCount">20</identifier><identifier type="VolumeIssueCount">12</identifier><part><date>2007</date><detail type="volume"><number>152</number><caption>vol.</caption></detail><detail type="issue"><number>5</number><caption>no.</caption></detail><extent unit="pages"><start>981</start><end>988</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 2007</recordOrigin></recordInfo></relatedItem><identifier type="istex">89B4468C27F81A38833BE74638CA24D6CC5C0773</identifier><identifier type="ark">ark:/67375/VQC-Q7K5HJVL-Q</identifier><identifier type="DOI">10.1007/s00705-006-0911-z</identifier><identifier type="ArticleID">911</identifier><identifier type="ArticleID">Art1</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 2007</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag, 2007</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-Q7K5HJVL-Q/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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