Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin.
Identifieur interne : 000201 ( Hal/Checkpoint ); précédent : 000200; suivant : 000202Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin.
Auteurs : Krister Melén [Finlande] ; Janne Tynell [Finlande] ; Riku Fagerlund [États-Unis] ; Pascal Roussel [France] ; Danièle Hernandez-Verdun [France] ; Ilkka Julkunen [Finlande]Source :
Abstract
UNLABELLED: ABSTRACT: BACKGROUND: Influenza A virus non-structural protein 1 (NS1) is a virulence factor, which is targeted into the cell cytoplasm, nucleus and nucleolus. NS1 is a multi-functional protein that inhibits host cell pre-mRNA processing and counteracts host cell antiviral responses. Previously, we have shown that the NS1 protein of the H3N2 subtype influenza viruses possesses a C-terminal nuclear localization signal (NLS) that also functions as a nucleolar localization signal (NoLS) and targets the protein into the nucleolus. RESULTS: Here, we show that the NS1 protein of the human H3N2 virus subtype interacts in vitro primarily via its C-terminal NLS2/NoLS and to a minor extent via its N-terminal NLS1 with the nucleolar proteins, nucleolin and fibrillarin. Using chimeric green fluorescence protein (GFP)-NS1 fusion constructs, we show that the nucleolar retention of the NS1 protein is determined by its C-terminal NLS2/NoLS in vivo. Confocal laser microscopy analysis shows that the NS1 protein colocalizes with nucleolin in nucleoplasm and nucleolus and with B23 and fibrillarin in the nucleolus of influenza A/Udorn/72 virus-infected A549 cells. Since some viral proteins contain NoLSs, it is likely that viruses have evolved specific nucleolar functions. CONCLUSION: NS1 protein of the human H3N2 virus interacts primarily via the C-terminal NLS2/NoLS and to a minor extent via the N-terminal NLS1 with the main nucleolar proteins, nucleolin, B23 and fibrillarin.
Url:
DOI: 10.1186/1743-422X-9-167
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Hal:hal-00764038Le document en format XML
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<front><div type="abstract" xml:lang="en"> <p>UNLABELLED: ABSTRACT: BACKGROUND: Influenza A virus non-structural protein 1 (NS1) is a virulence factor, which is targeted into the cell cytoplasm, nucleus and nucleolus. NS1 is a multi-functional protein that inhibits host cell pre-mRNA processing and counteracts host cell antiviral responses. Previously, we have shown that the NS1 protein of the H3N2 subtype influenza viruses possesses a C-terminal nuclear localization signal (NLS) that also functions as a nucleolar localization signal (NoLS) and targets the protein into the nucleolus. RESULTS: Here, we show that the NS1 protein of the human H3N2 virus subtype interacts in vitro primarily via its C-terminal NLS2/NoLS and to a minor extent via its N-terminal NLS1 with the nucleolar proteins, nucleolin and fibrillarin. Using chimeric green fluorescence protein (GFP)-NS1 fusion constructs, we show that the nucleolar retention of the NS1 protein is determined by its C-terminal NLS2/NoLS in vivo. Confocal laser microscopy analysis shows that the NS1 protein colocalizes with nucleolin in nucleoplasm and nucleolus and with B23 and fibrillarin in the nucleolus of influenza A/Udorn/72 virus-infected A549 cells. Since some viral proteins contain NoLSs, it is likely that viruses have evolved specific nucleolar functions. CONCLUSION: NS1 protein of the human H3N2 virus interacts primarily via the C-terminal NLS2/NoLS and to a minor extent via the N-terminal NLS1 with the main nucleolar proteins, nucleolin, B23 and fibrillarin.</p>
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<author role="aut"> <persName> <forename type="first">Danièle</forename>
<surname>Hernandez-Verdun</surname>
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</author>
<author role="aut"> <persName> <forename type="first">Ilkka</forename>
<surname>Julkunen</surname>
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<idno type="halauthorid">794957</idno>
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</author>
<editor role="depositor"> <persName> <forename>Martine</forename>
<surname>Bondidier</surname>
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<email type="md5">936cd32b8405a0c3eb8c6432ce90f978</email>
<email type="domain">ijm.fr</email>
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<date type="whenModified">2020-03-27 03:04:03</date>
<date type="whenReleased">2012-12-12 11:17:30</date>
<date type="whenProduced">2012</date>
<ref type="externalLink" target="https://virologyj.biomedcentral.com/track/pdf/10.1186/1743-422X-9-167"></ref>
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<name key="113036"> <persName> <forename>Martine</forename>
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<idno type="halRefHtml">Virol J, 2012, 9, pp.167. ⟨10.1186/1743-422X-9-167⟩</idno>
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<seriesStmt> <idno type="stamp" n="UNIV-PARIS7" corresp="UNIV-PARIS">Université Denis Diderot - Paris VII</idno>
<idno type="stamp" n="UPMC" corresp="SORBONNE-UNIVERSITE">Université Pierre et Marie Curie</idno>
<idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
<idno type="stamp" n="IJM">Institut Jacques Monod</idno>
<idno type="stamp" n="USPC">Université Sorbonne Paris Cité</idno>
<idno type="stamp" n="SORBONNE-UNIVERSITE">Sorbonne Université</idno>
<idno type="stamp" n="UNIV-PARIS">Université de Paris</idno>
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<sourceDesc> <biblStruct> <analytic> <title xml:lang="en">Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin.</title>
<author role="aut"> <persName> <forename type="first">Krister</forename>
<surname>Melén</surname>
</persName>
<idno type="halauthorid">794954</idno>
<affiliation ref="#struct-209196"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Janne</forename>
<surname>Tynell</surname>
</persName>
<idno type="halauthorid">794955</idno>
<affiliation ref="#struct-209196"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Riku</forename>
<surname>Fagerlund</surname>
</persName>
<idno type="halauthorid">794956</idno>
<affiliation ref="#struct-209197"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Pascal</forename>
<surname>Roussel</surname>
</persName>
<idno type="halauthorid">129289</idno>
<affiliation ref="#struct-148379"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Danièle</forename>
<surname>Hernandez-Verdun</surname>
</persName>
<idno type="halauthorid">87978</idno>
<affiliation ref="#struct-1131"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Ilkka</forename>
<surname>Julkunen</surname>
</persName>
<idno type="halauthorid">794957</idno>
<affiliation ref="#struct-209196"></affiliation>
</author>
</analytic>
<monogr> <idno type="localRef">Complexes macromoléculaires en cellules vivantes : Resp. M. Coppey</idno>
<idno type="halJournalId" status="INCOMING">36007</idno>
<title level="j">Virol J</title>
<imprint> <biblScope unit="volume">9</biblScope>
<biblScope unit="pp">167</biblScope>
<date type="datePub">2012</date>
<date type="dateEpub">2012-08-21</date>
</imprint>
</monogr>
<idno type="doi">10.1186/1743-422X-9-167</idno>
<idno type="pubmed">22909121</idno>
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</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <keywords scheme="author"> <term xml:lang="ro">Influenza A virus</term>
<term xml:lang="ro">NS1 protein</term>
<term xml:lang="ro">NoLS</term>
<term xml:lang="ro">Nucleolus</term>
<term xml:lang="ro">Nucleolin</term>
<term xml:lang="ro">B23</term>
<term xml:lang="ro">Fibrillarin</term>
</keywords>
<classCode scheme="halDomain" n="sdv.mp">Life Sciences [q-bio]/Microbiology and Parasitology</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
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<abstract xml:lang="en"> <p>UNLABELLED: ABSTRACT: BACKGROUND: Influenza A virus non-structural protein 1 (NS1) is a virulence factor, which is targeted into the cell cytoplasm, nucleus and nucleolus. NS1 is a multi-functional protein that inhibits host cell pre-mRNA processing and counteracts host cell antiviral responses. Previously, we have shown that the NS1 protein of the H3N2 subtype influenza viruses possesses a C-terminal nuclear localization signal (NLS) that also functions as a nucleolar localization signal (NoLS) and targets the protein into the nucleolus. RESULTS: Here, we show that the NS1 protein of the human H3N2 virus subtype interacts in vitro primarily via its C-terminal NLS2/NoLS and to a minor extent via its N-terminal NLS1 with the nucleolar proteins, nucleolin and fibrillarin. Using chimeric green fluorescence protein (GFP)-NS1 fusion constructs, we show that the nucleolar retention of the NS1 protein is determined by its C-terminal NLS2/NoLS in vivo. Confocal laser microscopy analysis shows that the NS1 protein colocalizes with nucleolin in nucleoplasm and nucleolus and with B23 and fibrillarin in the nucleolus of influenza A/Udorn/72 virus-infected A549 cells. Since some viral proteins contain NoLSs, it is likely that viruses have evolved specific nucleolar functions. CONCLUSION: NS1 protein of the human H3N2 virus interacts primarily via the C-terminal NLS2/NoLS and to a minor extent via the N-terminal NLS1 with the main nucleolar proteins, nucleolin, B23 and fibrillarin.</p>
</abstract>
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