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 : 000160 ( France/Analysis ); précédent : 000159; suivant : 000161Influenza 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
Affiliations:
Links toward previous steps (curation, corpus...)
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- to stream Main, to step Merge: 000990
- to stream Main, to step Curation: 000989
- to stream Main, to step Exploration: 000989
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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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<name sortKey="Julkunen, Ilkka" sort="Julkunen, Ilkka" uniqKey="Julkunen I" first="Ilkka" last="Julkunen">Ilkka Julkunen</name>
<name sortKey="Tynell, Janne" sort="Tynell, Janne" uniqKey="Tynell J" first="Janne" last="Tynell">Janne Tynell</name>
</country>
<country name="États-Unis"><noRegion><name sortKey="Fagerlund, Riku" sort="Fagerlund, Riku" uniqKey="Fagerlund R" first="Riku" last="Fagerlund">Riku Fagerlund</name>
</noRegion>
</country>
<country name="France"><noRegion><name sortKey="Roussel, Pascal" sort="Roussel, Pascal" uniqKey="Roussel P" first="Pascal" last="Roussel">Pascal Roussel</name>
</noRegion>
<name sortKey="Hernandez Verdun, Daniele" sort="Hernandez Verdun, Daniele" uniqKey="Hernandez Verdun D" first="Danièle" last="Hernandez-Verdun">Danièle Hernandez-Verdun</name>
</country>
</tree>
</affiliations>
</record>
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