Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin
<p>Abstract</p> <p>Background</p> <p>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 h...
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BMC
2012-08-01
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Series: | Virology Journal |
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Online Access: | http://www.virologyj.com/content/9/1/167 |
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author | Melén Krister Tynell Janne Fagerlund Riku Roussel Pascal Hernandez-Verdun Danièle Julkunen Ilkka |
author_facet | Melén Krister Tynell Janne Fagerlund Riku Roussel Pascal Hernandez-Verdun Danièle Julkunen Ilkka |
author_sort | Melén Krister |
collection | DOAJ |
description | <p>Abstract</p> <p>Background</p> <p>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.</p> <p>Results</p> <p>Here, we show that the NS1 protein of the human H3N2 virus subtype interacts <it>in vitro</it> 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 <it>in vivo</it>. 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.</p> <p>Conclusion</p> <p>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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language | English |
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publishDate | 2012-08-01 |
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series | Virology Journal |
spelling | doaj.art-df8f5a88b32e488189c7453624c878ba2022-12-22T00:25:36ZengBMCVirology Journal1743-422X2012-08-019116710.1186/1743-422X-9-167Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarinMelén KristerTynell JanneFagerlund RikuRoussel PascalHernandez-Verdun DanièleJulkunen Ilkka<p>Abstract</p> <p>Background</p> <p>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.</p> <p>Results</p> <p>Here, we show that the NS1 protein of the human H3N2 virus subtype interacts <it>in vitro</it> 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 <it>in vivo</it>. 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.</p> <p>Conclusion</p> <p>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>http://www.virologyj.com/content/9/1/167Influenza A virusNS1 proteinNoLSNucleolusNucleolinB23Fibrillarin |
spellingShingle | Melén Krister Tynell Janne Fagerlund Riku Roussel Pascal Hernandez-Verdun Danièle Julkunen Ilkka Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin Virology Journal Influenza A virus NS1 protein NoLS Nucleolus Nucleolin B23 Fibrillarin |
title | 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_full | 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_fullStr | 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_full_unstemmed | 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_short | 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_sort | influenza a h3n2 subtype virus ns1 protein targets into the nucleus and binds primarily via its c terminal nls2 nols to nucleolin and fibrillarin |
topic | Influenza A virus NS1 protein NoLS Nucleolus Nucleolin B23 Fibrillarin |
url | http://www.virologyj.com/content/9/1/167 |
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