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
Links toward previous steps (curation, corpus...)
Links to Exploration step
Hal:hal-00764038Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><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><name sortKey="Melen, Krister" sort="Melen, Krister" uniqKey="Melen K" first="Krister" last="Melén">Krister Melén</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209196" status="INCOMING"> <orgName>Virology Unit, Department of Infectious Disease Surveillance and Control</orgName>
<orgName type="acronym">THL</orgName>
<desc> <address> <addrLine>Mannerheimintie 166, FIN-00300, Helsinki</addrLine>
<country key="FI"></country>
</address>
</desc>
<listRelation> <relation active="#struct-420582" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-420582" type="direct"><org type="institution" xml:id="struct-420582" status="VALID"> <orgName>National Institute for Health and Welfare [Helsinki]</orgName>
<desc> <address> <addrLine>PO Box 30, FI-00271 Helsinki</addrLine>
<country key="FI"></country>
</address>
<ref type="url">https://www.thl.fi/fi/web/thlfi-en</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>Finlande</country>
</affiliation>
</author>
<author><name sortKey="Tynell, Janne" sort="Tynell, Janne" uniqKey="Tynell J" first="Janne" last="Tynell">Janne Tynell</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209196" status="INCOMING"> <orgName>Virology Unit, Department of Infectious Disease Surveillance and Control</orgName>
<orgName type="acronym">THL</orgName>
<desc> <address> <addrLine>Mannerheimintie 166, FIN-00300, Helsinki</addrLine>
<country key="FI"></country>
</address>
</desc>
<listRelation> <relation active="#struct-420582" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-420582" type="direct"><org type="institution" xml:id="struct-420582" status="VALID"> <orgName>National Institute for Health and Welfare [Helsinki]</orgName>
<desc> <address> <addrLine>PO Box 30, FI-00271 Helsinki</addrLine>
<country key="FI"></country>
</address>
<ref type="url">https://www.thl.fi/fi/web/thlfi-en</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>Finlande</country>
</affiliation>
</author>
<author><name sortKey="Fagerlund, Riku" sort="Fagerlund, Riku" uniqKey="Fagerlund R" first="Riku" last="Fagerlund">Riku Fagerlund</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209197" status="INCOMING"> <orgName>Signaling Systems Laboratory, Department of Chemistry and Biochemistry</orgName>
<desc> <address> <addrLine>San Diego, La Jolla, CA, 92093</addrLine>
<country key="US"></country>
</address>
</desc>
<listRelation> <relation active="#struct-300717" type="direct"></relation>
<relation active="#struct-471291" type="indirect"></relation>
</listRelation>
<tutelles><tutelle active="#struct-300717" type="direct"><org type="institution" xml:id="struct-300717" status="VALID"> <orgName>University of California [San Diego]</orgName>
<orgName type="acronym">UC San Diego</orgName>
<desc> <address> <addrLine>9500 Gilman Dr., La Jolla, CA 92093 USA</addrLine>
<country key="US"></country>
</address>
<ref type="url">https://ucsd.edu/</ref>
</desc>
<listRelation> <relation active="#struct-471291" type="direct"></relation>
</listRelation>
</org>
</tutelle>
<tutelle active="#struct-471291" type="indirect"><org type="regroupinstitution" xml:id="struct-471291" status="VALID"> <orgName>University of California</orgName>
<desc> <address> <country key="US"></country>
</address>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>États-Unis</country>
</affiliation>
</author>
<author><name sortKey="Roussel, Pascal" sort="Roussel, Pascal" uniqKey="Roussel P" first="Pascal" last="Roussel">Pascal Roussel</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-148379" status="OLD"> <orgName>Biologie de l'ARN</orgName>
<orgName type="acronym">RnBi</orgName>
<desc> <address> <country key="FR"></country>
</address>
</desc>
<listRelation> <relation active="#struct-93591" type="direct"></relation>
<relation name="FRE3402" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-93591" type="direct"><org type="institution" xml:id="struct-93591" status="OLD"> <orgName>Université Pierre et Marie Curie - Paris 6</orgName>
<orgName type="acronym">UPMC</orgName>
<date type="end">2017-12-31</date>
<desc> <address> <addrLine>4 place Jussieu - 75005 Paris</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.upmc.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="FRE3402" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>France</country>
</affiliation>
</author>
<author><name sortKey="Hernandez Verdun, Daniele" sort="Hernandez Verdun, Daniele" uniqKey="Hernandez Verdun D" first="Danièle" last="Hernandez-Verdun">Danièle Hernandez-Verdun</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-1131" status="OLD"> <idno type="IdRef">026536412</idno>
<idno type="RNSR">199712638E</idno>
<orgName>Institut Jacques Monod</orgName>
<orgName type="acronym">IJM (UMR_7592)</orgName>
<date type="end">2019-12-31</date>
<desc> <address> <addrLine>Université Paris Diderot, Bât. Buffon, 15 rue Hélène Brion, 75205 Paris cédex 13</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.ijm.fr/</ref>
</desc>
<listRelation> <relation name="UMR_7592" active="#struct-300301" type="direct"></relation>
<relation name="UMR_7592" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle name="UMR_7592" active="#struct-300301" type="direct"><org type="institution" xml:id="struct-300301" status="OLD"> <idno type="ISNI">0000000121514068</idno>
<idno type="IdRef">027542084</idno>
<orgName>Université Paris Diderot - Paris 7</orgName>
<orgName type="acronym">UPD7</orgName>
<date type="end">2019-12-31</date>
<desc> <address> <addrLine>5 rue Thomas-Mann - 75205 Paris cedex 13</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.univ-paris-diderot.fr</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR_7592" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>France</country>
</affiliation>
</author>
<author><name sortKey="Julkunen, Ilkka" sort="Julkunen, Ilkka" uniqKey="Julkunen I" first="Ilkka" last="Julkunen">Ilkka Julkunen</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209196" status="INCOMING"> <orgName>Virology Unit, Department of Infectious Disease Surveillance and Control</orgName>
<orgName type="acronym">THL</orgName>
<desc> <address> <addrLine>Mannerheimintie 166, FIN-00300, Helsinki</addrLine>
<country key="FI"></country>
</address>
</desc>
<listRelation> <relation active="#struct-420582" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-420582" type="direct"><org type="institution" xml:id="struct-420582" status="VALID"> <orgName>National Institute for Health and Welfare [Helsinki]</orgName>
<desc> <address> <addrLine>PO Box 30, FI-00271 Helsinki</addrLine>
<country key="FI"></country>
</address>
<ref type="url">https://www.thl.fi/fi/web/thlfi-en</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>Finlande</country>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">HAL</idno>
<idno type="RBID">Hal:hal-00764038</idno>
<idno type="halId">hal-00764038</idno>
<idno type="halUri">https://hal.archives-ouvertes.fr/hal-00764038</idno>
<idno type="url">https://hal.archives-ouvertes.fr/hal-00764038</idno>
<idno type="doi">10.1186/1743-422X-9-167</idno>
<date when="2012">2012</date>
<idno type="wicri:Area/Hal/Corpus">000158</idno>
<idno type="wicri:Area/Hal/Curation">000158</idno>
<idno type="wicri:Area/Hal/Checkpoint">000201</idno>
<idno type="wicri:explorRef" wicri:stream="Hal" wicri:step="Checkpoint">000201</idno>
</publicationStmt>
<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><name sortKey="Melen, Krister" sort="Melen, Krister" uniqKey="Melen K" first="Krister" last="Melén">Krister Melén</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209196" status="INCOMING"> <orgName>Virology Unit, Department of Infectious Disease Surveillance and Control</orgName>
<orgName type="acronym">THL</orgName>
<desc> <address> <addrLine>Mannerheimintie 166, FIN-00300, Helsinki</addrLine>
<country key="FI"></country>
</address>
</desc>
<listRelation> <relation active="#struct-420582" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-420582" type="direct"><org type="institution" xml:id="struct-420582" status="VALID"> <orgName>National Institute for Health and Welfare [Helsinki]</orgName>
<desc> <address> <addrLine>PO Box 30, FI-00271 Helsinki</addrLine>
<country key="FI"></country>
</address>
<ref type="url">https://www.thl.fi/fi/web/thlfi-en</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>Finlande</country>
</affiliation>
</author>
<author><name sortKey="Tynell, Janne" sort="Tynell, Janne" uniqKey="Tynell J" first="Janne" last="Tynell">Janne Tynell</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209196" status="INCOMING"> <orgName>Virology Unit, Department of Infectious Disease Surveillance and Control</orgName>
<orgName type="acronym">THL</orgName>
<desc> <address> <addrLine>Mannerheimintie 166, FIN-00300, Helsinki</addrLine>
<country key="FI"></country>
</address>
</desc>
<listRelation> <relation active="#struct-420582" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-420582" type="direct"><org type="institution" xml:id="struct-420582" status="VALID"> <orgName>National Institute for Health and Welfare [Helsinki]</orgName>
<desc> <address> <addrLine>PO Box 30, FI-00271 Helsinki</addrLine>
<country key="FI"></country>
</address>
<ref type="url">https://www.thl.fi/fi/web/thlfi-en</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>Finlande</country>
</affiliation>
</author>
<author><name sortKey="Fagerlund, Riku" sort="Fagerlund, Riku" uniqKey="Fagerlund R" first="Riku" last="Fagerlund">Riku Fagerlund</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209197" status="INCOMING"> <orgName>Signaling Systems Laboratory, Department of Chemistry and Biochemistry</orgName>
<desc> <address> <addrLine>San Diego, La Jolla, CA, 92093</addrLine>
<country key="US"></country>
</address>
</desc>
<listRelation> <relation active="#struct-300717" type="direct"></relation>
<relation active="#struct-471291" type="indirect"></relation>
</listRelation>
<tutelles><tutelle active="#struct-300717" type="direct"><org type="institution" xml:id="struct-300717" status="VALID"> <orgName>University of California [San Diego]</orgName>
<orgName type="acronym">UC San Diego</orgName>
<desc> <address> <addrLine>9500 Gilman Dr., La Jolla, CA 92093 USA</addrLine>
<country key="US"></country>
</address>
<ref type="url">https://ucsd.edu/</ref>
</desc>
<listRelation> <relation active="#struct-471291" type="direct"></relation>
</listRelation>
</org>
</tutelle>
<tutelle active="#struct-471291" type="indirect"><org type="regroupinstitution" xml:id="struct-471291" status="VALID"> <orgName>University of California</orgName>
<desc> <address> <country key="US"></country>
</address>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>États-Unis</country>
</affiliation>
</author>
<author><name sortKey="Roussel, Pascal" sort="Roussel, Pascal" uniqKey="Roussel P" first="Pascal" last="Roussel">Pascal Roussel</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-148379" status="OLD"> <orgName>Biologie de l'ARN</orgName>
<orgName type="acronym">RnBi</orgName>
<desc> <address> <country key="FR"></country>
</address>
</desc>
<listRelation> <relation active="#struct-93591" type="direct"></relation>
<relation name="FRE3402" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-93591" type="direct"><org type="institution" xml:id="struct-93591" status="OLD"> <orgName>Université Pierre et Marie Curie - Paris 6</orgName>
<orgName type="acronym">UPMC</orgName>
<date type="end">2017-12-31</date>
<desc> <address> <addrLine>4 place Jussieu - 75005 Paris</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.upmc.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="FRE3402" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>France</country>
</affiliation>
</author>
<author><name sortKey="Hernandez Verdun, Daniele" sort="Hernandez Verdun, Daniele" uniqKey="Hernandez Verdun D" first="Danièle" last="Hernandez-Verdun">Danièle Hernandez-Verdun</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-1131" status="OLD"> <idno type="IdRef">026536412</idno>
<idno type="RNSR">199712638E</idno>
<orgName>Institut Jacques Monod</orgName>
<orgName type="acronym">IJM (UMR_7592)</orgName>
<date type="end">2019-12-31</date>
<desc> <address> <addrLine>Université Paris Diderot, Bât. Buffon, 15 rue Hélène Brion, 75205 Paris cédex 13</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.ijm.fr/</ref>
</desc>
<listRelation> <relation name="UMR_7592" active="#struct-300301" type="direct"></relation>
<relation name="UMR_7592" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle name="UMR_7592" active="#struct-300301" type="direct"><org type="institution" xml:id="struct-300301" status="OLD"> <idno type="ISNI">0000000121514068</idno>
<idno type="IdRef">027542084</idno>
<orgName>Université Paris Diderot - Paris 7</orgName>
<orgName type="acronym">UPD7</orgName>
<date type="end">2019-12-31</date>
<desc> <address> <addrLine>5 rue Thomas-Mann - 75205 Paris cedex 13</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.univ-paris-diderot.fr</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR_7592" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>France</country>
</affiliation>
</author>
<author><name sortKey="Julkunen, Ilkka" sort="Julkunen, Ilkka" uniqKey="Julkunen I" first="Ilkka" last="Julkunen">Ilkka Julkunen</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-209196" status="INCOMING"> <orgName>Virology Unit, Department of Infectious Disease Surveillance and Control</orgName>
<orgName type="acronym">THL</orgName>
<desc> <address> <addrLine>Mannerheimintie 166, FIN-00300, Helsinki</addrLine>
<country key="FI"></country>
</address>
</desc>
<listRelation> <relation active="#struct-420582" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-420582" type="direct"><org type="institution" xml:id="struct-420582" status="VALID"> <orgName>National Institute for Health and Welfare [Helsinki]</orgName>
<desc> <address> <addrLine>PO Box 30, FI-00271 Helsinki</addrLine>
<country key="FI"></country>
</address>
<ref type="url">https://www.thl.fi/fi/web/thlfi-en</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>Finlande</country>
</affiliation>
</author>
</analytic>
<idno type="DOI">10.1186/1743-422X-9-167</idno>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="mix" xml:lang="ro"><term>B23</term>
<term>Fibrillarin</term>
<term>Influenza A virus</term>
<term>NS1 protein</term>
<term>NoLS</term>
<term>Nucleolin</term>
<term>Nucleolus</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</div>
</front>
</TEI>
<hal api="V3"> <titleStmt> <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>
<editor role="depositor"> <persName> <forename>Martine</forename>
<surname>Bondidier</surname>
</persName>
<email type="md5">936cd32b8405a0c3eb8c6432ce90f978</email>
<email type="domain">ijm.fr</email>
</editor>
</titleStmt>
<editionStmt> <edition n="v1" type="current"> <date type="whenSubmitted">2012-12-12 11:17:30</date>
<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>
</edition>
<respStmt> <resp>contributor</resp>
<name key="113036"> <persName> <forename>Martine</forename>
<surname>Bondidier</surname>
</persName>
<email type="md5">936cd32b8405a0c3eb8c6432ce90f978</email>
<email type="domain">ijm.fr</email>
</name>
</respStmt>
</editionStmt>
<publicationStmt> <distributor>CCSD</distributor>
<idno type="halId">hal-00764038</idno>
<idno type="halUri">https://hal.archives-ouvertes.fr/hal-00764038</idno>
<idno type="halBibtex">melen:hal-00764038</idno>
<idno type="halRefHtml">Virol J, 2012, 9, pp.167. ⟨10.1186/1743-422X-9-167⟩</idno>
<idno type="halRef">Virol J, 2012, 9, pp.167. ⟨10.1186/1743-422X-9-167⟩</idno>
</publicationStmt>
<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>
</seriesStmt>
<notesStmt> <note type="audience" n="2">International</note>
<note type="popular" n="0">No</note>
<note type="peer" n="1">Yes</note>
</notesStmt>
<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>
</biblStruct>
</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>
</textClass>
<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>
</profileDesc>
</hal>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Hal/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000201 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Hal/Checkpoint/biblio.hfd -nk 000201 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= H2N2V1 |flux= Hal |étape= Checkpoint |type= RBID |clé= Hal:hal-00764038 |texte= Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarin. }}
This area was generated with Dilib version V0.6.33. |