AustralieFrV1, Main, Exploration, bibRecord, 003592

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus*

Identifieur interne : 003592 ( Main/Exploration ); précédent : 003591; suivant : 003593

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus*

Auteurs : Jens Milbradt ; Alexandra Kraut [France] ; Corina Hutterer ; Eric Sonntag ; Cathrin Schmeiser ; Myriam Ferro [France] ; Sabrina Wagner ; Tihana Lenac [Croatie] ; Claudia Claus [Allemagne] ; Sandra Pinkert [Allemagne] ; Stuart T. Hamilton [Australie] ; William D. Rawlinson [Australie] ; Heinrich Sticht [Allemagne] ; Yohann Couté [France] ; Manfred Marschall

Source :

Molecular & Cellular Proteomics : MCP [ 1535-9476 ] ; 2014.

RBID : PMC:4125742

Descripteurs français

KwdFr :
- Animaux, Cellules HEK293, Cytomegalovirus (physiologie), Fibroblastes (virologie), Humains, Protéines membranaires (métabolisme), Protéines nucléaires (métabolisme), Protéines virales (métabolisme), Protéomique (), Souris, Techniques de knock-down de gènes.
MESH :
- métabolisme : Protéines membranaires, Protéines nucléaires, Protéines virales.
- physiologie : Cytomegalovirus.
- virologie : Fibroblastes.
- Animaux, Cellules HEK293, Humains, Protéomique, Souris, Techniques de knock-down de gènes.

English descriptors

KwdEn :
- Animals, Cytomegalovirus (physiology), Fibroblasts (virology), Gene Knockdown Techniques, HEK293 Cells, Humans, Membrane Proteins (metabolism), Mice, Nuclear Proteins (metabolism), Proteomics (methods), Viral Proteins (metabolism).
MESH :
- chemical , metabolism : Membrane Proteins, Nuclear Proteins, Viral Proteins.
- methods : Proteomics.
- physiology : Cytomegalovirus.
- virology : Fibroblasts.
- Animals, Gene Knockdown Techniques, HEK293 Cells, Humans, Mice.

Abstract

Herpesviral capsids are assembled in the host cell nucleus before being translocated into the cytoplasm for further maturation. The crossing of the nuclear envelope represents a major event that requires the formation of the nuclear egress complex (NEC). Previous studies demonstrated that human cytomegalovirus (HCMV) proteins pUL50 and pUL53, as well as their homologs in all members of Herpesviridae, interact with each other at the nuclear envelope and form the heterodimeric core of the NEC. In order to characterize further the viral and cellular protein content of the multimeric NEC, the native complex was isolated from HCMV-infected human primary fibroblasts at various time points and analyzed using quantitative proteomics. Previously postulated components of the HCMV-specific NEC, as well as novel potential NEC-associated proteins such as emerin, were identified. In this regard, interaction and colocalization between emerin and pUL50 were confirmed by coimmunoprecipitation and confocal microscopy analyses, respectively. A functional validation of viral and cellular NEC constituents was achieved through siRNA-mediated knockdown experiments. The important role of emerin in NEC functionality was demonstrated by a reduction of viral replication when emerin expression was down-regulated. Moreover, under such conditions, reduced production of viral proteins and deregulation of viral late cytoplasmic maturation were observed. Combined, these data prove the functional importance of emerin as an NEC component, associated with pUL50, pUL53, pUL97, p32/gC1qR, and further regulatory proteins. Summarized, our findings provide the first proteomics-based characterization and functional validation of the HCMV-specific multimeric NEC.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4125742

DOI: 10.1074/mcp.M113.035782
PubMed: 24969177
PubMed Central: 4125742

Affiliations:

Le document en format XML

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<author><name sortKey="Rawlinson, William D" sort="Rawlinson, William D" uniqKey="Rawlinson W" first="William D." last="Rawlinson">William D. Rawlinson</name>
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<author><name sortKey="Sticht, Heinrich" sort="Sticht, Heinrich" uniqKey="Sticht H" first="Heinrich" last="Sticht">Heinrich Sticht</name>
<affiliation wicri:level="1"><nlm:aff id="aff9">‖‖Division of Bioinformatics, Institute of Biochemistry, University of Erlangen-Nuremberg, 91054 Erlangen, Germany</nlm:aff>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>‖‖Division of Bioinformatics, Institute of Biochemistry, University of Erlangen-Nuremberg, 91054 Erlangen</wicri:regionArea>
<wicri:noRegion>91054 Erlangen</wicri:noRegion>
<placeName><settlement type="city">Erlangen</settlement>
<region type="land" nuts="1">Bavière</region>
<region type="district" nuts="2">District de Moyenne-Franconie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Coute, Yohann" sort="Coute, Yohann" uniqKey="Coute Y" first="Yohann" last="Couté">Yohann Couté</name>
<affiliation wicri:level="4"><nlm:aff id="aff2">Université Grenoble Alpes, iRTSV-BGE, F-38000 Grenoble, France;</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université Grenoble Alpes, iRTSV-BGE, F-38000 Grenoble</wicri:regionArea>
<wicri:noRegion>38000 Grenoble</wicri:noRegion>
<orgName type="university">Université Grenoble-Alpes</orgName>
<placeName><settlement type="city">Grenoble</settlement>
<region type="region" nuts="2">Auvergne-Rhône-Alpes</region>
<region type="old region" nuts="2">Rhône-Alpes</region>
</placeName>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff3">¶CEA, iRTSV-BGE, F-38000 Grenoble, France;</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>¶CEA, iRTSV-BGE, F-38000 Grenoble</wicri:regionArea>
<wicri:noRegion>38000 Grenoble</wicri:noRegion>
<wicri:noRegion>38000 Grenoble</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff4">INSERM, BGE, F-38000 Grenoble, France;</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM, BGE, F-38000 Grenoble</wicri:regionArea>
<wicri:noRegion>38000 Grenoble</wicri:noRegion>
<wicri:noRegion>38000 Grenoble</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Marschall, Manfred" sort="Marschall, Manfred" uniqKey="Marschall M" first="Manfred" last="Marschall">Manfred Marschall</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">Molecular & Cellular Proteomics : MCP</title>
<idno type="ISSN">1535-9476</idno>
<idno type="eISSN">1535-9484</idno>
<imprint><date when="2014">2014</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Cytomegalovirus (physiology)</term>
<term>Fibroblasts (virology)</term>
<term>Gene Knockdown Techniques</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Membrane Proteins (metabolism)</term>
<term>Mice</term>
<term>Nuclear Proteins (metabolism)</term>
<term>Proteomics (methods)</term>
<term>Viral Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cellules HEK293</term>
<term>Cytomegalovirus (physiologie)</term>
<term>Fibroblastes (virologie)</term>
<term>Humains</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Protéines nucléaires (métabolisme)</term>
<term>Protéines virales (métabolisme)</term>
<term>Protéomique ()</term>
<term>Souris</term>
<term>Techniques de knock-down de gènes</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Proteins</term>
<term>Nuclear Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Proteomics</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines membranaires</term>
<term>Protéines nucléaires</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cytomegalovirus</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cytomegalovirus</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Fibroblastes</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Fibroblasts</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Gene Knockdown Techniques</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Mice</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules HEK293</term>
<term>Humains</term>
<term>Protéomique</term>
<term>Souris</term>
<term>Techniques de knock-down de gènes</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Herpesviral capsids are assembled in the host cell nucleus before being translocated into the cytoplasm for further maturation. The crossing of the nuclear envelope represents a major event that requires the formation of the nuclear egress complex (NEC). Previous studies demonstrated that human cytomegalovirus (HCMV) proteins pUL50 and pUL53, as well as their homologs in all members of <italic>Herpesviridae</italic>
, interact with each other at the nuclear envelope and form the heterodimeric core of the NEC. In order to characterize further the viral and cellular protein content of the multimeric NEC, the native complex was isolated from HCMV-infected human primary fibroblasts at various time points and analyzed using quantitative proteomics. Previously postulated components of the HCMV-specific NEC, as well as novel potential NEC-associated proteins such as emerin, were identified. In this regard, interaction and colocalization between emerin and pUL50 were confirmed by coimmunoprecipitation and confocal microscopy analyses, respectively. A functional validation of viral and cellular NEC constituents was achieved through siRNA-mediated knockdown experiments. The important role of emerin in NEC functionality was demonstrated by a reduction of viral replication when emerin expression was down-regulated. Moreover, under such conditions, reduced production of viral proteins and deregulation of viral late cytoplasmic maturation were observed. Combined, these data prove the functional importance of emerin as an NEC component, associated with pUL50, pUL53, pUL97, p32/gC1qR, and further regulatory proteins. Summarized, our findings provide the first proteomics-based characterization and functional validation of the HCMV-specific multimeric NEC.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>Allemagne</li>
<li>Australie</li>
<li>Croatie</li>
<li>France</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Bavière</li>
<li>Berlin</li>
<li>District de Leipzig</li>
<li>District de Moyenne-Franconie</li>
<li>Nouvelle-Galles du Sud</li>
<li>Rhône-Alpes</li>
<li>Saxe (Land)</li>
</region>
<settlement><li>Berlin</li>
<li>Erlangen</li>
<li>Grenoble</li>
<li>Leipzig</li>
<li>Sydney</li>
</settlement>
<orgName><li>Université Grenoble-Alpes</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Hutterer, Corina" sort="Hutterer, Corina" uniqKey="Hutterer C" first="Corina" last="Hutterer">Corina Hutterer</name>
<name sortKey="Marschall, Manfred" sort="Marschall, Manfred" uniqKey="Marschall M" first="Manfred" last="Marschall">Manfred Marschall</name>
<name sortKey="Milbradt, Jens" sort="Milbradt, Jens" uniqKey="Milbradt J" first="Jens" last="Milbradt">Jens Milbradt</name>
<name sortKey="Schmeiser, Cathrin" sort="Schmeiser, Cathrin" uniqKey="Schmeiser C" first="Cathrin" last="Schmeiser">Cathrin Schmeiser</name>
<name sortKey="Sonntag, Eric" sort="Sonntag, Eric" uniqKey="Sonntag E" first="Eric" last="Sonntag">Eric Sonntag</name>
<name sortKey="Wagner, Sabrina" sort="Wagner, Sabrina" uniqKey="Wagner S" first="Sabrina" last="Wagner">Sabrina Wagner</name>
</noCountry>
<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Kraut, Alexandra" sort="Kraut, Alexandra" uniqKey="Kraut A" first="Alexandra" last="Kraut">Alexandra Kraut</name>
</region>
<name sortKey="Coute, Yohann" sort="Coute, Yohann" uniqKey="Coute Y" first="Yohann" last="Couté">Yohann Couté</name>
<name sortKey="Coute, Yohann" sort="Coute, Yohann" uniqKey="Coute Y" first="Yohann" last="Couté">Yohann Couté</name>
<name sortKey="Coute, Yohann" sort="Coute, Yohann" uniqKey="Coute Y" first="Yohann" last="Couté">Yohann Couté</name>
<name sortKey="Ferro, Myriam" sort="Ferro, Myriam" uniqKey="Ferro M" first="Myriam" last="Ferro">Myriam Ferro</name>
<name sortKey="Ferro, Myriam" sort="Ferro, Myriam" uniqKey="Ferro M" first="Myriam" last="Ferro">Myriam Ferro</name>
<name sortKey="Ferro, Myriam" sort="Ferro, Myriam" uniqKey="Ferro M" first="Myriam" last="Ferro">Myriam Ferro</name>
<name sortKey="Kraut, Alexandra" sort="Kraut, Alexandra" uniqKey="Kraut A" first="Alexandra" last="Kraut">Alexandra Kraut</name>
<name sortKey="Kraut, Alexandra" sort="Kraut, Alexandra" uniqKey="Kraut A" first="Alexandra" last="Kraut">Alexandra Kraut</name>
</country>
<country name="Croatie"><noRegion><name sortKey="Lenac, Tihana" sort="Lenac, Tihana" uniqKey="Lenac T" first="Tihana" last="Lenac">Tihana Lenac</name>
</noRegion>
</country>
<country name="Allemagne"><region name="Saxe (Land)"><name sortKey="Claus, Claudia" sort="Claus, Claudia" uniqKey="Claus C" first="Claudia" last="Claus">Claudia Claus</name>
</region>
<name sortKey="Pinkert, Sandra" sort="Pinkert, Sandra" uniqKey="Pinkert S" first="Sandra" last="Pinkert">Sandra Pinkert</name>
<name sortKey="Sticht, Heinrich" sort="Sticht, Heinrich" uniqKey="Sticht H" first="Heinrich" last="Sticht">Heinrich Sticht</name>
</country>
<country name="Australie"><region name="Nouvelle-Galles du Sud"><name sortKey="Hamilton, Stuart T" sort="Hamilton, Stuart T" uniqKey="Hamilton S" first="Stuart T." last="Hamilton">Stuart T. Hamilton</name>
</region>
<name sortKey="Rawlinson, William D" sort="Rawlinson, William D" uniqKey="Rawlinson W" first="William D." last="Rawlinson">William D. Rawlinson</name>
</country>
</tree>
</affiliations>
</record>

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Serveur d'exploration sur les relations entre la France et l'Australie

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus*

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human Cytomegalovirus*

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	Serveur d'exploration sur les relations entre la France et l'Australie
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