Global Reprogramming of Host SUMOylation during Influenza Virus Infection.
Identifieur interne : 000D37 ( Main/Exploration ); précédent : 000D36; suivant : 000D38Global Reprogramming of Host SUMOylation during Influenza Virus Infection.
Auteurs : Patricia Domingues [Royaume-Uni] ; Filip Golebiowski [Royaume-Uni] ; Michael H. Tatham [Royaume-Uni] ; Antonio M. Lopes [Royaume-Uni] ; Aislynn Taggart [Royaume-Uni] ; Ronald T. Hay [Royaume-Uni] ; Benjamin G. Hale [Royaume-Uni]Source :
- Cell reports [ 2211-1247 ] ; 2015.
Descripteurs français
- KwdFr :
- ARN viral (physiologie), Activation de la transcription, Animaux, Cellules HEK293, Cellules Vero, Cellules rénales canines Madin-Darby, Chiens, Humains, Interactions hôte-pathogène, Lignée cellulaire tumorale, Protéines suppresseurs de tumeurs (métabolisme), Protéome (métabolisme), Sumoylation, Transport de protéines, Virus de la grippe A (physiologie).
- MESH :
- métabolisme : Protéines suppresseurs de tumeurs, Protéome.
- physiologie : ARN viral, Virus de la grippe A.
- Activation de la transcription, Animaux, Cellules HEK293, Cellules Vero, Cellules rénales canines Madin-Darby, Chiens, Humains, Interactions hôte-pathogène, Lignée cellulaire tumorale, Sumoylation, Transport de protéines.
English descriptors
- KwdEn :
- Animals, Cell Line, Tumor, Chlorocebus aethiops, Dogs, HEK293 Cells, Host-Pathogen Interactions, Humans, Influenza A virus (physiology), Madin Darby Canine Kidney Cells, Protein Transport, Proteome (metabolism), RNA, Viral (physiology), Sumoylation, Transcriptional Activation, Tumor Suppressor Proteins (metabolism), Vero Cells.
- MESH :
- chemical , metabolism : Proteome, Tumor Suppressor Proteins.
- physiology : Influenza A virus, RNA, Viral.
- Animals, Cell Line, Tumor, Chlorocebus aethiops, Dogs, HEK293 Cells, Host-Pathogen Interactions, Humans, Madin Darby Canine Kidney Cells, Protein Transport, Sumoylation, Transcriptional Activation, Vero Cells.
Abstract
Dynamic nuclear SUMO modifications play essential roles in orchestrating cellular responses to proteotoxic stress, DNA damage, and DNA virus infection. Here, we describe a non-canonical host SUMOylation response to the nuclear-replicating RNA pathogen, influenza virus, and identify viral RNA polymerase activity as a major contributor to SUMO proteome remodeling. Using quantitative proteomics to compare stress-induced SUMOylation responses, we reveal that influenza virus infection triggers unique re-targeting of SUMO to 63 host proteins involved in transcription, mRNA processing, RNA quality control, and DNA damage repair. This is paralleled by widespread host deSUMOylation. Depletion screening identified ten virus-induced SUMO targets as potential antiviral factors, including C18orf25 and the SMC5/6 and PAF1 complexes. Mechanistic studies further uncovered a role for SUMOylation of the PAF1 complex component, parafibromin (CDC73), in potentiating antiviral gene expression. Our global characterization of influenza virus-triggered SUMO redistribution provides a proteomic resource to understand host nuclear SUMOylation responses to infection.
DOI: 10.1016/j.celrep.2015.10.001
PubMed: 26549460
Affiliations:
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Electronic address: hale.ben@virology.uzh.ch.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>MRC-University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH</wicri:regionArea><wicri:noRegion>Glasgow G61 1QH</wicri:noRegion></affiliation></author></analytic><series><title level="j">Cell reports</title><idno type="eISSN">2211-1247</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>Chlorocebus aethiops</term><term>Dogs</term><term>HEK293 Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Influenza A virus (physiology)</term><term>Madin Darby Canine Kidney Cells</term><term>Protein Transport</term><term>Proteome (metabolism)</term><term>RNA, Viral (physiology)</term><term>Sumoylation</term><term>Transcriptional Activation</term><term>Tumor Suppressor Proteins (metabolism)</term><term>Vero Cells</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (physiologie)</term><term>Activation de la transcription</term><term>Animaux</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cellules rénales canines Madin-Darby</term><term>Chiens</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Lignée cellulaire tumorale</term><term>Protéines suppresseurs de tumeurs (métabolisme)</term><term>Protéome (métabolisme)</term><term>Sumoylation</term><term>Transport de protéines</term><term>Virus de la grippe A (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Proteome</term><term>Tumor Suppressor Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines suppresseurs de tumeurs</term><term>Protéome</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>ARN viral</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A virus</term><term>RNA, Viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>Chlorocebus aethiops</term><term>Dogs</term><term>HEK293 Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Madin Darby Canine Kidney Cells</term><term>Protein Transport</term><term>Sumoylation</term><term>Transcriptional Activation</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation de la transcription</term><term>Animaux</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cellules rénales canines Madin-Darby</term><term>Chiens</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Lignée cellulaire tumorale</term><term>Sumoylation</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Dynamic nuclear SUMO modifications play essential roles in orchestrating cellular responses to proteotoxic stress, DNA damage, and DNA virus infection. Here, we describe a non-canonical host SUMOylation response to the nuclear-replicating RNA pathogen, influenza virus, and identify viral RNA polymerase activity as a major contributor to SUMO proteome remodeling. Using quantitative proteomics to compare stress-induced SUMOylation responses, we reveal that influenza virus infection triggers unique re-targeting of SUMO to 63 host proteins involved in transcription, mRNA processing, RNA quality control, and DNA damage repair. This is paralleled by widespread host deSUMOylation. Depletion screening identified ten virus-induced SUMO targets as potential antiviral factors, including C18orf25 and the SMC5/6 and PAF1 complexes. Mechanistic studies further uncovered a role for SUMOylation of the PAF1 complex component, parafibromin (CDC73), in potentiating antiviral gene expression. Our global characterization of influenza virus-triggered SUMO redistribution provides a proteomic resource to understand host nuclear SUMOylation responses to infection. </div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Domingues, Patricia" sort="Domingues, Patricia" uniqKey="Domingues P" first="Patricia" last="Domingues">Patricia Domingues</name></noRegion><name sortKey="Golebiowski, Filip" sort="Golebiowski, Filip" uniqKey="Golebiowski F" first="Filip" last="Golebiowski">Filip Golebiowski</name><name sortKey="Hale, Benjamin G" sort="Hale, Benjamin G" uniqKey="Hale B" first="Benjamin G" last="Hale">Benjamin G. Hale</name><name sortKey="Hay, Ronald T" sort="Hay, Ronald T" uniqKey="Hay R" first="Ronald T" last="Hay">Ronald T. Hay</name><name sortKey="Lopes, Antonio M" sort="Lopes, Antonio M" uniqKey="Lopes A" first="Antonio M" last="Lopes">Antonio M. Lopes</name><name sortKey="Taggart, Aislynn" sort="Taggart, Aislynn" uniqKey="Taggart A" first="Aislynn" last="Taggart">Aislynn Taggart</name><name sortKey="Tatham, Michael H" sort="Tatham, Michael H" uniqKey="Tatham M" first="Michael H" last="Tatham">Michael H. Tatham</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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