Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.
Identifieur interne : 001562 ( Main/Exploration ); précédent : 001561; suivant : 001563Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.
Auteurs : Kam-Leung Siu [Hong Kong] ; Chi-Ping Chan [Hong Kong] ; Kin-Hang Kok [Hong Kong] ; Patrick Chiu-Yat Woo [Hong Kong] ; Dong-Yan Jin [Hong Kong]Source :
- Cellular & molecular immunology [ 2042-0226 ] ; 2014.
Descripteurs français
- KwdFr :
- Appareil de Golgi (métabolisme), Cellules HEK293, Cellules HeLa, Coronavirus (immunologie), Facteur-3 associé aux récepteurs de TNF (métabolisme), Humains, I-kappa B Kinase (métabolisme), Immunité innée, Immunosuppression thérapeutique, Interféron de type I (métabolisme), Liaison aux protéines (génétique), Mutation (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Protéines membranaires (génétique), Protéines membranaires (métabolisme), Signaux de triage des protéines (génétique), Structure tertiaire des protéines (génétique), Syndrome respiratoire aigu sévère (immunologie), Syndrome respiratoire aigu sévère (virologie), Échappement immunitaire.
- MESH :
- génétique : Liaison aux protéines, Mutation, Protéines de la matrice virale, Protéines membranaires, Signaux de triage des protéines, Structure tertiaire des protéines.
- immunologie : Coronavirus, Syndrome respiratoire aigu sévère.
- métabolisme : Appareil de Golgi, Facteur-3 associé aux récepteurs de TNF, I-kappa B Kinase, Interféron de type I, Protein-Serine-Threonine Kinases, Protéines de la matrice virale, Protéines membranaires.
- virologie : Syndrome respiratoire aigu sévère.
- Cellules HEK293, Cellules HeLa, Humains, Immunité innée, Immunosuppression thérapeutique, Échappement immunitaire.
English descriptors
- KwdEn :
- Coronavirus (immunology), Golgi Apparatus (metabolism), HEK293 Cells, HeLa Cells, Humans, I-kappa B Kinase (metabolism), Immune Evasion, Immunity, Innate, Immunosuppression, Interferon Type I (metabolism), Membrane Proteins (genetics), Membrane Proteins (metabolism), Mutation (genetics), Protein Binding (genetics), Protein Sorting Signals (genetics), Protein Structure, Tertiary (genetics), Protein-Serine-Threonine Kinases (metabolism), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (virology), TNF Receptor-Associated Factor 3 (metabolism), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism).
- MESH :
- chemical , genetics : Membrane Proteins, Protein Sorting Signals, Viral Matrix Proteins.
- chemical , metabolism : I-kappa B Kinase, Interferon Type I, Membrane Proteins, Protein-Serine-Threonine Kinases, TNF Receptor-Associated Factor 3, Viral Matrix Proteins.
- genetics : Mutation, Protein Binding, Protein Structure, Tertiary.
- immunology : Coronavirus, Severe Acute Respiratory Syndrome.
- metabolism : Golgi Apparatus.
- virology : Severe Acute Respiratory Syndrome.
- HEK293 Cells, HeLa Cells, Humans, Immune Evasion, Immunity, Innate, Immunosuppression.
Abstract
Coronaviruses have developed various measures to evade innate immunity. We have previously shown that severe acute respiratory syndrome (SARS) coronavirus M protein suppresses type I interferon (IFN) production by impeding the formation of functional TRAF3-containing complex. In this study, we demonstrate that the IFN-antagonizing activity is specific to SARS coronavirus M protein and is mediated through its first transmembrane domain (TM1) located at the N terminus. M protein from human coronavirus HKU1 does not inhibit IFN production. Whereas N-linked glycosylation of SARS coronavirus M protein has no influence on IFN antagonism, TM1 is indispensable for the suppression of IFN production. TM1 targets SARS coronavirus M protein and heterologous proteins to the Golgi apparatus, yet Golgi localization is required but not sufficient for IFN antagonism. Mechanistically, TM1 is capable of binding with RIG-I, TRAF3, TBK1 and IKKε, and preventing the interaction of TRAF3 with its downstream effectors. Our work defines the molecular architecture of SARS coronavirus M protein required for suppression of innate antiviral response.
DOI: 10.1038/cmi.2013.61
PubMed: 24509444
Affiliations:
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Le document en format XML
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wicri:level="1"><nlm:affiliation>Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong.</nlm:affiliation><country xml:lang="fr">Hong Kong</country><wicri:regionArea>Department of Biochemistry, The University of Hong Kong, Pokfulam</wicri:regionArea><wicri:noRegion>Pokfulam</wicri:noRegion></affiliation></author><author><name sortKey="Chan, Chi Ping" sort="Chan, Chi Ping" uniqKey="Chan C" first="Chi-Ping" last="Chan">Chi-Ping Chan</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong.</nlm:affiliation><country xml:lang="fr">Hong Kong</country><wicri:regionArea>Department of Biochemistry, The University of Hong Kong, Pokfulam</wicri:regionArea><wicri:noRegion>Pokfulam</wicri:noRegion></affiliation></author><author><name sortKey="Kok, Kin Hang" sort="Kok, Kin Hang" uniqKey="Kok K" first="Kin-Hang" last="Kok">Kin-Hang Kok</name><affiliation wicri:level="1"><nlm:affiliation>Department of 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University of Hong Kong, Pokfulam, Hong Kong.</nlm:affiliation><country xml:lang="fr">Hong Kong</country><wicri:regionArea>Department of Biochemistry, The University of Hong Kong, Pokfulam</wicri:regionArea><wicri:noRegion>Pokfulam</wicri:noRegion></affiliation></author></analytic><series><title level="j">Cellular & molecular immunology</title><idno type="eISSN">2042-0226</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus (immunology)</term><term>Golgi Apparatus (metabolism)</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>I-kappa B Kinase (metabolism)</term><term>Immune Evasion</term><term>Immunity, Innate</term><term>Immunosuppression</term><term>Interferon Type I (metabolism)</term><term>Membrane Proteins (genetics)</term><term>Membrane Proteins (metabolism)</term><term>Mutation (genetics)</term><term>Protein Binding (genetics)</term><term>Protein Sorting Signals (genetics)</term><term>Protein Structure, Tertiary (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Severe Acute Respiratory Syndrome (immunology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>TNF Receptor-Associated Factor 3 (metabolism)</term><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Appareil de Golgi (métabolisme)</term><term>Cellules HEK293</term><term>Cellules HeLa</term><term>Coronavirus (immunologie)</term><term>Facteur-3 associé aux récepteurs de TNF (métabolisme)</term><term>Humains</term><term>I-kappa B Kinase (métabolisme)</term><term>Immunité innée</term><term>Immunosuppression thérapeutique</term><term>Interféron de type I (métabolisme)</term><term>Liaison aux protéines (génétique)</term><term>Mutation (génétique)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines de la matrice virale (génétique)</term><term>Protéines de la matrice virale (métabolisme)</term><term>Protéines membranaires (génétique)</term><term>Protéines membranaires (métabolisme)</term><term>Signaux de triage des protéines (génétique)</term><term>Structure tertiaire des protéines (génétique)</term><term>Syndrome respiratoire aigu sévère (immunologie)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Échappement immunitaire</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Proteins</term><term>Protein Sorting Signals</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>I-kappa B Kinase</term><term>Interferon Type I</term><term>Membrane Proteins</term><term>Protein-Serine-Threonine Kinases</term><term>TNF Receptor-Associated Factor 3</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Liaison aux protéines</term><term>Mutation</term><term>Protéines de la matrice virale</term><term>Protéines membranaires</term><term>Signaux de triage des protéines</term><term>Structure tertiaire des protéines</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Coronavirus</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Coronavirus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Golgi Apparatus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Facteur-3 associé aux récepteurs de TNF</term><term>I-kappa B Kinase</term><term>Interféron de type I</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de la matrice virale</term><term>Protéines membranaires</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Immune Evasion</term><term>Immunity, Innate</term><term>Immunosuppression</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Cellules HeLa</term><term>Humains</term><term>Immunité innée</term><term>Immunosuppression thérapeutique</term><term>Échappement immunitaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses have developed various measures to evade innate immunity. We have previously shown that severe acute respiratory syndrome (SARS) coronavirus M protein suppresses type I interferon (IFN) production by impeding the formation of functional TRAF3-containing complex. In this study, we demonstrate that the IFN-antagonizing activity is specific to SARS coronavirus M protein and is mediated through its first transmembrane domain (TM1) located at the N terminus. M protein from human coronavirus HKU1 does not inhibit IFN production. Whereas N-linked glycosylation of SARS coronavirus M protein has no influence on IFN antagonism, TM1 is indispensable for the suppression of IFN production. TM1 targets SARS coronavirus M protein and heterologous proteins to the Golgi apparatus, yet Golgi localization is required but not sufficient for IFN antagonism. Mechanistically, TM1 is capable of binding with RIG-I, TRAF3, TBK1 and IKKε, and preventing the interaction of TRAF3 with its downstream effectors. Our work defines the molecular architecture of SARS coronavirus M protein required for suppression of innate antiviral response. </div></front></TEI><affiliations><list><country><li>Hong Kong</li></country></list><tree><country name="Hong Kong"><noRegion><name sortKey="Siu, Kam Leung" sort="Siu, Kam Leung" uniqKey="Siu K" first="Kam-Leung" last="Siu">Kam-Leung Siu</name></noRegion><name sortKey="Chan, Chi Ping" sort="Chan, Chi Ping" uniqKey="Chan C" first="Chi-Ping" last="Chan">Chi-Ping Chan</name><name sortKey="Chiu Yat Woo, Patrick" sort="Chiu Yat Woo, Patrick" uniqKey="Chiu Yat Woo P" first="Patrick" last="Chiu-Yat Woo">Patrick Chiu-Yat Woo</name><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</name><name sortKey="Kok, Kin Hang" sort="Kok, Kin Hang" uniqKey="Kok K" first="Kin-Hang" last="Kok">Kin-Hang Kok</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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