Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.
Identifieur interne : 002826 ( Ncbi/Merge ); précédent : 002825; suivant : 002827Suppression 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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001052
- to stream PubMed, to step Curation: 001052
- to stream PubMed, to step Checkpoint: 000F19
Links to Exploration step
pubmed:24509444Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.</title><author><name sortKey="Siu, Kam Leung" sort="Siu, Kam Leung" uniqKey="Siu K" first="Kam-Leung" last="Siu">Kam-Leung Siu</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="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 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="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><affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology, The University of Hong Kong, Pokfulam, Hong Kong.</nlm:affiliation><country xml:lang="fr">Hong Kong</country><wicri:regionArea>Department of Microbiology, The University of Hong Kong, Pokfulam</wicri:regionArea><wicri:noRegion>Pokfulam</wicri:noRegion></affiliation></author><author><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24509444</idno><idno type="pmid">24509444</idno><idno type="doi">10.1038/cmi.2013.61</idno><idno type="wicri:Area/PubMed/Corpus">001052</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001052</idno><idno type="wicri:Area/PubMed/Curation">001052</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001052</idno><idno type="wicri:Area/PubMed/Checkpoint">000F19</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000F19</idno><idno type="wicri:Area/Ncbi/Merge">002826</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.</title><author><name sortKey="Siu, Kam Leung" sort="Siu, Kam Leung" uniqKey="Siu K" first="Kam-Leung" last="Siu">Kam-Leung Siu</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="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 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="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><affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology, The University of Hong Kong, Pokfulam, Hong Kong.</nlm:affiliation><country xml:lang="fr">Hong Kong</country><wicri:regionArea>Department of Microbiology, The University of Hong Kong, Pokfulam</wicri:regionArea><wicri:noRegion>Pokfulam</wicri:noRegion></affiliation></author><author><name sortKey="Jin, Dong Yan" sort="Jin, Dong Yan" uniqKey="Jin D" first="Dong-Yan" last="Jin">Dong-Yan Jin</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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24509444</PMID><DateCompleted><Year>2014</Year><Month>11</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2042-0226</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>2</Issue><PubDate><Year>2014</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Cellular & molecular immunology</Title><ISOAbbreviation>Cell. Mol. Immunol.</ISOAbbreviation></Journal><ArticleTitle>Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.</ArticleTitle><Pagination><MedlinePgn>141-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/cmi.2013.61</ELocationID><Abstract><AbstractText>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. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Siu</LastName><ForeName>Kam-Leung</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>Chi-Ping</ForeName><Initials>CP</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kok</LastName><ForeName>Kin-Hang</ForeName><Initials>KH</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chiu-Yat Woo</LastName><ForeName>Patrick</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Microbiology, The University of Hong Kong, Pokfulam, Hong Kong.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Dong-Yan</ForeName><Initials>DY</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>02</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>China</Country><MedlineTA>Cell Mol Immunol</MedlineTA><NlmUniqueID>101242872</NlmUniqueID><ISSNLinking>1672-7681</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007370">Interferon Type I</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021382">Protein Sorting Signals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048008">TNF Receptor-Associated Factor 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>108502-71-2</RegistryNumber><NameOfSubstance UI="C067997">M protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C403191">TBK1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.10</RegistryNumber><NameOfSubstance UI="D051550">I-kappa B Kinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017934" MajorTopicYN="N">Coronavirus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006056" MajorTopicYN="N">Golgi Apparatus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051550" MajorTopicYN="N">I-kappa B Kinase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057131" MajorTopicYN="N">Immune Evasion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007113" MajorTopicYN="N">Immunity, Innate</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007165" MajorTopicYN="N">Immunosuppression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007370" MajorTopicYN="N">Interferon Type I</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="N">Membrane Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021382" MajorTopicYN="N">Protein Sorting Signals</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D048008" MajorTopicYN="N">TNF Receptor-Associated Factor 3</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014763" MajorTopicYN="N">Viral Matrix Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>08</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>11</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>11</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>2</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>2</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>11</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24509444</ArticleId><ArticleId IdType="pii">cmi201361</ArticleId><ArticleId IdType="doi">10.1038/cmi.2013.61</ArticleId><ArticleId IdType="pmc">PMC4003381</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Formos Med Assoc. 2013 Jul;112(7):372-81</Citation><ArticleIdList><ArticleId IdType="pubmed">23883791</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Host Microbe. 2011 Apr 21;9(4):299-309</Citation><ArticleIdList><ArticleId IdType="pubmed">21501829</ArticleId></ArticleIdList></Reference><Reference><Citation>J Clin Microbiol. 2006 Jun;44(6):2063-71</Citation><ArticleIdList><ArticleId IdType="pubmed">16757599</ArticleId></ArticleIdList></Reference><Reference><Citation>Immunity. 2013 May 23;38(5):855-69</Citation><ArticleIdList><ArticleId IdType="pubmed">23706667</ArticleId></ArticleIdList></Reference><Reference><Citation>Viruses. 2009 Jun;1(1):57-71</Citation><ArticleIdList><ArticleId IdType="pubmed">21994538</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Microbiol. 2007 May;15(5):211-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17398101</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Biosci. 2014 Jan 13;4(1):3</Citation><ArticleIdList><ArticleId IdType="pubmed">24410900</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2009 Jun 12;284(24):16202-9</Citation><ArticleIdList><ArticleId IdType="pubmed">19380580</ArticleId></ArticleIdList></Reference><Reference><Citation>Virol J. 2009;6:79</Citation><ArticleIdList><ArticleId IdType="pubmed">19534833</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Jan;79(2):884-95</Citation><ArticleIdList><ArticleId IdType="pubmed">15613317</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2013;8(7):e70129</Citation><ArticleIdList><ArticleId IdType="pubmed">23894604</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 2008 Jan;89(Pt 1):1-47</Citation><ArticleIdList><ArticleId IdType="pubmed">18089727</ArticleId></ArticleIdList></Reference><Reference><Citation>N Engl J Med. 2012 Nov 8;367(19):1814-20</Citation><ArticleIdList><ArticleId IdType="pubmed">23075143</ArticleId></ArticleIdList></Reference><Reference><Citation>BMC Infect Dis. 2012;12:365</Citation><ArticleIdList><ArticleId IdType="pubmed">23256846</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2013 Jun;87(11):6081-90</Citation><ArticleIdList><ArticleId IdType="pubmed">23427150</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 2009 Sep;90(Pt 9):2107-13</Citation><ArticleIdList><ArticleId IdType="pubmed">19423547</ArticleId></ArticleIdList></Reference><Reference><Citation>Cancer Res. 2007 Feb 1;67(3):1072-81</Citation><ArticleIdList><ArticleId IdType="pubmed">17283140</ArticleId></ArticleIdList></Reference><Reference><Citation>Retrovirology. 2013;10:40</Citation><ArticleIdList><ArticleId IdType="pubmed">23577667</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Mar;80(5):2326-36</Citation><ArticleIdList><ArticleId IdType="pubmed">16474139</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Immunol. 2004 Jul;5(7):730-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15208624</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Microbiol Rev. 2007 Oct;20(4):660-94</Citation><ArticleIdList><ArticleId IdType="pubmed">17934078</ArticleId></ArticleIdList></Reference><Reference><Citation>Lancet. 2003 Apr 19;361(9366):1319-25</Citation><ArticleIdList><ArticleId IdType="pubmed">12711465</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Cell Biol. 2006 Jul;8(7):717-24</Citation><ArticleIdList><ArticleId IdType="pubmed">16767081</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2013 Oct;1833(10):2165-75</Citation><ArticleIdList><ArticleId IdType="pubmed">23665047</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 1995 Dec;131(6 Pt 2):1715-26</Citation><ArticleIdList><ArticleId IdType="pubmed">8557739</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Virol. 2012 Jun;2(3):264-75</Citation><ArticleIdList><ArticleId IdType="pubmed">22572391</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2013 Nov;87(22):12489-95</Citation><ArticleIdList><ArticleId IdType="pubmed">24027320</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1994 Jan 21;263(5145):387-90</Citation><ArticleIdList><ArticleId IdType="pubmed">8278814</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Nov;82(22):11318-30</Citation><ArticleIdList><ArticleId IdType="pubmed">18753196</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1998 Jan 30;273(5):2714-20</Citation><ArticleIdList><ArticleId IdType="pubmed">9446577</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2000 Feb;74(3):1061-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10627515</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Biol. 2011 Jul 12;21(13):R488-93</Citation><ArticleIdList><ArticleId IdType="pubmed">21741580</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2010 Nov;84(21):11255-63</Citation><ArticleIdList><ArticleId IdType="pubmed">20719951</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2007 Apr 20;282(16):11817-26</Citation><ArticleIdList><ArticleId IdType="pubmed">17327220</ArticleId></ArticleIdList></Reference><Reference><Citation>J Immunol. 2011 Dec 15;187(12):6473-82</Citation><ArticleIdList><ArticleId IdType="pubmed">22079989</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2014 May;88(9):4866-76</Citation><ArticleIdList><ArticleId IdType="pubmed">24522921</ArticleId></ArticleIdList></Reference><Reference><Citation>Immunity. 2002 Sep;17(3):251-63</Citation><ArticleIdList><ArticleId IdType="pubmed">12354379</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><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)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002826 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 002826 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Ncbi
|étape= Merge
|type= RBID
|clé= pubmed:24509444
|texte= Suppression of innate antiviral response by severe acute respiratory syndrome coronavirus M protein is mediated through the first transmembrane domain.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:24509444" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |