Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane.
Identifieur interne : 001C99 ( PubMed/Checkpoint ); précédent : 001C98; suivant : 001D00Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane.
Auteurs : Matthew Frieman [États-Unis] ; Boyd Yount ; Mark Heise ; Sarah A. Kopecky-Bromberg ; Peter Palese ; Ralph S. BaricSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Appareil de Golgi (génétique), Appareil de Golgi (immunologie), Appareil de Golgi (métabolisme), Cadres ouverts de lecture (physiologie), Cariophérines alpha (génétique), Cariophérines alpha (immunologie), Cariophérines alpha (métabolisme), Caryophérines bêta (génétique), Caryophérines bêta (immunologie), Caryophérines bêta (métabolisme), Cellules Caco-2, Cellules Vero, Facteur de transcription STAT-1 (génétique), Facteur de transcription STAT-1 (immunologie), Facteur de transcription STAT-1 (métabolisme), Humains, Immunité innée (génétique), Interférons (immunologie), Interférons (métabolisme), Mutation, Noyau de la cellule (génétique), Noyau de la cellule (immunologie), Noyau de la cellule (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (immunologie), Protéines recombinantes (métabolisme), Régulation de l'expression des gènes (génétique), Régulation de l'expression des gènes (immunologie), Réplication virale (physiologie), Réticulum endoplasmique (génétique), Réticulum endoplasmique (immunologie), Réticulum endoplasmique (métabolisme), Structure tertiaire des protéines (génétique), Transduction du signal (génétique), Transduction du signal (immunologie), Transport nucléaire actif (physiologie), Virus du SRAS (génétique), Virus du SRAS (immunologie), Virus du SRAS (métabolisme).
- MESH :
- génétique : Appareil de Golgi, Cariophérines alpha, Caryophérines bêta, Facteur de transcription STAT-1, Immunité innée, Noyau de la cellule, Protéines recombinantes, Régulation de l'expression des gènes, Réticulum endoplasmique, Structure tertiaire des protéines, Transduction du signal, Virus du SRAS.
- immunologie : Appareil de Golgi, Cariophérines alpha, Caryophérines bêta, Facteur de transcription STAT-1, Interférons, Noyau de la cellule, Protéines recombinantes, Régulation de l'expression des gènes, Réticulum endoplasmique, Transduction du signal, Virus du SRAS.
- métabolisme : Appareil de Golgi, Cariophérines alpha, Caryophérines bêta, Facteur de transcription STAT-1, Interférons, Noyau de la cellule, Protéines recombinantes, Réticulum endoplasmique, Virus du SRAS.
- physiologie : Cadres ouverts de lecture, Réplication virale, Transport nucléaire actif.
- Animaux, Cellules Caco-2, Cellules Vero, Humains, Mutation.
English descriptors
- KwdEn :
- Active Transport, Cell Nucleus (physiology), Animals, Caco-2 Cells, Cell Nucleus (genetics), Cell Nucleus (immunology), Cell Nucleus (metabolism), Chlorocebus aethiops, Endoplasmic Reticulum (genetics), Endoplasmic Reticulum (immunology), Endoplasmic Reticulum (metabolism), Gene Expression Regulation (genetics), Gene Expression Regulation (immunology), Golgi Apparatus (genetics), Golgi Apparatus (immunology), Golgi Apparatus (metabolism), Humans, Immunity, Innate (genetics), Interferons (immunology), Interferons (metabolism), Mutation, Open Reading Frames (physiology), Protein Structure, Tertiary (genetics), Recombinant Proteins (genetics), Recombinant Proteins (immunology), Recombinant Proteins (metabolism), SARS Virus (genetics), SARS Virus (immunology), SARS Virus (metabolism), STAT1 Transcription Factor (genetics), STAT1 Transcription Factor (immunology), STAT1 Transcription Factor (metabolism), Signal Transduction (genetics), Signal Transduction (immunology), Vero Cells, Virus Replication (physiology), alpha Karyopherins (genetics), alpha Karyopherins (immunology), alpha Karyopherins (metabolism), beta Karyopherins (genetics), beta Karyopherins (immunology), beta Karyopherins (metabolism).
- MESH :
- chemical , genetics : Recombinant Proteins, STAT1 Transcription Factor, alpha Karyopherins, beta Karyopherins.
- chemical , immunology : Interferons, Recombinant Proteins, STAT1 Transcription Factor, alpha Karyopherins, beta Karyopherins.
- genetics : Cell Nucleus, Endoplasmic Reticulum, Gene Expression Regulation, Golgi Apparatus, Immunity, Innate, Protein Structure, Tertiary, SARS Virus, Signal Transduction.
- immunology : Cell Nucleus, Endoplasmic Reticulum, Gene Expression Regulation, Golgi Apparatus, SARS Virus, Signal Transduction.
- metabolism : Cell Nucleus, Endoplasmic Reticulum, Golgi Apparatus, Interferons, Recombinant Proteins, SARS Virus, STAT1 Transcription Factor, alpha Karyopherins, beta Karyopherins.
- physiology : Active Transport, Cell Nucleus, Open Reading Frames, Virus Replication.
- Animals, Caco-2 Cells, Chlorocebus aethiops, Humans, Mutation, Vero Cells.
Abstract
The host innate immune response is an important deterrent of severe viral infection in humans and animals. Nuclear import factors function as key gatekeepers that regulate the transport of innate immune regulatory cargo to the nucleus of cells to activate the antiviral response. Using severe acute respiratory syndrome coronavirus (SARS-CoV) as a model, we demonstrate that SARS-COV ORF6 protein is localized to the endoplasmic reticulum (ER)/Golgi membrane in infected cells, where it binds to and disrupts nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane. Retention of import factors at the ER/Golgi membrane leads to a loss of STAT1 transport into the nucleus in response to interferon signaling, thus blocking the expression of STAT1-activated genes that establish an antiviral state. We mapped the region of ORF6, which binds karyopherin alpha 2, to the C terminus of ORF6 and show that mutations in the C terminus no longer bind karyopherin alpha 2 or block the nuclear import of STAT1. We also show that N-terminal deletions of karyopherin alpha 2 that no longer bind to karyopherin beta 1 still retain ORF6 binding activity but no longer block STAT1 nuclear import. Recombinant SARS-CoV lacking ORF6 did not tether karyopherin alpha 2 to the ER/Golgi membrane and allowed the import of the STAT1 complex into the nucleus. We discuss the likely implications of these data on SARS-CoV replication and pathogenesis.
DOI: 10.1128/JVI.01012-07
PubMed: 17596301
Affiliations:
- États-Unis
- Caroline du Nord
- Chapel Hill (Caroline du Nord)
- Université de Caroline du Nord à Chapel Hill
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:17596301Le document en format XML
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(immunology)</term><term>Interferons (metabolism)</term><term>Mutation</term><term>Open Reading Frames (physiology)</term><term>Protein Structure, Tertiary (genetics)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (immunology)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (genetics)</term><term>SARS Virus (immunology)</term><term>SARS Virus (metabolism)</term><term>STAT1 Transcription Factor (genetics)</term><term>STAT1 Transcription Factor (immunology)</term><term>STAT1 Transcription Factor (metabolism)</term><term>Signal Transduction (genetics)</term><term>Signal Transduction (immunology)</term><term>Vero Cells</term><term>Virus Replication (physiology)</term><term>alpha Karyopherins (genetics)</term><term>alpha Karyopherins (immunology)</term><term>alpha Karyopherins (metabolism)</term><term>beta Karyopherins (genetics)</term><term>beta Karyopherins (immunology)</term><term>beta Karyopherins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Appareil de Golgi (génétique)</term><term>Appareil de Golgi (immunologie)</term><term>Appareil de Golgi (métabolisme)</term><term>Cadres ouverts de lecture (physiologie)</term><term>Cariophérines alpha (génétique)</term><term>Cariophérines alpha (immunologie)</term><term>Cariophérines alpha (métabolisme)</term><term>Caryophérines bêta (génétique)</term><term>Caryophérines bêta (immunologie)</term><term>Caryophérines bêta (métabolisme)</term><term>Cellules Caco-2</term><term>Cellules Vero</term><term>Facteur de transcription STAT-1 (génétique)</term><term>Facteur de transcription STAT-1 (immunologie)</term><term>Facteur de transcription STAT-1 (métabolisme)</term><term>Humains</term><term>Immunité innée (génétique)</term><term>Interférons (immunologie)</term><term>Interférons (métabolisme)</term><term>Mutation</term><term>Noyau de la cellule (génétique)</term><term>Noyau de la cellule (immunologie)</term><term>Noyau de la cellule (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (immunologie)</term><term>Protéines recombinantes (métabolisme)</term><term>Régulation de l'expression des gènes (génétique)</term><term>Régulation de l'expression des gènes (immunologie)</term><term>Réplication virale (physiologie)</term><term>Réticulum endoplasmique (génétique)</term><term>Réticulum endoplasmique (immunologie)</term><term>Réticulum endoplasmique (métabolisme)</term><term>Structure tertiaire des protéines (génétique)</term><term>Transduction du signal (génétique)</term><term>Transduction du signal (immunologie)</term><term>Transport nucléaire actif (physiologie)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (immunologie)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Proteins</term><term>STAT1 Transcription Factor</term><term>alpha Karyopherins</term><term>beta Karyopherins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Interferons</term><term>Recombinant Proteins</term><term>STAT1 Transcription Factor</term><term>alpha Karyopherins</term><term>beta Karyopherins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cell Nucleus</term><term>Endoplasmic Reticulum</term><term>Gene Expression Regulation</term><term>Golgi Apparatus</term><term>Immunity, Innate</term><term>Protein Structure, Tertiary</term><term>SARS Virus</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Appareil de Golgi</term><term>Cariophérines alpha</term><term>Caryophérines bêta</term><term>Facteur de transcription STAT-1</term><term>Immunité innée</term><term>Noyau de la cellule</term><term>Protéines recombinantes</term><term>Régulation de l'expression des gènes</term><term>Réticulum endoplasmique</term><term>Structure tertiaire des protéines</term><term>Transduction du signal</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Appareil de Golgi</term><term>Cariophérines alpha</term><term>Caryophérines bêta</term><term>Facteur de transcription STAT-1</term><term>Interférons</term><term>Noyau de la cellule</term><term>Protéines recombinantes</term><term>Régulation de l'expression des gènes</term><term>Réticulum endoplasmique</term><term>Transduction du signal</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cell Nucleus</term><term>Endoplasmic Reticulum</term><term>Gene Expression Regulation</term><term>Golgi Apparatus</term><term>SARS Virus</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Endoplasmic Reticulum</term><term>Golgi Apparatus</term><term>Interferons</term><term>Recombinant Proteins</term><term>SARS Virus</term><term>STAT1 Transcription Factor</term><term>alpha Karyopherins</term><term>beta Karyopherins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Cariophérines alpha</term><term>Caryophérines bêta</term><term>Facteur de transcription STAT-1</term><term>Interférons</term><term>Noyau de la cellule</term><term>Protéines recombinantes</term><term>Réticulum endoplasmique</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cadres ouverts de lecture</term><term>Réplication virale</term><term>Transport nucléaire actif</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Active Transport, Cell Nucleus</term><term>Open Reading Frames</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Caco-2 Cells</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Mutation</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Caco-2</term><term>Cellules Vero</term><term>Humains</term><term>Mutation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The host innate immune response is an important deterrent of severe viral infection in humans and animals. Nuclear import factors function as key gatekeepers that regulate the transport of innate immune regulatory cargo to the nucleus of cells to activate the antiviral response. Using severe acute respiratory syndrome coronavirus (SARS-CoV) as a model, we demonstrate that SARS-COV ORF6 protein is localized to the endoplasmic reticulum (ER)/Golgi membrane in infected cells, where it binds to and disrupts nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane. Retention of import factors at the ER/Golgi membrane leads to a loss of STAT1 transport into the nucleus in response to interferon signaling, thus blocking the expression of STAT1-activated genes that establish an antiviral state. We mapped the region of ORF6, which binds karyopherin alpha 2, to the C terminus of ORF6 and show that mutations in the C terminus no longer bind karyopherin alpha 2 or block the nuclear import of STAT1. We also show that N-terminal deletions of karyopherin alpha 2 that no longer bind to karyopherin beta 1 still retain ORF6 binding activity but no longer block STAT1 nuclear import. Recombinant SARS-CoV lacking ORF6 did not tether karyopherin alpha 2 to the ER/Golgi membrane and allowed the import of the STAT1 complex into the nucleus. We discuss the likely implications of these data on SARS-CoV replication and pathogenesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17596301</PMID><DateCompleted><Year>2007</Year><Month>10</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>81</Volume><Issue>18</Issue><PubDate><Year>2007</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane.</ArticleTitle><Pagination><MedlinePgn>9812-24</MedlinePgn></Pagination><Abstract><AbstractText>The host innate immune response is an important deterrent of severe viral infection in humans and animals. Nuclear import factors function as key gatekeepers that regulate the transport of innate immune regulatory cargo to the nucleus of cells to activate the antiviral response. Using severe acute respiratory syndrome coronavirus (SARS-CoV) as a model, we demonstrate that SARS-COV ORF6 protein is localized to the endoplasmic reticulum (ER)/Golgi membrane in infected cells, where it binds to and disrupts nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane. Retention of import factors at the ER/Golgi membrane leads to a loss of STAT1 transport into the nucleus in response to interferon signaling, thus blocking the expression of STAT1-activated genes that establish an antiviral state. We mapped the region of ORF6, which binds karyopherin alpha 2, to the C terminus of ORF6 and show that mutations in the C terminus no longer bind karyopherin alpha 2 or block the nuclear import of STAT1. We also show that N-terminal deletions of karyopherin alpha 2 that no longer bind to karyopherin beta 1 still retain ORF6 binding activity but no longer block STAT1 nuclear import. Recombinant SARS-CoV lacking ORF6 did not tether karyopherin alpha 2 to the ER/Golgi membrane and allowed the import of the STAT1 complex into the nucleus. We discuss the likely implications of these data on SARS-CoV replication and pathogenesis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Frieman</LastName><ForeName>Matthew</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Epidemiology, School of Public Health, University of North Carolina at Chapel Hill, 3304 Hooker Research Center, Chapel Hill, NC 27599-7435, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yount</LastName><ForeName>Boyd</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Heise</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kopecky-Bromberg</LastName><ForeName>Sarah A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Palese</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Baric</LastName><ForeName>Ralph S</ForeName><Initials>RS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>F32 AI066542</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI059443</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>F32 AI 066542</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI 059443-02</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>06</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C490630">KPNA2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C424166">KPNB1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050794">STAT1 Transcription Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C494079">STAT1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D028901">alpha Karyopherins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D028961">beta Karyopherins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9008-11-1</RegistryNumber><NameOfSubstance UI="D007372">Interferons</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D021581" MajorTopicYN="N">Active Transport, Cell Nucleus</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018938" MajorTopicYN="N">Caco-2 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002522" 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