Severe acute respiratory syndrome coronavirus protein 6 mediates ubiquitin-dependent proteosomal degradation of N-Myc (and STAT) interactor.
Identifieur interne : 000E27 ( PubMed/Curation ); précédent : 000E26; suivant : 000E28Severe acute respiratory syndrome coronavirus protein 6 mediates ubiquitin-dependent proteosomal degradation of N-Myc (and STAT) interactor.
Auteurs : Weijia Cheng [République populaire de Chine] ; Shiyou Chen ; Ruiling Li ; Yu Chen ; Min Wang ; Deyin GuoSource :
- Virologica Sinica [ 1995-820X ] ; 2015.
Descripteurs français
- KwdFr :
- Banque de gènes, Cartographie d'interactions entre protéines, Humains, Interactions hôte-pathogène, Liaison aux protéines, Protéines et peptides de signalisation intracellulaire (métabolisme), Protéines virales (métabolisme), Protéolyse, Techniques de double hybride, Ubiquitine (métabolisme), Virus du SRAS (physiologie).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Intracellular Signaling Peptides and Proteins, Ubiquitin, Viral Proteins.
- physiology : SARS Virus.
- Gene Library, Host-Pathogen Interactions, Humans, Protein Binding, Protein Interaction Mapping, Proteolysis, Two-Hybrid System Techniques.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes eight accessory proteins, the functions of which are not yet fully understood. SARS-CoV protein 6 (P6) is one of the previously studied accessory proteins that have been documented to enhance viral replication and suppress host interferon (IFN) signaling pathways. Through yeast two-hybrid screening, we identified eight potential cellular P6-interacting proteins from a human spleen cDNA library. For further investigation, we targeted the IFN signaling pathway-mediating protein, N-Myc (and STAT) interactor (Nmi). Its interaction with P6 was confirmed within cells. The results showed that P6 can promote the ubiquitin-dependent proteosomal degradation of Nmi. This study revealed a new mechanism of SARS-CoV P6 in limiting the IFN signaling to promote SARS-CoV survival in host cells.
DOI: 10.1007/s12250-015-3581-8
PubMed: 25907116
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uniqKey="Guo D" first="Deyin" last="Guo">Deyin Guo</name></author></analytic><series><title level="j">Virologica Sinica</title><idno type="eISSN">1995-820X</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Gene Library</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Intracellular Signaling Peptides and Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Interaction Mapping</term><term>Proteolysis</term><term>SARS Virus (physiology)</term><term>Two-Hybrid System Techniques</term><term>Ubiquitin (metabolism)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Banque de gènes</term><term>Cartographie d'interactions entre protéines</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Protéines et peptides de signalisation intracellulaire (métabolisme)</term><term>Protéines virales (métabolisme)</term><term>Protéolyse</term><term>Techniques de double hybride</term><term>Ubiquitine (métabolisme)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Intracellular Signaling Peptides and Proteins</term><term>Ubiquitin</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines et peptides de signalisation intracellulaire</term><term>Protéines virales</term><term>Ubiquitine</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Library</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Protein Binding</term><term>Protein Interaction Mapping</term><term>Proteolysis</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Banque de gènes</term><term>Cartographie d'interactions entre protéines</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Protéolyse</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes eight accessory proteins, the functions of which are not yet fully understood. SARS-CoV protein 6 (P6) is one of the previously studied accessory proteins that have been documented to enhance viral replication and suppress host interferon (IFN) signaling pathways. Through yeast two-hybrid screening, we identified eight potential cellular P6-interacting proteins from a human spleen cDNA library. For further investigation, we targeted the IFN signaling pathway-mediating protein, N-Myc (and STAT) interactor (Nmi). Its interaction with P6 was confirmed within cells. The results showed that P6 can promote the ubiquitin-dependent proteosomal degradation of Nmi. This study revealed a new mechanism of SARS-CoV P6 in limiting the IFN signaling to promote SARS-CoV survival in host cells. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25907116</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1995-820X</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>2</Issue><PubDate><Year>2015</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Virologica Sinica</Title><ISOAbbreviation>Virol Sin</ISOAbbreviation></Journal><ArticleTitle>Severe acute respiratory syndrome coronavirus protein 6 mediates ubiquitin-dependent proteosomal degradation of N-Myc (and STAT) interactor.</ArticleTitle><Pagination><MedlinePgn>153-61</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12250-015-3581-8</ELocationID><Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes eight accessory proteins, the functions of which are not yet fully understood. SARS-CoV protein 6 (P6) is one of the previously studied accessory proteins that have been documented to enhance viral replication and suppress host interferon (IFN) signaling pathways. Through yeast two-hybrid screening, we identified eight potential cellular P6-interacting proteins from a human spleen cDNA library. For further investigation, we targeted the IFN signaling pathway-mediating protein, N-Myc (and STAT) interactor (Nmi). Its interaction with P6 was confirmed within cells. The results showed that P6 can promote the ubiquitin-dependent proteosomal degradation of Nmi. 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