Severe acute respiratory syndrome coronavirus protein 6 mediates ubiquitin-dependent proteosomal degradation of N-Myc (and STAT) interactor.
Identifieur interne : 001244 ( Main/Exploration ); précédent : 001243; suivant : 001245Severe 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
Affiliations:
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Le document en format XML
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<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>
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<name sortKey="Guo, Deyin" sort="Guo, Deyin" uniqKey="Guo D" first="Deyin" last="Guo">Deyin Guo</name>
<name sortKey="Li, Ruiling" sort="Li, Ruiling" uniqKey="Li R" first="Ruiling" last="Li">Ruiling Li</name>
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