The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha.
Identifieur interne : 001B57 ( PubMed/Corpus ); précédent : 001B56; suivant : 001B58The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha.
Auteurs : Bing Zhou ; Junli Liu ; Qiuna Wang ; Xuan Liu ; Xiaorong Li ; Ping Li ; Qingjun Ma ; Cheng CaoSource :
- Journal of virology [ 1098-5514 ] ; 2008.
English descriptors
- KwdEn :
- Actins (metabolism), Blotting, Far-Western, Cell Line, Cell Proliferation, Cytokinesis (physiology), Humans, Immunoprecipitation, Lymphocytes (virology), Nucleocapsid Proteins (metabolism), Peptide Elongation Factor 1 (metabolism), Protein Binding, Protein Biosynthesis (physiology), Protein Interaction Mapping, SARS Virus (physiology), Surface Plasmon Resonance, Two-Hybrid System Techniques.
- MESH :
- chemical , metabolism : Actins, Nucleocapsid Proteins, Peptide Elongation Factor 1.
- physiology : Cytokinesis, Protein Biosynthesis, SARS Virus.
- virology : Lymphocytes.
- Blotting, Far-Western, Cell Line, Cell Proliferation, Humans, Immunoprecipitation, Protein Binding, Protein Interaction Mapping, Surface Plasmon Resonance, Two-Hybrid System Techniques.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of SARS, an emerging disease characterized by atypical pneumonia. Using a yeast two-hybrid screen with the nucleocapsid (N) protein of SARS-CoV as a bait, the C terminus (amino acids 251 to 422) of the N protein was found to interact with human elongation factor 1-alpha (EF1alpha), an essential component of the translational machinery with an important role in cytokinesis, promoting the bundling of filamentous actin (F-actin). In vitro and in vivo interaction was then confirmed by immuno-coprecipitation, far-Western blotting, and surface plasmon resonance. It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1alpha, inhibiting protein translation and cytokinesis by blocking F-actin bundling. Proliferation of human peripheral blood lymphocytes and other human cell lines was significantly inhibited by the infection of recombinant retrovirus expressing SARS-CoV N protein.
DOI: 10.1128/JVI.00133-08
PubMed: 18448518
Links to Exploration step
pubmed:18448518Le document en format XML
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of SARS, an emerging disease characterized by atypical pneumonia. Using a yeast two-hybrid screen with the nucleocapsid (N) protein of SARS-CoV as a bait, the C terminus (amino acids 251 to 422) of the N protein was found to interact with human elongation factor 1-alpha (EF1alpha), an essential component of the translational machinery with an important role in cytokinesis, promoting the bundling of filamentous actin (F-actin). In vitro and in vivo interaction was then confirmed by immuno-coprecipitation, far-Western blotting, and surface plasmon resonance. It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1alpha, inhibiting protein translation and cytokinesis by blocking F-actin bundling. Proliferation of human peripheral blood lymphocytes and other human cell lines was significantly inhibited by the infection of recombinant retrovirus expressing SARS-CoV N protein.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of SARS, an emerging disease characterized by atypical pneumonia. Using a yeast two-hybrid screen with the nucleocapsid (N) protein of SARS-CoV as a bait, the C terminus (amino acids 251 to 422) of the N protein was found to interact with human elongation factor 1-alpha (EF1alpha), an essential component of the translational machinery with an important role in cytokinesis, promoting the bundling of filamentous actin (F-actin). In vitro and in vivo interaction was then confirmed by immuno-coprecipitation, far-Western blotting, and surface plasmon resonance. It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1alpha, inhibiting protein translation and cytokinesis by blocking F-actin bundling. Proliferation of human peripheral blood lymphocytes and other human cell lines was significantly inhibited by the infection of recombinant retrovirus expressing SARS-CoV N protein.</AbstractText>
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