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  • The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha.

The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha.

Journal of virology (2008-05-02)
Bing Zhou, Junli Liu, Qiuna Wang, Xuan Liu, Xiaorong Li, Ping Li, Qingjun Ma, Cheng Cao
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
α-Amanitin, from Amanita phalloides, ≥85% (HPLC), powder
Sigma-Aldrich
Heat Shock Protein 70 human, recombinant, expressed in E. coli, buffered aqueous solution, ≥90% (SDS-PAGE)