Key result
The SARS-CoV nucleocapsid protein binds directly to human elongation factor 1-alpha, inducing its aggregation and thereby inhibiting protein translation, cell cytokinesis, and cell proliferation.
The SARS-CoV nucleocapsid protein inhibits host cell cytokinesis and proliferation by interacting with and aggregating translation elongation factor 1-alpha.
Suggests a novel mechanism of SARS-CoV cytopathogenicity; leaves open relevance to human disease and therapeutic targeting.
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.
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Zhou et al. (2008) studied SARS-CoV infection mechanisms. SARS-CoV Nucleocapsid (N) protein expression vs. Control vectors or uninfected cells was evaluated on Cell cytokinesis, proliferation, and protein translation. The SARS-CoV nucleocapsid protein binds directly to human elongation factor 1-alpha, inducing its aggregation and thereby inhibiting protein translation, cell cytokinesis, and cell proliferation.
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