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Journal of Virology, July 2008, p. 6962-6971, Vol. 82, No. 14
0022-538X/08/$08.00+0 doi:10.1128/JVI.00133-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Junli Liu,
Qiuna Wang,
Xuan Liu,
Xiaorong Li,
Ping Li,
Qingjun Ma, and
Cheng Cao*
State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Biotechnology, Beijing 100071, China
Received 18 January 2008/ Accepted 24 April 2008
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 (EF1
), 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 EF1
, 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.
Published ahead of print on 30 April 2008.
B.Z. and J.L. contributed equally to this work.
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