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J. Biol. Chem., Vol. 280, Issue 24, 23280-23286, June 17, 2005

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Recombinant Severe Acute Respiratory Syndrome (SARS) Coronavirus Nucleocapsid Protein Forms a Dimer through Its C-terminal Domain^*

I-Mei Yu, Christin L. T. Gustafson, Jianbo Diao, John W. Burgner, II, Zhihong Li¶, Jingqiang Zhang¶, and Jue Chen||

From the Department of Biological Sciences and the Cancer Center, Bindley Biosciences Center, Purdue University, West Lafayette, Indiana 47907 and the ^¶State Key Laboratory for Biocontrol, Zhongshan University, Guangzhou, People's Republic of China

The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The viral nucleocapsid (N) protein plays an essential role in viral RNA packaging. In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking. Dimeric N proteins self-associate into tetramers and higher molecular weight oligomers at high concentrations. The dimerization domain of N was mapped through studies of the oligomeric states of several truncated mutants. Although mutants consisting of residues 1–210 and 1–284 fold as monomers, constructs consisting of residues 211–422 and 285–422 efficiently form dimers. When in excess, the truncated construct 285–422 inhibits the homodimerization of full-length N protein by forming a heterodimer with the full-length N protein. These results suggest that the N protein oligomerization involves the C-terminal residues 285–422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly.

Received for publication, January 27, 2005 , and in revised form, April 19, 2005.

^* This work was supported by the Pew Scholarship (to J. C.) and the SARS Research Foundation of Guangdong Province (to J. Z.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Dept. of Biological Sciences, Purdue University, West Lafayette, IN 47907-1393. Tel.: 765-496-3113; Fax: 765-496-1189; E-mail: chenjue{at}purdue.edu.

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