1. The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
- Author
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Wang, Jingqiang, Ji, Jia, Ye, Jia, Zhao, Xiaoqian, Wen, Jie, Li, Wei, Hu, Jianfei, Li, Dawei, Sun, Min, Zeng, Haipan, Hu, Yongwu, Tian, Xiangjun, Tan, Xuehai, Xu, Ningzhi, Zeng, Changqing, Wang, Jian, Bi, Shengli, and Yang, Huanming
- Abstract
The Coronaviridaefamily is characterized by a nucleocapsid that is composed of the genome RNA molecule in combination with the nucleoprotein (N protein) within a virion. The most striking physiochemical feature of the N protein of SARS-CoV is that it is a typical basic protein with a high predicted pI and high hydrophilicity, which is consistent with its function of binding to the ribophosphate backbone of the RNA molecule. The predicted high extent of phosphorylation of the N protein on multiple candidate phosphorylation sites demonstrates that it would be related to important functions, such as RNA-binding and localization to the nucleolus of host cells. Subsequent study shows that there is an SR-rich region in the N protein and this region might be involved in the protein-protein interaction. The abundant antigenic sites predicted in the N protein, as well as experimental evidence with synthesized polypeptides, indicate that the N protein is one of the major antigens of the SARS-CoV. Compared with other viral structural proteins, the low variation rate of the N protein with regards to its size suggests its importance to the survival of the virus.
- Published
- 2003
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