The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV

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; Yang, Huanming

The Coronaviridae family 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.