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

Previous study reported that the N protein of MHV could interact with the M (membrane) protein to help the envelopment of MHV nucleocapsid (7). By targeting RNA recombination, Ding, et al. found that the SR-rich region could not be transferred from MHV to BCoV (bovine coronavirus), which means that this region was unable to be substituted between various species (6). It is believed that the SR-rich region is possibly derived from the SR (or RS) domain of many RNA-binding proteins, such as SR proteins (6). The SR proteins are essential for constitutive mRNA splicing and the regulation of alternative splice site selection (8). The C-terminal SR domain of SR proteins is involved in mediating protein-protein interaction as well as nuclear localization 8., 9.. The SR-rich region might be necessary for the interaction of the N and M proteins. It also possibly contributes to the interaction of the N protein with other viral proteins, including the N protein itself.