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The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV 被引量:4
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作者 JingqiangWang JiaJi +15 位作者 JiaYe XiaoqianZhao JieWen WeiLi JianfeiHu DaweiLi MinSun HaipanZeng YongwuHu XiangjunTian XuehaiTan ningzhixu ChangqingZeng JianWang ShengliBi HuanmingYang 《Genomics, Proteomics & Bioinformatics》 SCIE CAS CSCD 2003年第2期145-154,共10页
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 th... 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. 展开更多
关键词 SARS-COV NUCLEOPROTEIN PHOSPHORYLATION SR-rich region antigenic sites
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