The structure analysis and antigenicity study of the N protein of SARS-CoV.

Autor: Wang J; Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China., Ji J, Ye J, Zhao X, Wen J, Li W, Hu J, Li D, Sun M, Zeng H, Hu Y, Tian X, Tan X, Xu N, Zeng C, Wang J, Bi S, Yang H
Jazyk: angličtina
Zdroj: Genomics, proteomics & bioinformatics [Genomics Proteomics Bioinformatics] 2003 May; Vol. 1 (2), pp. 145-54.
DOI: 10.1016/s1672-0229(03)01018-0
Abstrakt: 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.
Databáze: MEDLINE