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

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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172421/
https://www.ncbi.nlm.nih.gov/pubmed/15626344
http://dx.doi.org/10.1016/S1672-0229(03)01018-0
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author 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
author_facet 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
author_sort Wang, Jingqiang
collection PubMed
description 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.
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spelling pubmed-51724212016-12-23 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 Genomics Proteomics Bioinformatics Invited Article 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. Elsevier 2003-05 2016-11-28 /pmc/articles/PMC5172421/ /pubmed/15626344 http://dx.doi.org/10.1016/S1672-0229(03)01018-0 Text en . http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Invited Article
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 Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
title The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
title_full The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
title_fullStr The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
title_full_unstemmed The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
title_short The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV
title_sort structure analysis and antigenicity study of the n protein of sars-cov
topic Invited Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172421/
https://www.ncbi.nlm.nih.gov/pubmed/15626344
http://dx.doi.org/10.1016/S1672-0229(03)01018-0
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