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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...
Autores principales: | , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2003
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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. |
format | Online Article Text |
id | pubmed-5172421 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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