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The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04
The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from B...
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/PMC5172245/ https://www.ncbi.nlm.nih.gov/pubmed/15626345 http://dx.doi.org/10.1016/S1672-0229(03)01019-2 |
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author | Xu, Zuyuan Zhang, Haiqing Tian, Xiangjun Ji, Jia Li, Wei Li, Yan Tian, Wei Han, Yujun Wang, Lili Zhang, Zizhang Xu, Jing Wei, Wei Zhu, Jingui Sun, Haiyan Zhang, Xiaowei Zhou, Jun Li, Songgang Wang, Jun Wang, Jian Bi, Shengli Yang, Huanming |
author_facet | Xu, Zuyuan Zhang, Haiqing Tian, Xiangjun Ji, Jia Li, Wei Li, Yan Tian, Wei Han, Yujun Wang, Lili Zhang, Zizhang Xu, Jing Wei, Wei Zhu, Jingui Sun, Haiyan Zhang, Xiaowei Zhou, Jun Li, Songgang Wang, Jun Wang, Jian Bi, Shengli Yang, Huanming |
author_sort | Xu, Zuyuan |
collection | PubMed |
description | The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phylogeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS. |
format | Online Article Text |
id | pubmed-5172245 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-51722452016-12-23 The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 Xu, Zuyuan Zhang, Haiqing Tian, Xiangjun Ji, Jia Li, Wei Li, Yan Tian, Wei Han, Yujun Wang, Lili Zhang, Zizhang Xu, Jing Wei, Wei Zhu, Jingui Sun, Haiyan Zhang, Xiaowei Zhou, Jun Li, Songgang Wang, Jun Wang, Jian Bi, Shengli Yang, Huanming Genomics Proteomics Bioinformatics Invited Article The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phylogeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS. Elsevier 2003-05 2016-11-28 /pmc/articles/PMC5172245/ /pubmed/15626345 http://dx.doi.org/10.1016/S1672-0229(03)01019-2 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 Xu, Zuyuan Zhang, Haiqing Tian, Xiangjun Ji, Jia Li, Wei Li, Yan Tian, Wei Han, Yujun Wang, Lili Zhang, Zizhang Xu, Jing Wei, Wei Zhu, Jingui Sun, Haiyan Zhang, Xiaowei Zhou, Jun Li, Songgang Wang, Jun Wang, Jian Bi, Shengli Yang, Huanming The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 |
title | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 |
title_full | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 |
title_fullStr | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 |
title_full_unstemmed | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 |
title_short | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 |
title_sort | r protein of sars-cov: analyses of structure and function based on four complete genome sequences of isolates bj01-bj04 |
topic | Invited Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172245/ https://www.ncbi.nlm.nih.gov/pubmed/15626345 http://dx.doi.org/10.1016/S1672-0229(03)01019-2 |
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