Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein
Abstract The newly emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in a global human health crisis. The CoV nucleocapsid (N) protein plays essential roles both in the viral genomic RNA packaging and the regulation of host cellular machinery. Here, to contribute to...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Springer
2020-08-01
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| Series: | Molecular Biomedicine |
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| Online Access: | https://doi.org/10.1186/s43556-020-00001-4 |
| _version_ | 1831572420300898304 |
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| author | Renjie Zhou Rui Zeng Albrecht von Brunn Jian Lei |
| author_facet | Renjie Zhou Rui Zeng Albrecht von Brunn Jian Lei |
| author_sort | Renjie Zhou |
| collection | DOAJ |
| description | Abstract The newly emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in a global human health crisis. The CoV nucleocapsid (N) protein plays essential roles both in the viral genomic RNA packaging and the regulation of host cellular machinery. Here, to contribute to the structural information of the N protein, we describe the 2.0 Å crystal structure of the SARS-CoV-2 N protein C-terminal domain (N-CTD). The structure indicates an extensive interaction dimer in a domain-swapped manner. The interface of this dimer was first thoroughly illustrated. Also, the SARS-CoV-2 N-CTD dimerization form was verified in solution using size-exclusion chromatography. Based on the structural comparison of the N-CTDs from alpha-, beta-, and gamma-CoVs, we demonstrate the common and specific characteristics of the SARS-CoV-2 N-CTD. Furthermore, we provide evidence that the SARS-CoV-2 N-CTD possesses the binding ability to single-stranded RNA, single-stranded DNA as well as double-stranded DNA in vitro. In conclusion, this study could potentially accelerate research to understand the complete biological functions of the new CoV N protein. |
| first_indexed | 2024-12-17T13:27:17Z |
| format | Article |
| id | doaj.art-c863e38eded74aa2a72f02f7f0a68dc8 |
| institution | Directory Open Access Journal |
| issn | 2662-8651 |
| language | English |
| last_indexed | 2024-12-17T13:27:17Z |
| publishDate | 2020-08-01 |
| publisher | Springer |
| record_format | Article |
| series | Molecular Biomedicine |
| spelling | doaj.art-c863e38eded74aa2a72f02f7f0a68dc82022-12-21T21:46:42ZengSpringerMolecular Biomedicine2662-86512020-08-011111110.1186/s43556-020-00001-4Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid proteinRenjie Zhou0Rui Zeng1Albrecht von Brunn2Jian Lei3National Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan UniversityMax von Pettenkofer-Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF)National Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan UniversityAbstract The newly emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in a global human health crisis. The CoV nucleocapsid (N) protein plays essential roles both in the viral genomic RNA packaging and the regulation of host cellular machinery. Here, to contribute to the structural information of the N protein, we describe the 2.0 Å crystal structure of the SARS-CoV-2 N protein C-terminal domain (N-CTD). The structure indicates an extensive interaction dimer in a domain-swapped manner. The interface of this dimer was first thoroughly illustrated. Also, the SARS-CoV-2 N-CTD dimerization form was verified in solution using size-exclusion chromatography. Based on the structural comparison of the N-CTDs from alpha-, beta-, and gamma-CoVs, we demonstrate the common and specific characteristics of the SARS-CoV-2 N-CTD. Furthermore, we provide evidence that the SARS-CoV-2 N-CTD possesses the binding ability to single-stranded RNA, single-stranded DNA as well as double-stranded DNA in vitro. In conclusion, this study could potentially accelerate research to understand the complete biological functions of the new CoV N protein.https://doi.org/10.1186/s43556-020-00001-4CoronavirusSARSNucleocapsidViral RNAStructure |
| spellingShingle | Renjie Zhou Rui Zeng Albrecht von Brunn Jian Lei Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein Molecular Biomedicine Coronavirus SARS Nucleocapsid Viral RNA Structure |
| title | Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein |
| title_full | Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein |
| title_fullStr | Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein |
| title_full_unstemmed | Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein |
| title_short | Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein |
| title_sort | structural characterization of the c terminal domain of sars cov 2 nucleocapsid protein |
| topic | Coronavirus SARS Nucleocapsid Viral RNA Structure |
| url | https://doi.org/10.1186/s43556-020-00001-4 |
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