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Identification and functional analysis of the SARS-COV-2 nucleocapsid protein
BACKGROUND: A severe form of pneumonia, named coronavirus disease 2019 (COVID-19) by the World Health Organization is widespread on the whole world. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was proved to be the main agent of COVID-19. In the present study, we conducted an in...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7898026/ https://www.ncbi.nlm.nih.gov/pubmed/33618668 http://dx.doi.org/10.1186/s12866-021-02107-3 |
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author | Gao, Tianyi Gao, Yingdong Liu, Xiangxiang Nie, Zhenlin Sun, Huilin Lin, Kang Peng, Hongxin Wang, Shukui |
author_facet | Gao, Tianyi Gao, Yingdong Liu, Xiangxiang Nie, Zhenlin Sun, Huilin Lin, Kang Peng, Hongxin Wang, Shukui |
author_sort | Gao, Tianyi |
collection | PubMed |
description | BACKGROUND: A severe form of pneumonia, named coronavirus disease 2019 (COVID-19) by the World Health Organization is widespread on the whole world. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was proved to be the main agent of COVID-19. In the present study, we conducted an in depth analysis of the SARS-COV-2 nucleocapsid to identify potential targets that may allow identification of therapeutic targets. METHODS: The SARS-COV-2 N protein subcellular localization and physicochemical property was analyzed by PSORT II Prediction and ProtParam tool. Then SOPMA tool and swiss-model was applied to analyze the structure of N protein. Next, the biological function was explored by mass spectrometry analysis and flow cytometry. At last, its potential phosphorylation sites were analyzed by NetPhos3.1 Server and PROVEAN PROTEIN. RESULTS: SARS-COV-2 N protein composed of 419 aa, is a 45.6 kDa positively charged unstable hydrophobic protein. It has 91 and 49% similarity to SARS-CoV and MERS-CoV and is predicted to be predominantly a nuclear protein. It mainly contains random coil (55.13%) of which the tertiary structure was further determined with high reliability (95.76%). Cells transfected with SARS-COV-2 N protein usually show a G1/S phase block company with an increased expression of TUBA1C, TUBB6. At last, our analysis of SARS-COV-2 N protein predicted a total number of 12 phosphorylated sites and 9 potential protein kinases which would significantly affect SARS-COV-2 N protein function. CONCLUSION: In this study, we report the physicochemical properties, subcellular localization, and biological function of SARS-COV-2 N protein. The 12 phosphorylated sites and 9 potential protein kinase sites in SARS-COV-2 N protein may serve as promising targets for drug discovery and development for of a recombinant virus vaccine. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12866-021-02107-3. |
format | Online Article Text |
id | pubmed-7898026 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-78980262021-02-22 Identification and functional analysis of the SARS-COV-2 nucleocapsid protein Gao, Tianyi Gao, Yingdong Liu, Xiangxiang Nie, Zhenlin Sun, Huilin Lin, Kang Peng, Hongxin Wang, Shukui BMC Microbiol Research Article BACKGROUND: A severe form of pneumonia, named coronavirus disease 2019 (COVID-19) by the World Health Organization is widespread on the whole world. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was proved to be the main agent of COVID-19. In the present study, we conducted an in depth analysis of the SARS-COV-2 nucleocapsid to identify potential targets that may allow identification of therapeutic targets. METHODS: The SARS-COV-2 N protein subcellular localization and physicochemical property was analyzed by PSORT II Prediction and ProtParam tool. Then SOPMA tool and swiss-model was applied to analyze the structure of N protein. Next, the biological function was explored by mass spectrometry analysis and flow cytometry. At last, its potential phosphorylation sites were analyzed by NetPhos3.1 Server and PROVEAN PROTEIN. RESULTS: SARS-COV-2 N protein composed of 419 aa, is a 45.6 kDa positively charged unstable hydrophobic protein. It has 91 and 49% similarity to SARS-CoV and MERS-CoV and is predicted to be predominantly a nuclear protein. It mainly contains random coil (55.13%) of which the tertiary structure was further determined with high reliability (95.76%). Cells transfected with SARS-COV-2 N protein usually show a G1/S phase block company with an increased expression of TUBA1C, TUBB6. At last, our analysis of SARS-COV-2 N protein predicted a total number of 12 phosphorylated sites and 9 potential protein kinases which would significantly affect SARS-COV-2 N protein function. CONCLUSION: In this study, we report the physicochemical properties, subcellular localization, and biological function of SARS-COV-2 N protein. The 12 phosphorylated sites and 9 potential protein kinase sites in SARS-COV-2 N protein may serve as promising targets for drug discovery and development for of a recombinant virus vaccine. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12866-021-02107-3. BioMed Central 2021-02-22 /pmc/articles/PMC7898026/ /pubmed/33618668 http://dx.doi.org/10.1186/s12866-021-02107-3 Text en © The Author(s) 2021 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Article Gao, Tianyi Gao, Yingdong Liu, Xiangxiang Nie, Zhenlin Sun, Huilin Lin, Kang Peng, Hongxin Wang, Shukui Identification and functional analysis of the SARS-COV-2 nucleocapsid protein |
title | Identification and functional analysis of the SARS-COV-2 nucleocapsid protein |
title_full | Identification and functional analysis of the SARS-COV-2 nucleocapsid protein |
title_fullStr | Identification and functional analysis of the SARS-COV-2 nucleocapsid protein |
title_full_unstemmed | Identification and functional analysis of the SARS-COV-2 nucleocapsid protein |
title_short | Identification and functional analysis of the SARS-COV-2 nucleocapsid protein |
title_sort | identification and functional analysis of the sars-cov-2 nucleocapsid protein |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7898026/ https://www.ncbi.nlm.nih.gov/pubmed/33618668 http://dx.doi.org/10.1186/s12866-021-02107-3 |
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