期刊
BMC MICROBIOLOGY
卷 21, 期 1, 页码 -出版社
BMC
DOI: 10.1186/s12866-021-02107-3
关键词
SARS-COV-2; Nucleocapsid protein (N protein); Structure; Phosphorylation
类别
资金
- New Testing Technology Center of Guangdong Experimental Animal Monitoring Institute
- National Nature Science Foundation of China [81972806, 81802093, 81903034]
- Key Project of Science and Technology Development of Nanjing Medicine [ZDX16001]
- Nanjing medical science and technology foundation [YKK17123]
This study analyzed the physicochemical properties, subcellular localization, and biological function of the SARS-COV-2N protein. The identification of 12 phosphorylated sites and 9 potential protein kinase sites in the SARS-COV-2N protein may serve as promising targets for drug discovery and development of a recombinant virus vaccine.
BackgroundA 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.MethodsThe SARS-COV-2N 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.ResultsSARS-COV-2N protein composed of 419 aa, is a 45.6kDa 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-2N protein usually show a G1/S phase block company with an increased expression of TUBA1C, TUBB6. At last, our analysis of SARS-COV-2N protein predicted a total number of 12 phosphorylated sites and 9 potential protein kinases which would significantly affect SARS-COV-2N protein function.ConclusionIn this study, we report the physicochemical properties, subcellular localization, and biological function of SARS-COV-2N protein. The 12 phosphorylated sites and 9 potential protein kinase sites in SARS-COV-2N protein may serve as promising targets for drug discovery and development for of a recombinant virus vaccine.
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