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.
【저자키워드】 Structure, SARS-CoV-2, Nucleocapsid protein (N protein), Phosphorylation, 【초록키워드】 COVID-19, coronavirus disease, Coronavirus disease 2019, Vaccine, coronavirus, mass spectrometry, Drug discovery, reliability, Pneumonia, SARS-CoV, prediction, severe acute respiratory syndrome Coronavirus, virus, MERS-CoV, flow cytometry, Protein, biological function, nucleocapsid, N protein, target, targets, respiratory, therapeutic targets, Analysis, Physicochemical properties, similarity, protein kinase, kinases, protein kinases, Health Organization, tertiary structure, World Health Organization, coil, acute respiratory syndrome, supplementary material, increased expression, acute respiratory syndrome coronavirus, acute respiratory syndrome coronavirus 2, hydrophobic, random, SARS-CoV-2 nucleocapsid, subcellular localization, nuclear protein, PROVEAN, phosphorylation sites, SOPMA tool, TUBA1C, TUBB6, server, depth analysis, Affect, widespread, ProtParam tool, Result, predicted, analyzed, identify, significantly, composed, conducted, applied, phosphorylated, phosphorylation site, physicochemical, transfected with, 【제목키워드】 nucleocapsid protein, Analysis, identification, functional,