Biochemical characterization of SARS-CoV-2 nucleocapsid protein
The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-a...
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| Published in | Biochemical and biophysical research communications Vol. 527; no. 3; pp. 618 - 623 |
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| Main Authors | , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
30.06.2020
Published by Elsevier Inc |
| Subjects | |
| Online Access | Get full text |
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| Abstract | The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients’ sera, proving the importance of this antigen in host immunity and diagnostics.
•SARS-CoV-2 nucleocapsid protein is full of coils and highly disordered.•SARS-CoV-2 N protein forms a dimer by CTD-CTD interaction.•SARS-CoV-2 N protein can bind with non-specific nucleic acid with high affinity.•SARS-CoV-2 N protein can be a good antigen for serological test of COVID-19. |
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| AbstractList | The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients' sera, proving the importance of this antigen in host immunity and diagnostics. The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients’ sera, proving the importance of this antigen in host immunity and diagnostics. •SARS-CoV-2 nucleocapsid protein is full of coils and highly disordered.•SARS-CoV-2 N protein forms a dimer by CTD-CTD interaction.•SARS-CoV-2 N protein can bind with non-specific nucleic acid with high affinity.•SARS-CoV-2 N protein can be a good antigen for serological test of COVID-19. The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients’ sera, proving the importance of this antigen in host immunity and diagnostics. • SARS-CoV-2 nucleocapsid protein is full of coils and highly disordered. • SARS-CoV-2 N protein forms a dimer by CTD-CTD interaction. • SARS-CoV-2 N protein can bind with non-specific nucleic acid with high affinity. • SARS-CoV-2 N protein can be a good antigen for serological test of COVID-19. The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients’ sera, proving the importance of this antigen in host immunity and diagnostics. The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients' sera, proving the importance of this antigen in host immunity and diagnostics.The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed the N protein of SARS-CoV-2 and characterized its biochemical properties. Static light scattering, size exclusive chromatography, and small-angle X-ray scattering (SAXS) showed that the purified N protein is largely a dimer in solution. CD spectra showed that it has a high percentage of disordered region at room temperature while it was best structured at 55 °C, suggesting its structural dynamics. Fluorescence polarization assay showed it has non-specific nucleic acid binding capability, which raised a concern in using it as a diagnostic marker. Immunoblot assays confirmed the presence of IgA, IgM and IgG antibodies against N antigen in COVID-19 infection patients' sera, proving the importance of this antigen in host immunity and diagnostics. |
| Author | Yang, Yunru Zhao, Dan Liu, Guangfeng He, Hongliang Ding, Chengchao Zeng, Weihong Ma, Huan Ma, Xiaoling Liu, Muziying Yang, Yun Mohammed, Ahmed Gao, Yong Zhao, Changcheng Xie, Jiajia Jin, Tengchuan Weng, Jianping |
| Author_xml | – sequence: 1 givenname: Weihong surname: Zeng fullname: Zeng, Weihong organization: Department of Obstetrics and Gynecology, The First Affiliated Hospital of USTC, Division of Molecular Medicine, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 2 givenname: Guangfeng orcidid: 0000-0003-0334-7299 surname: Liu fullname: Liu, Guangfeng organization: National Center for Protein Science Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai, 201210, China – sequence: 3 givenname: Huan surname: Ma fullname: Ma, Huan organization: Hefei National Laboratory for Physical Sciences at Microscale, Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230027, China – sequence: 4 givenname: Dan surname: Zhao fullname: Zhao, Dan organization: Hefei National Laboratory for Physical Sciences at Microscale, Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230027, China – sequence: 5 givenname: Yunru surname: Yang fullname: Yang, Yunru organization: Hefei National Laboratory for Physical Sciences at Microscale, Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230027, China – sequence: 6 givenname: Muziying surname: Liu fullname: Liu, Muziying organization: Hefei National Laboratory for Physical Sciences at Microscale, Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230027, China – sequence: 7 givenname: Ahmed surname: Mohammed fullname: Mohammed, Ahmed organization: Hefei National Laboratory for Physical Sciences at Microscale, Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230027, China – sequence: 8 givenname: Changcheng surname: Zhao fullname: Zhao, Changcheng organization: Department of Infectious Diseases, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 9 givenname: Yun orcidid: 0000-0002-2709-6423 surname: Yang fullname: Yang, Yun organization: Department of Infectious Diseases, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 10 givenname: Jiajia surname: Xie fullname: Xie, Jiajia organization: Department of Dermatology, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 11 givenname: Chengchao surname: Ding fullname: Ding, Chengchao organization: Department of Infectious Diseases, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 12 givenname: Xiaoling surname: Ma fullname: Ma, Xiaoling organization: Department of Laboratory Medicine, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 13 givenname: Jianping surname: Weng fullname: Weng, Jianping organization: Institute of Public Health, University of Science and Technology of China, Hefei, Anhui, 230026, China – sequence: 14 givenname: Yong surname: Gao fullname: Gao, Yong organization: Department of Infectious Diseases, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 15 givenname: Hongliang surname: He fullname: He, Hongliang email: hhl725@ustc.edu.cn organization: Department of Infectious Diseases, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China – sequence: 16 givenname: Tengchuan surname: Jin fullname: Jin, Tengchuan email: jint@ustc.edu.cn organization: Department of Obstetrics and Gynecology, The First Affiliated Hospital of USTC, Division of Molecular Medicine, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, 230001, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32416961$$D View this record in MEDLINE/PubMed |
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| Snippet | The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. In this study, we expressed... |
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| SubjectTerms | ambient temperature Antibodies, Viral - blood Antigenicity antigens Betacoronavirus - chemistry chromatography Coronavirus Infections COVID-19 COVID-19 infection diagnostic techniques fluorescence Humans immunity Nucleic Acids nucleocapsid Nucleocapsid protein nucleocapsid proteins Nucleocapsid Proteins - chemistry Pandemics Pneumonia, Viral Protein Binding Protein Multimerization Protein Structure, Tertiary RNA packaging SARS-CoV-2 SAXS Scattering, Small Angle Severe acute respiratory syndrome coronavirus 2 small-angle X-ray scattering Structure and function virion X-Ray Diffraction |
| Title | Biochemical characterization of SARS-CoV-2 nucleocapsid protein |
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