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Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein.

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机构： [1]National Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, No.17, Block 3, Southern Renmin Road, Chengdu 610041, Sichuan, China. [2]Max von Pettenkofer-Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), Partner Site Munich, 80336 Munich, Germany.

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关键词： Coronavirus SARS Nucleocapsid Viral RNA Structure

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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.© The Author(s) 2020.

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大类 | 4 区医学

小类 | 4 区生化与分子生物学 4 区细胞生物学 4 区医学：研究与实验

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第一作者机构： [1]National Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, No.17, Block 3, Southern Renmin Road, Chengdu 610041, Sichuan, China.

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