期刊
ANTIVIRAL RESEARCH
卷 103, 期 -, 页码 39-50出版社
ELSEVIER
DOI: 10.1016/j.antiviral.2013.12.009
关键词
SARS; Coronavirus; Nucleocapsid protein; Capsid packaging; Intrinsic disorder; RNP
资金
- National Science Council [NSC 101-2311-B-001-025]
- National Health Research Institute of the Republic of China [NHRI-EX99-9933B1]
- National Science Council of the Republic of China
The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses. (C) 2014 Elsevier B.V. All rights reserved.
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