The SARS coronavirus nucleocapsid protein - Forms and functions

Chung Ke Chang, Ming Hon Hou, Chi Fon Chang, Chwan Deng Hsiao, Tai Huang Huang*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

346 Citations (Scopus)


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."

Original languageEnglish
Pages (from-to)39-50
Number of pages12
JournalAntiviral Research
Issue number1
Publication statusPublished - 2014 Mar


  • Capsid packaging
  • Coronavirus
  • Intrinsic disorder
  • Nucleocapsid protein
  • RNP
  • SARS

ASJC Scopus subject areas

  • Pharmacology
  • Virology


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