Transient Oligomerization of the SARS-CoV N Protein - Implication for Virus Ribonucleoprotein Packaging

Chung ke Chang, Chia Min Michael Chen, Ming hui Chiang, Yen lan Hsu, Tai-huang Huang

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The nucleocapsid (N) phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genome into a helical ribonucleocapsid and plays a fundamental role during viral self-assembly. The N protein consists of two structural domains interspersed between intrinsically disordered regions and dimerizes through the C-terminal structural domain (CTD). A key activity of the protein is the ability to oligomerize during capsid formation by utilizing the dimer as a building block, but the structural and mechanistic bases of this activity are not well understood. By disulfide trapping technique we measured the amount of transient oligomers of N protein mutants with strategically located cysteine residues and showed that CTD acts as a primary transient oligomerization domain in solution. The data is consistent with the helical oligomer packing model of N protein observed in crystal. A systematic study of the oligomerization behavior revealed that altering the intermolecular electrostatic repulsion through changes in solution salt concentration or phosphorylation-mimicking mutations affects oligomerization propensity. We propose a biophysical mechanism where electrostatic repulsion acts as a switch to regulate N protein oligomerization.

Original languageEnglish
Article numbere65045
JournalPLoS ONE
Volume8
Issue number5
DOIs
Publication statusPublished - 2013 May 23

Fingerprint

Virus Assembly
Severe Acute Respiratory Syndrome
ribonucleoproteins
Oligomerization
Ribonucleoproteins
Viruses
packaging
Packaging
viruses
Static Electricity
Oligomers
electrostatic interactions
Electrostatics
Proteins
proteins
Nucleocapsid
Coronavirus
Phosphorylation
Viral Genome
Capsid

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Cite this

Transient Oligomerization of the SARS-CoV N Protein - Implication for Virus Ribonucleoprotein Packaging. / Chang, Chung ke; Chen, Chia Min Michael; Chiang, Ming hui; Hsu, Yen lan; Huang, Tai-huang.

In: PLoS ONE, Vol. 8, No. 5, e65045, 23.05.2013.

Research output: Contribution to journalArticle

Chang, Chung ke ; Chen, Chia Min Michael ; Chiang, Ming hui ; Hsu, Yen lan ; Huang, Tai-huang. / Transient Oligomerization of the SARS-CoV N Protein - Implication for Virus Ribonucleoprotein Packaging. In: PLoS ONE. 2013 ; Vol. 8, No. 5.
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