Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein

Yu Sheng Lo, Shing Yen Lin, Shiu Mei Wang, Chin Tien Wang, Ya Li Chiu, Tai Huang Huang, Ming Hon Hou

Research output: Contribution to journalArticle

18 Citations (Scopus)


The coronavirus (CoV) N protein oligomerizes via its carboxyl terminus. However, the oligomerization mechanism of the C-terminal domains (CTD) of CoV N proteins remains unclear. Based on the protein disorder prediction system, a comprehensive series of HCoV-229E N protein mutants with truncated CTD was generated and systematically investigated by biophysical and biochemical analyses to clarify the role of the C-terminal tail of the HCoV-229E N protein in oligomerization. These results indicate that the last C-terminal tail plays an important role in dimer-dimer association. The C-terminal tail peptide is able to interfere with the oligomerization of the CTD of HCoV-229E N protein and performs the inhibitory effect on viral titre of HCoV-229E. This study may assist the development of anti-viral drugs against HCoV. Structured summary of protein interactions: N and C-terminal tail peptide bind by cosedimentation in solution (View interaction) N and N bind by cosedimentation in solution (View Interaction: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12) C-terminal tail peptide and N bind by fluorescence technology (View interaction) N and N bind by cross-linking study (View interaction) N and N bind by cross-linking study (View Interaction: 1, 2, 3, 4)

Original languageEnglish
Pages (from-to)120-127
Number of pages8
JournalFEBS Letters
Issue number2
Publication statusPublished - 2013 Jan 16



  • 229E strain
  • C-terminal domain
  • Human coronavirus
  • Nucleocapsid protein
  • Oligomerization
  • Ribonucleocapsid
  • Secondary structure
  • Stability

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this