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

16 Citations (Scopus)

Abstract

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
Volume587
Issue number2
DOIs
Publication statusPublished - 2013 Jan 16

Fingerprint

Human Coronavirus 229E
Nucleocapsid Proteins
Oligomerization
Dimers
Peptides
Proteins
Mutant Proteins
Fluorescence
Association reactions
Technology
Coronavirus nucleocapsid protein
Pharmaceutical Preparations

Keywords

  • 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

Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein. / Lo, Yu Sheng; Lin, Shing Yen; Wang, Shiu Mei; Wang, Chin Tien; Chiu, Ya Li; Huang, Tai Huang; Hou, Ming Hon.

In: FEBS Letters, Vol. 587, No. 2, 16.01.2013, p. 120-127.

Research output: Contribution to journalArticle

Lo, Yu Sheng ; Lin, Shing Yen ; Wang, Shiu Mei ; Wang, Chin Tien ; Chiu, Ya Li ; Huang, Tai Huang ; Hou, Ming Hon. / Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein. In: FEBS Letters. 2013 ; Vol. 587, No. 2. pp. 120-127.
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abstract = "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)",
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