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

研究成果: 雜誌貢獻文章

16 引文 (Scopus)

摘要

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)

原文英語
頁(從 - 到)120-127
頁數8
期刊FEBS Letters
587
發行號2
DOIs
出版狀態已發佈 - 2013 一月 16

指紋

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

ASJC Scopus subject areas

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

引用此文

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.

於: FEBS Letters, 卷 587, 編號 2, 16.01.2013, p. 120-127.

研究成果: 雜誌貢獻文章

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. 於: FEBS Letters. 2013 ; 卷 587, 編號 2. 頁 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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AU - Huang, Tai Huang

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AB - 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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