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*

*此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

66 引文 斯高帕斯(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 1月 16
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 分子生物學
  • 遺傳學
  • 細胞生物學

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