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- Title
Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein
- Authors
Lo, Yu-Sheng; Lin, Shing-Yen; Wang, Shiu-Mei; Wang, Chin-Tien; Chiu, Ya-Li; Huang, Tai-Huang; Hou, Ming-Hon
- Abstract
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)
- Subjects
OLIGOMERIZATION; CORONAVIRUSES; NUCLEOCAPSIDS; C-terminal binding proteins; SODIUM dodecyl sulfate; MUTANT proteins
- Publication
FEBS Letters, 2013, Vol 587, Issue 2, p120
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.11.016