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
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.
Circular dichroism, Secondary structure, Thermal stability, Thermodynamics, Biochemistry