Published in:
01-12-2016 | Brief Report
Simultaneous mutation of G275A and P276A in the matrix protein of Newcastle disease virus decreases virus replication and budding
Authors:
Haixu Xu, Zhiqiang Duan, Yu Chen, Jiajia Liu, Xin Cheng, Jingjing Liu, Jie Zhu, Xiaoquan Wang, Xiaowen Liu, Shunlin Hu, Xiufan Liu
Published in:
Archives of Virology
|
Issue 12/2016
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Abstract
The matrix (M) protein of Newcastle disease virus (NDV) is a highly conserved hydrophobic viral protein. In some paramyxoviruses (measles virus and Sendai virus), the paired glycine (G) near the C terminus of the M protein may form a turn that mediates the specific interaction with the cell membrane. Similar amino acids (glycine-proline [GP], at position 275–276) exist in the M protein of NDV. However, the role of these residues in the replication and pathogenicity of NDV is unknown. In this study, recombinant NDV with the sequence GP/AA or LGP/GGL in the M protein was generated to investigate the role of this conserved sequence. Budding experiments on the mutant viruses revealed that the GP/AA mutation reduced virus budding and virus replication in DF-1 cells; biological characterization revealed attenuated virulence and pathogenicity in chickens, indicating that the GP sequence plays a critical role in the life cycle of the virus.