Simultaneous mutation of G275A and P276A in the matrix protein of Newcastle disease virus decreases virus replication and budding

Simultaneous mutation of G275A and P276A in the matrix protein of Newcastle disease virus decreases virus replication and budding

Archives of Virology, September 2016

27600544

Haixu Xu, Zhiqiang Duan, Yu Chen, Jiajia Liu, Xin Cheng, Jingjing Liu, Jie Zhu, Xiaoquan Wang, Xiaowen Liu, Shunlin Hu, Xiufan Liu

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.