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- Title
Simultaneous mutation of G275A and P276A in the matrix protein of Newcastle disease virus decreases virus replication and budding.
- Authors
Xu, Haixu; Duan, Zhiqiang; Chen, Yu; Liu, Jiajia; Cheng, Xin; Liu, Jingjing; Zhu, Jie; Wang, Xiaoquan; Liu, Xiaowen; Hu, Shunlin; Liu, Xiufan
- 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.
- Subjects
NEWCASTLE disease virus; VIRAL proteins; GENETIC mutation; EXTRACELLULAR matrix proteins; HYDROPHOBIC interactions; VIRAL replication; BUDDING (Zoology); MOLECULAR interactions
- Publication
Archives of Virology, 2016, Vol 161, Issue 12, p3527
- ISSN
0304-8608
- Publication type
Report
- DOI
10.1007/s00705-016-3046-x