Mutations in the FPIV motif of Newcastle disease virus matrix protein attenuate virus replication and reduce virus budding.
The FPIV-like late domains identified in the matrix (M) proteins of parainfluenza virus 5 and mumps virus have been demonstrated to be critical for virus budding. In this study, we found that the same FPIV sequence motif is present in the N-terminus of the Newcastle disease virus (NDV) M protein. Mutagenesis experiments demonstrated that mutation of either phenylalanine (F) or proline (P) to alanine led to a more obvious decrease in viral virulence and replication and resulted in poor budding of the mutant viruses. Additionally, evidence for the involvement of cellular multivesicular body (MVB) proteins was obtained, since NDV production was inhibited upon expression of dominant-negative versions of the VPS4A-E228Q protein. Together, these results demonstrate that the FPIV motif, especially the residues F and P, within the NDV M protein, plays a critical role in NDV replication and budding, and this budding process likely involves the cellular MVB pathway.
Animal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, 225009, Jiangsu, China.
Zhiqiang
Z
Duan
Zenglei
Z
Hu
Jie
J
Zhu
Haixu
H
Xu
Jian
J
Chen
Huimou
H
Liu
Shunlin
S
Hu
Xiufan
X
Liu
D020816:Amino Acid Motifs; D009154:Mutation; D009522:Newcastle disease virus / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D057074:Virus Release / Q000502:physiology*; D014779:Virus Replication / Q000502:physiology*
D014763:Viral Matrix Proteins