Journal
ARCHIVES OF VIROLOGY
Volume 159, Issue 7, Pages 1813-1819Publisher
SPRINGER WIEN
DOI: 10.1007/s00705-014-1998-2
Keywords
Newcastle disease virus; Matrix protein; Late domain; Virus replication; Budding
Categories
Funding
- National Natural Science Foundation of China [31172338]
- Excellent Doctoral Dissertation of Yangzhou University
- Earmarked Fund for Modern Agro-industry Technology Research System [nycytx-41-G07]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- Chinese Special Fund for Agro-Scientific Research in the Public Interest [201303033]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available