201. M protein is sufficient for assembly and release of Peste des petits ruminants virus-like particles.
- Author
-
Wang Q, Ou C, Dou Y, Chen L, Meng X, Liu X, Yu Y, Jiang J, Ma J, Zhang Z, Hu J, and Cai X
- Subjects
- Animals, Antibodies, Viral, Chlorocebus aethiops metabolism, Chlorocebus aethiops physiology, DNA, Complementary, DNA, Viral, Hemagglutinins, Viral metabolism, Hemagglutinins, Viral physiology, Mice, Nucleocapsid Proteins metabolism, Nucleocapsid Proteins physiology, Peste-des-petits-ruminants virus genetics, Peste-des-petits-ruminants virus immunology, Viral Fusion Proteins metabolism, Viral Fusion Proteins physiology, Peste-des-petits-ruminants virus metabolism, Peste-des-petits-ruminants virus physiology, Vero Cells metabolism, Viral Matrix Proteins metabolism
- Abstract
Peste des petits ruminants virus (PPRV), belonging to paramyxoviruses, has six structure proteins (such as matrix protein (M), nucleocapsid proteins (N), fusion protein (F) and hemagglutinin protein (H)) and could cause high morbidity and mortality in sheep and goats. Although a vaccine strain of PPRV has been rescued and co-expression of M and N could yield PPRV-like particles, the roles of structure proteins in virion assembly and release have not been investigated in detail. In this study, plasmids carrying PPRV cDNA sequences encoding the N, M, H, and F proteins were expressed in Vero cells. The co-expression of all four proteins resulted in the release of virus-like particles (VLPs) with similar release efficiency to that of authentic virions. Moreover, the co-expression of M together with F also resulted in efficient VLPs release. In the absence of M protein, the expression of no combination of the other proteins resulted in particle release. In summary, a VLPs production system for PPRV has been established and M protein is necessary for promoting the assembly and release of VLPs, of which the predominant protein is M protein. Further study will be focused on the immunogenicity of the VLPs., (Copyright © 2017. Published by Elsevier Ltd.)
- Published
- 2017
- Full Text
- View/download PDF