The cytoplasmic tail substitution increases the assembly efficiency of Ebola virus glycoprotein on the budded virus of Bombyx mori nucleopolyhedrovirus

Glycoprotein (GP_1,2) of the Ebola virus (EBOV) is the key membrane fusion protein, which is a key candidate protein for vaccine preparations. Previously, GP_1,2 was expressed by Bombyx mori nucleopolyhedrovirus (BmNPV) expression vector system; however, few GP_1,2 was incorporated into budded virus (BV) of BmNPV. To improve the incorporation efficiency of GP_1,2 into the virion, the GP_1,2 fusion with the cytoplasmic tail of GP64 of BmNPV was expressed in BmN cells by the BmNPV expression system. The BV was purified by ultracentrifugation, and GP_1,2 expression in BV was detected by the antibody. The result indicated that a 532% increase in the relative GP_1,2 densitometry signal was observed in constructs utilizing the GP64 C-terminal domain; moreover, the substitution of GP_1,2 native signal peptide with GP64 signal peptide increased the incorporation efficiency by 34.6% in the relative GP_1,2 densitometry signal. We revealed that the application of the cytoplasmic tail of BmNPV GP64 significantly increased the incorporation rate of GP_1,2 into the BV envelope. This study lays a foundation for GP_1,2 vaccine development.