Abstract
Ebola virus (EBOV) disease outbreaks have resulted in many fatalities, yet no licensed vaccines are available to prevent infection. Recombinant glycoprotein (GP) production may contribute to finding a cure for Ebola virus disease, which is the key candidate protein for vaccine preparation. To explore GP(1,2) expression in BmN cells, EBOV-GP(1,2) with its native signal peptide or the GP64 signal peptide was cloned and transferred into a normal or gp64 null Bombyx mori nucleopolyhedrovirus (BmNPV) bacmid via transposition. The infectivity of the recombinant bacmids was investigated after transfection, expression and localization of EBOV-GP were investigated, and cell morphological changes were analyzed by TEM. The GP64 signal peptide, but not the GP(1,2) native signal peptide, caused GP(1,2) localization to the cell membrane, and the differentially localized GP(1,2) proteins were cleaved into GP(1) and GP(2) fragments in BmN cells. GP(1,2) expression resulted in dramatic morphological changes in BmN cells in the early stage of infection. However, GP(1,2) expression did not rescue GP64 deficiency in BmNPV infection. This study provides a better understanding of GP expression and processing in BmN cells, which may lay a foundation for EBOV-GP expression using the BmNPV baculovirus expression system.