The baculovirus-insect cell expression system has been widely used method for the recombinant protein expression. The present study has several limitation. In this study, we constructed vectors consisting of transcriptional enhanced factor and promoter that improve the expression level. To confirm the usefulness of these vector system, Human papillomavirus (HPV) VLPs have been expressed by baculovirus hyper expression system. HPV VLPs were purified using a CaptoTM Core 700 (GE Healthcare Life Sciences) chromatography approach. Baculovirus hyper expression system production efficiency was influenced by the HPV VLPs production. HPV VLPs vaccination to BALB/c mice induced the generation of antibody confirmed by ELISA. This study could provide improvements on the vaccine production for the development of VLP vaccines high expression of useful heterologous proteins.

The baculovirus expression system is a very useful tool widely used for expression of foreign proteins. To use the baculovirus expression system, a recombinant baculovirus must be prepared. The development of the Bac to Bac system has reduced the time and effort required to produce recombinant baculovirus. But, it will take at least two weeks. Further, it takes more time to measure the activity of recombinant baculovirus. In order to overcome this problem, a virus inducible expression system is being studied recently. Although baculovirus is able to rapidly express foreign proteins, it still has a low expression level. Thus, in this study, we aimed to construct a novel baculovirus inducible expression vector that not only shortens the production time of protein but also can express at a high level. The novel baculovirus inducible expression vector has been evaluated using EGFP and is expected to be a very useful tool for production of various proteins.

Among the various expression systems used for foreign protein expression, baculovirus expression system (BES) has the high level of post-translational modification ability such as glycosylation, folding and disulfide bonding. BES is widely used now in the production of VLPs because it is possible for the efficient multi-gene expression. However, there are not many cases of VLPs being manufactured through BES. Therefore, in this study, three improvements were made to increase the productivity of VLP through BES. A new heper enhanced expression vector was constructed to increase the expression of structural proteins of virus-like particles, and baculovirus bacmid was modified to increase production time. In addition, an easy purification system was constructed to efficiently purify VLP, and finally the construction of BES optimized for VLP production was completed.

Virus-like particles (VLPs) are similar to pathogenic viruses, but because they have no nucleic acid, they have excellent safety and immunogenicity and are used as a good vaccine material. However, in the selection of various structural proteins of pathogenic viruses to form VLPs, all expression systems consume a lot of time in common. Among them, the baculovirus expression system causes additional time consumption to construct the recombinant baculovirus. Therefore, there is a need for a system that can rapidly determine the structural proteins required for effective VLP production. This study aims at solving this problem by constructing a BmNPV inducible expression platform through the construction of vectors induced by BmNPV. The platform was evaluated for overexpression using EGFP. We also confirmed the formation of virus-like particles through overexpression of canine parvovirus structural proteins.