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.

Viral particles of Porcine epidemic diarrhea virus (PEDV) consist of a four structural proteins. Among them Spikeprotein mediated responsible for receptor binding and membrane fusion during viral infection and therefore the main targetof neutralizing antibodies. Virus-like particles (VLPs) are consisted of one or more viral structural proteins, and theirmorphologies closely resemble those of the native virus. VLPs have no virulence and can elicit robust immune responsesas compared with inactivated or live-attenuated virus vaccines. Thus, in this study, we tried two methods for VLP constructionin Bombyx mori, one is traditional method and the other is chimeric VLP method using the influenza matrix protein.Both methods could produce successfully PEDV VLPs.