Pseudorabies virus (PRV), a member of the Alphaherpesviridae, is the causative agent of Aujeszky’s disease in pigs. Glycoprotein B (gB) of PRV, a major constituent of the viral envelope, consists of 916 amino acids. We continuously combined three gB epitopes, E1 (aa 62-129), E2 (aa 217-282), and E3 (aa 543-737). The DNA fragment containing the PRV gB epitopes was fused with polyhedrin gene in order to generate recombinant baculovirus that expresses the recombinant polyhedra with PRV gB epitopes under the control of the Bombyx mori nucleopolyhedrovirus polyhedrin promoter. Recombinant baculoviruses were injected into fifth-instar B. mori larvae. SDS-PAGE and Western blot analyses revealed that recombinant polyhedra constitute polyhedrin and PRV gB epitopes, and that the recombinant PRV gB epitopes showed cross-reactivity against antiserum of PRV gB produced from pig. To examine the immunogenicity of recombinant PRV gB epitopes, we injected into mice as model animals. ELISA results indicated that antibody production is increased in a similar manner in the injection of recombinant polyhedra with PRV gB epitopes, either injected recombinant polyhedra as a granule form antigen without adjuvant or injected recombinant polyhedrin as a soluble form antigen with adjuvant. Taken together, these data show that PRV gB epitopes were produced as a granule form antigen by fusing recombinant polyhedra in baculovirus-infected silkworm larvae and displayed the immunogenicity in mice, indicating the efficacy of the granule form antigen as a PRV gB vaccine.