Proteins fusing to the occlusion bodies of the baculovirus were tested for quick purification and for antibodies generation. In recombinant baculoviruses, the polyhedrin promoter was used to drive engineered proteins fusing to the polyhedrin coding region. After viral infection, the engineered proteins were properly formed as occlusion body-like particles in the nuclei of infected cells. Then, the engineered protein contained in particles can be easily separated and purified by low-speed centrifugation from cells. The green fluorescent protein (GFP), a model protein, and the virus proteinl (VPI) of foot and mouth disease, a vaccine candidate, were both tested and successfully incorporated into the occlusion body-like particles for quick purification from cells. Such fusion-engineered proteins have very high yields and induce antibody with high titers. Since strong green fluorescence was emitted from the particle with fusion GFP, suggested that the maintenance of protein function is possible. Thus, protein production by in vivo particle formation is proved to be a useful technology for the isolation, purification, and antibody induction of the engineered proteins.
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