| Institution: | 1.College of Animal Science and Veterinary Medicine,Henan Agricultural University,Zhengzhou,People’s Republic of China;2.Henan Provincial Key Laboratory of Animal Immunology,Henan Academy of Agricultural Sciences,Zhengzhou,People’s Republic of China;3.School of Life Sciences,Zhengzhou University,Zhengzhou,People’s Republic of China |
| Abstract: | ObjectivesTo improve the expression of soluble IBDV VP2 protein by using different tagged vectors in Escherichia coli.ResultsFusion tags, Grifin, MBP, SUMO, thioredoxin, γ-crystallin, ArsC and PpiB, enhanced the expression and solubility of VP2 protein. The fusion proteins were purified by Ni–NTA chromatography, MBP-VP2 showed the highest purity about 90 %. After removing the MBP tag, VP2 self-assembled into virus-like particles, ~25 nm diam. Results from AGP suggested the recombinant IBDV VP2 protein identified by reference serum like IBDV.ConclusionAll the seven tags enhanced the expression and solubility of IBDV VP2 protein. The recombinant protein self-assembly into virus like particles and possess antigenicity as reference IBDV. |
