This study aims to produce an effective subunit vaccine against infectious bursal disease virus （IBDV）. The genes of chicken interleukin-2 （ChIL-2） and IBDV viral protein 2 （VP2） were amplified and fused by spli...This study aims to produce an effective subunit vaccine against infectious bursal disease virus （IBDV）. The genes of chicken interleukin-2 （ChIL-2） and IBDV viral protein 2 （VP2） were amplified and fused by splice overlap extension-polymerase chain reaction （SOE-PCR）. The fusion gene was digested by EcoR I/Kpn I and inserted into pBacPAK8 vector, resulting in recombinant transfer plasmid pBacPakVP2-IL2. The recombinant plasmid was transfected into Sf-9 cells accompanied with hybrid nuclear polyhedrosis virus （HyNPV） genome DNA and lipofectin. Plaque-purification indicated that we had got the recombinant Hy-VP2-IL2. Fusion protein VP2-IL2 was expressed effectively both in insect cells and bombyx mori. The expression of fusion protein was confirmed by ELISA, SDS-PAGE and Western blotting assay, respectively. This efficient system allows us to meet the need for inexpensive vaccines required by the poultry industry. Cellular ＆ Molecular Immunology. 2005;2（3）：231-235.展开更多
基金This work was supported in part by the grants from the National High Technology Research and Development Program of China(No.2004BA757C)the Key Project of Zhejiang Province(NO.011102465).
文摘This study aims to produce an effective subunit vaccine against infectious bursal disease virus （IBDV）. The genes of chicken interleukin-2 （ChIL-2） and IBDV viral protein 2 （VP2） were amplified and fused by splice overlap extension-polymerase chain reaction （SOE-PCR）. The fusion gene was digested by EcoR I/Kpn I and inserted into pBacPAK8 vector, resulting in recombinant transfer plasmid pBacPakVP2-IL2. The recombinant plasmid was transfected into Sf-9 cells accompanied with hybrid nuclear polyhedrosis virus （HyNPV） genome DNA and lipofectin. Plaque-purification indicated that we had got the recombinant Hy-VP2-IL2. Fusion protein VP2-IL2 was expressed effectively both in insect cells and bombyx mori. The expression of fusion protein was confirmed by ELISA, SDS-PAGE and Western blotting assay, respectively. This efficient system allows us to meet the need for inexpensive vaccines required by the poultry industry. Cellular ＆ Molecular Immunology. 2005;2（3）：231-235.
