Expression of the VP2 Gene Fragment of Goose Parvovirus in Prokaryotic System and Preparation of its Antiserum

A 969bp fragment at the 5′- end of the vp2 gene of Goose parvovirus isolate HG5/82 was subcloned into the Nco I site of prokaryotic expression vector pPROEX~{TM}HTb. The recombinant plasmid was transformed into E.coli DH5α and induced with IPTG. SDS-PAGE analysis showed an induced product band about 36kDa, which was corresponding to the size of the fragment. The amount of the recombiant protein was evaluated by densitometric scanning. It indicated that the product was 21.4% of total bacterial protein.The induced bacteria was solubilized by 6mol/L Guanidine hydrochloric acid and purified by ProBond~{TM} Resin. The antiserum against the recombinant protein was obtained by injecting the rabbit with fusion protein. We successfully expressed and purified the fusion protein from E.coli and obtained the antiserum against it, and laid a foundation for future studies on the bioactivity of GPV.