Abstract:

The recombinant expression vectors pET-VP2a and pET-VP2b were constructed by cloning VP2 gene of Aleutian mink disease parvovirus (ADV-G) into a prokaryotic expression plasmid pET-28a. The recombinant vectors were transformed into recipient germs BL21. Samples were collected at different induction time after induction with IPTG. The specificity of the expressed proteins were identified with SDS-PAGE, Western Blotting . And the protein were about 23kDa and 28 KDa in size. The expressed protein were purified byNi-NTA His-Bind purification system and the degree of purity is about 91%.The purified protein was coated on 96-well plate at 60μg/well and used for identification of ADV-positive sera from different regions. The results are 93% identical to CIEP. But this method is safer and easier to perform. High efficient expression of ADV protein will benefit for diagnosis of ADV in practice.