Expression and Purification of the Capsid Protein of Chicken Anemia Virus and Preparation of Antibody

The coding region of capsid protein gene from Chicken Anemia virus(CAV) was amplified from pPro-VP1 by PCR and cloned into pET-30a（+）. E.coli BL21（DE3）were transformed by the recombinant plasmid pET30-VP1. Analysis by SDS-PAGE and Western blot showed that the target gene was expressed successfully in the form of inclusion body when induced with IPTG. The protein was then purified by Ni2+-affinity chromatography and used to immunize female Balb/c mice. After three rounds of immunizations, antiserum was collected and used to detect the specificity of recombinant protein. ELISA showed that the titer of antiserum was above 1:12800. Moreover, antiserum reacted specifically with purified recombinant protein in Western blot. This study laid a foundation for the development of CAV diagnostic kit and vaccine.