Expression, purification, and characterization of VP2 capsid protein of canine parvovirus in Escherichia coli

The capsid protein VP2 of canine parvovirus (CPV) was expressed in Escherichia coli using pMAL-c2x vector. After codon optimization, the mutant resulted in high-level expression of fusion protein. A simple procedure was used to purify fusion protein and remove endotoxin from fusion protein preparations. The fusion protein was antigenical similar to the native capsid protein as Western-blot assay performed with polyclonal antibodies obtained from dogs vaccinated with CPV. The immunogenicity of fusion protein was demonstrated in a vaccination experiment conducted with rabbits subcutaneously immunized. Rabbits vaccinated with fusion protein developed high titers of virus-specific antibodies response that neutralized CPV in vitro.