In the present study, we expressed rubella virus (RV) capsid protein (C) in yeast S. cerevisiae cells. Two different methods for purification of recombinant C protein were employed: CsCl gradient ultracentrifugation and nickel chelation chromatography. The yield of recombinant C protein was approximately 3.2 mg of purified protein from 1g of wet yeast biomass. The antigenic characteristics of recombinant C protein purified in different ways were further evaluated by indirect IgG ELISA with RV-positive and RV-negative human serum specimens. Recombinant C protein purified using CsCl gradient ultracentrifugation possessed a higher antigenicity as compared to that purified by nickel chelate chromatography. The resu... More
In the present study, we expressed rubella virus (RV) capsid protein (C) in yeast S. cerevisiae cells. Two different methods for purification of recombinant C protein were employed: CsCl gradient ultracentrifugation and nickel chelation chromatography. The yield of recombinant C protein was approximately 3.2 mg of purified protein from 1g of wet yeast biomass. The antigenic characteristics of recombinant C protein purified in different ways were further evaluated by indirect IgG ELISA with RV-positive and RV-negative human serum specimens. Recombinant C protein purified using CsCl gradient ultracentrifugation possessed a higher antigenicity as compared to that purified by nickel chelate chromatography. The results indicate that the recombinant C protein has a potential for use in detection of human IgG antibodies against RV. The yeast-expressed rubella C protein is a promising antigen for the development of diagnostic tools in serology.
