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.

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