Urea/DTT solubilization of a recombinant Taenia ovis antigen, 45W, expressed as a GST fusion protein results in enhanced protective immune response to the 45W moiety

Abstract

Vaccination and challenge infection experiments were conducted in sheep using different forms of a recombinant protein (45W) from the cestode parasite Taenia ovis. 45W was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase (45W-GST) and was produced as both soluble protein and insoluble inclusion bodies. Vaccination of animals with either the soluble or inclusion body derived protein resulted in the immune response being predominantly directed to the GST moiety of 45W-GST. Conversely, vaccination with 45W-GST which had been solubilized/treated with urea and dithiothreitol (DTT), elicited enhanced responses to the 45W moiety and significantly reduced responses to..