The characterisation of an esterase derived from Babesia bovis and its use as a vaccine.

An esterase was isolated from a crude extract of Babesia bovis by affinity chromatography, using soy bean trypsin inhibitor as a ligand. In native form this enzyme had a molecular weight greater than 200 000, but on denaturing gels major bands were observed with molecular weights of 20 000, 10 000 and 7 000. Western transfer analysis revealed a major band with a molecular weight of 19 000-20 000. Both bovine and rabbit antisera avidly stained infected red cells, using indirect immunofluorescence. Weak parasite staining was also observed using this test. Two groups of five animals were vaccinated twice 4 weeks apart with esterase derived from 5 X 10(9) parasites as water-in-oil emulsions with Freund's complete adjuvant. Two control groups, each of five animals were also included. One group of vaccinates and a control group were challenged with virulent homologous B. bovis, whilst the other vaccinated and the remaining control group were challenged with virulent heterologous organisms. In the homologous groups two controls but no vaccinates died, whereas in the heterologous groups four animals in each group died. Significant differences in parasitaemia, temperature rise and total haemolytic complement were observed in the homologous vaccinated group compared to their controls but no differences were observed between heterologous groups.