Abstract
The immunodominant 33/35 kDa antigen of a Theileria isolate from West Java, Indonesia, was characterised and immuno-affinity purified by use of a monoclonal antibody, KUL-a4, and was shown to be representative of the T. orientalis/sergenti/buffeli group. The aminoterminal sequence of the purified 35 kDa peptide (20 residues) was determined by automated Edman degradation and found to correspond to the predicted amino acid sequence of a prospective p33 gene previously sequenced from the same isolate. The cleavage site of a putative signal peptide was identified and conforms the (−3, −1) rule for signal peptidases. The existence of dimeric and trimeric forms of the p33/35 antigen is hypothesised from Western blot profiles. KUL-a4 appeared specific for the T. orientalis/sergenti/buffeli group. It did not recognise in indirect fluorescence antibody test (IFAT), intraerythrocytic bodies of Anaplasma marginale or piroplasms and schizonts of T. mutans, T. parva and T. annulata, whereas cattle antisera raised to these species showed cross-reactivity in IFAT. It however, appeared weakly cross-reactive in Western blot and ELISA, with the 34 kDa piroplasm antigen of one T. annulata (Gharb) isolate. The present study indicates that the isolated antigen belongs to the p33/34 antigen family described within the T. sergenti/orientalis/buffeli group, and documents the group-specificity of one of its epitopes.
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