Previous studies using monoclonal antibody (mAb) 4C9 specific for a 32 kDa
antigen (p32) of Theileria parva demonstrated expression of the antigen on
the surface of the sporozoite, making it a potential antigen for sporozoite
neutralization. A full-length cDNA encoding the major merozoite/piroplasm
surface antigen (mMPSA) of T. parva was cloned and expressed in bacteria. T
he expressed product reacted strongly with mAb 4C9, demonstrating identity
between the p32 and mMPSA of T. parva. Using immunoblot analysis and immuno
electron microscopy with mAb 4C9 it was shown that the mMPSA is a major ant
igen of the merozoite and piroplasm at the cell surface, while lower levels
of antigen are expressed in the sporozoite and schizont stages. Upregulati
on of the mMPSA occurs at merogony and can be induced by culturing schizont
-infected lymphocytes at 42 degrees C. Recombinant mMPSA of T. parva induce
d high titres of specific antibodies in cattle but failed to confer protect
ion against a T. parva sporozoite stabilate challenge. The pre-challenge se
ra also failed to neutralize infectivity of sporozoites in an in vitro assa
y. Possible reasons for the lack of parasite neutralization in vivo and in
vitro are discussed.