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A 20-kDa protease, analogous to the Kunitz-type serine protease inhibitors (KSPIs) in plasmodia and in mammals, was purified from plasmodial tissue culture fluid and from a purified sporozoite surface membrane preparation, indicating it is synthesized by the sporozoite and expressed on the surface of the sporozoite. The 20-kDa protease in all isolates studied was composed of a C-terminal polypeptide and a N-terminal polypeptide of 27-32 amino acids; it was inactivated by 1mM 2,4,6-trinitrobenzene sulfonic acid. A monoclonal antibody with broad specificity also inactivated the 20-kDa protease. Immunoblot and cross-reactivity analyses suggested that the surface expression of the 20-kDa protease was upregulated by parasite infection and the antibody cross-reacted with the Plasmodium falciparum blood-stage surface antigen Pf155/RESA. These data are consistent with the idea that this antigen is closely linked to this protease. All blood isolates examined contained a homologous sequence of 8 to 11 amino acids in the C-terminal region of the N-terminal polypept 0b46394aab

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