Antibodies to the glutamate dehydrogenase ofPlasmodium falciparum

Abstract

SUMMARYPolyclonal antisera raised againstPlasmodium knowlesireacted with (1) NADP-specific glutamate dehydrogenase (GLDH) ofP. knowlesi, (2) GLDH ofP. falciparumand (3) GLDH ofProteus spp. The antisera did not react with NAD(P) GLDH from bovine liver. Polyclonal antisera raised against the GLDH ofProteus spp. cross-reacted with GLDH fromP. falciparum. Monoclonal antibodies (McAbs) obtained from mice immunized with Proteus GLDH were either specific for the bacterial enzyme or cross-reacted withP. falciparumGLDH. The selected McAbs did not react with GLDI-1 fromP. knowlesi,P. chabaudiorP. berghei. The GLDH ofP. falciparumwas shown to be a cytosolic protein (by FAT) with a subunit molecular weight of approximately 49000 Da (by immunoprecipitation) having a pre dominantly hexameric form (by sucrose density gradient). Implications of the conserved sequences of GLDHs and other enzymes are discussed.