The biosynthesis of the knob protein and a 65 000 dalton histidine-rich polypeptide of Plasmodium falciparum.

Previous studies have shown the association of an 80 kDa polypeptide (KP) with the knobs which develop on the membranes of erythrocytes infected with Plasmodium falciparum. KP was also found to share antigenic determinants with the histidine-rich protein of Plasmodium lophurae. In this study, ring stages of knobby (K+) and knobless (K-) variants of P. falciparum were used in pulse-chase experiments to elucidate the temporal sequence of the biosynthesis of KP. Analysis of radiolabeled parasite-polypeptides on SDS-polyacrylamide gels indicated that pulse-labeled KP has the electrophoretic mobility of a 75 kDa polypeptide and is subsequently chased to an apparently 80-85 kDa form. In addition to KP, antibodies raised against HRP immunoprecipitated a 65 kDa histidine-rich polypeptide from K- as well as K+ parasites. Differential incorporation of selected amino acids into KP and the 65 kDa polypeptide revealed some distinct differences between these two polypeptides as well as from HRP.