PLASMODIUM-FALCIPARUM - THROMBOSPONDIN MEDIATES PARASITIZED ERYTHROCYTE BAND 3-RELATED ADHESIN BINDING

Plasmodium falciparum-parasitized red sells attach to endothelial cell s through several receptor-adhesin pairs. One of the adhesins on the s urface of malaria-infected red blood cell is the modified band 3 molec ule. We tested a synthetic peptide (HPLQKTY) based on a peptidic seque nce of human band 3 protein to determine whether CD36 or thrombospondi n is a receptor for the band 3-related adhesin. Although both CD36 and thrombospondin can bind parasitized cells independently, the HPLQKTY peptide and a monoclonal antibody (3H3) that recognizes the HPLQKTY se quence blocked only the adhesion of parasitized red cells to thrombosp ondin. The binding of thrombospondin, but not CD36, to the immobilized multiple antigen peptide-conjugated HPLQKTY was dependent on the conc entration of the immobilized peptide. It would appear therefore, that thrombospondin is a receptor for the band 3-related cytoadhesion of pa rasitized erythrocytes. (C) 1998 Academic Press.