CD36 directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes.

Erythrocytes infected with P. falciparum express knob-like adhesion structures that allow the infected cells to cling to the postcapilliary endothelium of characteristic host organs. At present, the mechanism of cytoadherence is not fully understood. While parasitized erythrocytes have been shown to specifically bind to the platelet/matrix molecule thrombospondin, adherence to suitable target cells can also be blocked by monoclonal antibody OKM5, which recognizes a surface molecule expressed by hematopoietic cells and endothelium. In apparent reconciliation of these findings, it has been reported that the OKM5 antigen (CD36) is a receptor for thrombospondin. Here we report that expression of a CD36 cDNA clone in COS cells supports cytoadherence of parasitized erythrocytes but does not support increased binding of purified human thrombospondin.