Adherence of Plasmodium falciparum parasitized erythrocytes to the microvascular endothelium is mediated by different receptors expressed by endothelial cells. The study of the adherence of P. falciparum-infected erythrocytes to Saimiri monkey brain microvascular endothelial cells revealed the presence of an additional receptor, which was identified and further characterized. This receptor was also found on the surface of primary human lung endothelial cells (HLEC). We developed two mAbs to this receptor which very efficiently blocked the adherence of parasite strains to Saimiri brain endothelial cells (SBEC). The ability of these mAb to bind to SBEC was partially blocked by chondroitin-4-sulphate (CSA). Competitive inhibition assays on adherence of parasitized red blood cells (PRBC) showed that CSA, but not hyaluronic acid, chondroitin-6-sulphate, dermatan sulphate, keratane sulphate, heparan sulphate or chondroitin-4S-disaccharide, was able to almost completely inhibit PRBC adherence. The same effect was obtained with chondroitinase ABC and AC, but not B, hyaluronidase or heparinase. These results strongly suggest that a member of the chondroitin-glycosaminoglycan family, CSA, represents an additional receptor used by P. falciparum PRBC to cytoadhere to microvascular endothelial cells.