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<i>Plasmodium falciparum-</i>infected erythrocytes (<i>Pf</i>IEs) present <i>P. falciparum</i> erythrocyte membrane protein 1 proteins (<i>Pf</i>EMP1s) on the cell surface, via which they cytoadhere to various endothelial cell receptors (ECRs) on the walls of human blood vessels. This prevents the parasite from passing through the spleen, which would lead to its elimination. Each <i>P. falciparum</i> isolate has about 60 different <i>Pf</i>EMP1s acting as ligands, and at least 24 ECRs have been identified as interaction partners. Interestingly, in every parasite genome sequenced to date, at least 75% of the encoded <i>Pf</i>EMP1s have a binding domain for the scavenger receptor CD36 widely distributed on host endothelial cells and many other cell types. Here, we discuss why the interaction between <i>Pf</i>IEs and CD36 is optimal to maintain a finely regulated equilibrium that allows the parasite to multiply and spread while causing minimal harm to the host in most infections.