The human anion transport protein, band 3, contains a CD36-like binding domain for Plasmodium falciparum-infected erythrocytes.

Epitope mapping of a murine monoclonal antibody (mAb), 5H12, prepared against live Plasmodium falciparum-infected red blood cells indicated that the epitope consisted of amino acid residues 474-487 of the human anion transport protein, band 3. mAb 5H12 enhanced cytoadherence, but inhibited the CD36-like mediated rosetting. A synthetic peptide based on the sequence of the epitope (FSFCETNGLE) blocked both rosetting and cytoadherence, suggesting that this amino acid sequence may form the CD36-like receptor. The CD36-like region of band 3 was antigenically distinct from platelet or endothelial CD36.