The red cell sialoglycoproteins (glycophorins, <latex>$\alpha$</latex>(A), <latex>$\delta$</latex>(B) and <latex>$\beta$</latex> and <latex>$\gamma$</latex>(C)) play a crucial role in the invasion of human red cells by merozoites of Plasmodium falciparum. Red cells deficient in any of the glycophorins, including <latex>$\beta$</latex> (also known as glycoconnectin), resist infection by this parasite to varying degrees. These cells and other naturally occurring well-characterized glycophorin variants provide extremely powerful tools to dissect the role of these molecules in invasion. The binding of merozoites to human red cells appears analogous to the binding of wheatgerm agglutinin to sialoglycoconjugates. In both systems O- and N-linked oligosaccharides may be involved. Membrane lipid has not been implicated as a receptor for merozoites, but may instead non-specifically modify binding, as may electrostatic and hydrophobic interactions. The results of data using monoclonal antibodies and lectins, although possibly helpful in identifying specific determinants, must be interpreted with caution. Overall the data suggest that the red cell receptors for all strains of P. falciparum tested to date are located on the glycophorins. Accordingly these putative receptors have been used to affinity-purify complementary parasite components which may yet prove to be of protective immunological significance in a vaccine.