Abstract
Glycophorin, the major sialoglycoprotein in the human erythrocyte surface membrane, can serve as a red cell receptor for both wheat-germ agglutinin (WGA) and encephalomyocarditis (EMC) virus since glycophorin bound to WGA-Sepharose can at the same time bind EMC virus. In contrast, glycophorin bound to WGA-Sepharose cannot bind EMC virus in the presence of SDS. The evidence suggests that virus binding to glycophorin-WGA-Sepharose occurred in the absence of SDS because glycophorin was present in aggregated complexes which were large enough either to accommodate both EMC virus and WGA at the same time, or alternatively to provide sufficient attachment sites for multivalent binding of virions.