Abstract
Summary
Glycoproteins extracted in water-soluble form from rhesus monkey erythrocytes were shown to inhibit hemagglutination by measles virus. PAGE analysis of glycoproteins from erythrocyte membranes and in LIS-ph extracts showed that lower-molecular-weight glycoproteins readily formed aggregates which resisted dissociation with SDS and 2-ME at 100°. Preferential binding of isolated glycoproteins of erythrocyte membranes to purified virus was demonstrated even though all of these inhibited hemagglutination to some extent. Data presented here suggest that specific forms or configurations of membrane glycoproteins constitute receptors for measles virus.
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