Isolation and Characterization of Erythrocyte Receptors for Measles Virus

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Abstract
Glycoproteins extracted in water-soluble form from rhesus monkey erythrocytes inhibited hemagglutination by measles virus. PAGE [polyacrylamide gel electrophoresis] analysis of glycoproteins from erythrocyte membranes and in LIS-ph [lithium diiodosalicylate-phenol] extracts showed that lower MW glycoproteins readily formed aggregates which resisted dissociation with SDS [sodium dodecyl sulfate] and 2-ME [mercaptoethanol] at 100.degree. C. Preferential binding of isolated glycoproteins of erythrocyte membranes to purified virus was demonstrated even though all of these inhibited hemagglutination to some extent. Specific forms or configurations of membrane glycoproteins may constitute receptors for measles virus.

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