Site of attachment of encephalomyocarditis virus on human erythrocytes.
Previous studies of the attachment of encephalomyocarditis (EMC) virus to human erythrocytes concluded that the glycophorins, a family of human erythrocyte sialoglycoproteins, act as EMC virus receptors. Evidence is presented that the major glycophorin species, glycophorin A, is the receptor for EMC virus attachment to human erythrocytes. Comparison of the structures of glycophorins A and B and sialoglycopeptides released by chymotrypsin and trypsin treatment of erythrocytes confirmed our previous suggestion (A. T. H. Burness and I. U. Pardoe, J. Gen. Virol. 64:1137-1148, 1983) that attachment of EMC virus to glycophorin A involves the region containing amino acids 35 to approximately 70 (numbered from the NH2 terminus), four of which (amino acids 37, 44, 47, and 50) are glycosylated. In addition, we provide evidence that the segment containing amino acids 35 to 39 with an oligosaccharide side chain on threonine-37 is particularly important for EMC virus attachment.
D002918:Chymotrypsin; D004686:Encephalomyocarditis virus / Q000378:metabolism*; D004912:Erythrocytes / Q000382:microbiology*; D006021:Glycophorins / Q000378:metabolism*; D006801:Humans; D009439:Neuraminidase; D011991:Receptors, Virus / Q000378:metabolism*; D012795:Sialoglycoproteins / Q000378:metabolism*; D014357:Trypsin
D006021:Glycophorins; D011991:Receptors, Virus; D012795:Sialoglycoproteins; D009439:Neuraminidase; D002918:Chymotrypsin; D014357:Trypsin