Allaway G P, Burness A T
J Virol. 1986 Sep;59(3):768-70. doi: 10.1128/JVI.59.3.768-770.1986.
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.
先前关于脑心肌炎（EMC）病毒与人红细胞结合的研究得出结论，血型糖蛋白（一类人红细胞唾液酸糖蛋白）作为EMC病毒的受体。有证据表明，主要的血型糖蛋白种类，即血型糖蛋白A，是EMC病毒与人红细胞结合的受体。对血型糖蛋白A和B的结构以及经胰凝乳蛋白酶和胰蛋白酶处理红细胞后释放的唾液酸糖肽进行比较，证实了我们之前的推测（A.T.H.伯内斯和I.U.帕尔多，《普通病毒学杂志》64:1137 - 1148，1983年），即EMC病毒与血型糖蛋白A的结合涉及包含第35至大约70位氨基酸（从氨基末端开始编号）的区域，其中四个氨基酸（第37、44、47和50位氨基酸）是糖基化的。此外，我们提供证据表明，在苏氨酸 - 37上带有寡糖侧链的包含第35至39位氨基酸的片段对于EMC病毒的结合尤为重要。
