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Enterovirus 70 Binds to Different Glycoconjugates Containing 2,3-Linked Sialic Acid on Different Cell Lines

Department of Biochemistry, Microbiology and Immunology,¹ Department of Cellular and Molecular Medicine, University of Ottawa, Faculty of Medicine, Ottawa, ON, Canada K1H 8M5,² University of Ottawa Eye Institute, Ottawa, ON, Canada K1H 8L6³

Received 6 July 2004/ Accepted 31 January 2005

Enterovirus 70 (EV70), the causative agent of acute hemorrhagic conjunctivitis, exhibits a restricted tropism for conjunctival and corneal cells in vivo but infects a wide spectrum of mammalian cells in culture. Previously, we demonstrated that human CD55 is a receptor for EV70 on HeLa cells but that EV70 also binds to sialic acid-containing receptors on a variety of other human cell lines. Virus recognition of sialic acid attached to underlying glycans by a particular glycosidic linkage may contribute to host range, tissue tropism, and pathogenesis. Therefore, we tested the possibility that EV70 binds to 2,3-linked sialic acid, like other viruses associated with ocular infections. Through the use of linkage-specific sialidases, sialyltransferases, and lectins, we show that EV70 recognizes 2,3-linked sialic acid on human corneal epithelial cells and on U-937 cells. Virus attachment to both cell lines is CD55 independent and sensitive to benzyl N-acetyl--D-galactosaminide, an inhibitor of O-linked glycosylation. Virus binding to corneal cells, but not U-937 cells, is inhibited by proteinase K, but not by phosphatidylinositol-specific phospholipase C treatment. These results are consistent with the idea that a major EV70 receptor on corneal epithelial cells is an O-glycosylated, non-glycosyl phosphatidylinositol-anchored membrane glycoprotein containing 2,3-linked sialic acid, while sialylated receptors on U-937 cells are not proteinaceous.

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