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Enterovirus 70 binds to different glycoconjugates containing alpha 2,3-linked sialic acid on different cell lines
Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Faculty of Medicine, Ottawa, ON, Canada.
Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Faculty of Medicine, Ottawa, ON, Canada.
Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Faculty of Medicine, Ottawa, ON, Canada.
Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Faculty of Medicine, Ottawa, ON, Canada.
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2005 (English)In: Journal of Virology, ISSN 0022-538X, E-ISSN 1098-5514, Vol. 79, no 11, 7087-7094 p.Article in journal (Refereed) Published
Abstract [en]

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 andalpha; 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 andalpha; 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-andalpha;-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 andalpha; 2,3-linked sialic acid, while sialylated receptors on U-937 cells are not proteinaceous.

Place, publisher, year, edition, pages
American Society for Microbiology , 2005. Vol. 79, no 11, 7087-7094 p.
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Engineering and Technology
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URN: urn:nbn:se:liu:diva-70672DOI: 10.1128/JVI.79.11.7087-7094.2005ISI: 000229085400053OAI: oai:DiVA.org:liu-70672DiVA: diva2:441035
Available from: 2011-09-14 Created: 2011-09-14 Last updated: 2017-12-08

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