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A 23 kDa membrane glycoprotein bearing NeuNAc{alpha}2-3Gal{beta}1-3GalNAc O-linked carbohydrate chains acts as a receptor for Streptococcus sanguis OMZ 9 on human buccal epithelial cells |
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| Authors: | Neeser Jean-Richard; Grafstrm Roland C; Woltz Arlerre; Brassart Dominique; Fryder Vincent; Guggenheim Bernhard |
| Institution: | Nestl Research Centre, Nestec Limited Vers-chez-les-Blanc, PO Box 44, CH-1000 Lausanne 26, Switzerland 1Institute of Environmental Medicine, Division of Toxicology, Karolinska Institute Box 210, S-17177 Stockholm, Sweden 2Department of Oral Microbiology and General Immunology, Dental Institutc, University of Zrich CH-8038 Zrich, Switzerland |
| Abstract: | Streptococcus sanguis colonizes several human oral surfaces,including both hard and soft tissues. Large salivary mucin likeglycoproteins bearing sialic acid residues are known to bindvarious S.sanguis strains. However, the molecular basis forthe adhesion of S.sanguis to human buccal epithelial cells (HBEC)has not been established. The present study shows that S.sanguisOMZ 9 binds to exfoliated HBEC in a sialic acid-sensitive manner.The desialylation of such cells invariably abolhhes adhesionof S.sanguis OMZ 9 to the cell surface. A soluble glycopeptidebearing short sialylated O-linked carbohydrate chains behavesas a potent inhibitor of the attachment of S.sanguis OMZ 9 toexfoliated HBEC. The resialylation of desialylated HBEC withCMP-sialic acid and Galß1,3GalNAc |
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