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Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells

Glycoconjugates containing the disaccharide unit GlcNAc beta 1 leads to 3Gal beta were suggested as receptors for pneumococci adhering to human pharyngeal epithelial cells. The receptor activity was detected both by inhibition of adhesion by an excess of free oligosaccharide and by induction or incr...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187347/
https://www.ncbi.nlm.nih.gov/pubmed/6886624
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description Glycoconjugates containing the disaccharide unit GlcNAc beta 1 leads to 3Gal beta were suggested as receptors for pneumococci adhering to human pharyngeal epithelial cells. The receptor activity was detected both by inhibition of adhesion by an excess of free oligosaccharide and by induction or increase of adhesion after coating of target cells with glycolipid. Studies with free natural and synthetic oligosaccharides identified the disaccharide GlcNAc beta 1 leads to 3Gal beta as one critical binding site. The specificity of recognition was shown inter alia by the lack of inhibitory activity of GlcNAc beta 1 leads to 4Gal beta, which differs only in the linkage of the two sugars. Specific interference with pneumococcal adhesion by administration of soluble receptor sugar may improve our understanding of the role of adhesion in vivo.
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spelling pubmed-21873472008-04-17 Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells J Exp Med Articles Glycoconjugates containing the disaccharide unit GlcNAc beta 1 leads to 3Gal beta were suggested as receptors for pneumococci adhering to human pharyngeal epithelial cells. The receptor activity was detected both by inhibition of adhesion by an excess of free oligosaccharide and by induction or increase of adhesion after coating of target cells with glycolipid. Studies with free natural and synthetic oligosaccharides identified the disaccharide GlcNAc beta 1 leads to 3Gal beta as one critical binding site. The specificity of recognition was shown inter alia by the lack of inhibitory activity of GlcNAc beta 1 leads to 4Gal beta, which differs only in the linkage of the two sugars. Specific interference with pneumococcal adhesion by administration of soluble receptor sugar may improve our understanding of the role of adhesion in vivo. The Rockefeller University Press 1983-08-01 /pmc/articles/PMC2187347/ /pubmed/6886624 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
title Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
title_full Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
title_fullStr Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
title_full_unstemmed Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
title_short Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
title_sort identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187347/
https://www.ncbi.nlm.nih.gov/pubmed/6886624