Specificity of salivary-bacterial interactions: II. Evidence for a lectin on Streptococcussanguis with specificity for a NeuAcα2,3Ga1β1,3Ga1NAc sequence

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Abstract

Evidence is presented for the presence of a lectin on Streptococcussanguis with specificity towards the major acidic oligosaccharide of human salivary mucin. Based upon hemagglutination inhibition studies, the strongest inhibitor was NeuAcα2,3Galβ1,3GalNAcol ⪢ NeuAcα2,3Galβ1,4Glc ⪢ NeuAc > Gal. Interactions were not heat sensitive or charge dependent, and were not affected by the presence of bacterial cell associated neuraminidase. The lectin could be extracted from Streptococcussanguis with lithium 3,5-diiodosalicylate (LIS). Incubation of LIS extracts with carbohydrate ligands demonstrated that the specificity of binding was NeuAcα2,3Galβ1,3[3H-]GalNAcol ⪢ Galβ1,3[3H-]GalNAcol.

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