Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans.
Four highly purified salivary glycoproteins were used to study salivary-bacterial interactions. One pair of glycoproteins was mucin-like in composition, whereas the second pair was not. By an agglutination assay, it was found that only the mucin-glycoproteins agglutinated Streptococcus sanguis and S. mutans. Removal of sialic acid from these molecules resulted in a loss of agglutination of S. sanguis but not of S. mutans. The agglutination phenomenon was shown to require a salivary macromolecule of at least 150,000 daltons.
D000371:Agglutination; D000818:Animals; D005260:Female; D006023:Glycoproteins / Q000032:analysis / Q000276:immunology*; D000882:Haplorhini; D006801:Humans; D008251:Macaca; D008970:Molecular Weight; D009077:Mucins / Q000276:immunology; D012471:Salivary Proteins and Peptides / Q000032:analysis / Q000276:immunology*; D012794:Sialic Acids / Q000276:immunology*; D013295:Streptococcus mutans / Q000276:immunology*; D013298:Streptococcus sanguis / Q000276:immunology*
D006023:Glycoproteins; D009077:Mucins; D012471:Salivary Proteins and Peptides; D012794:Sialic Acids