Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans

M. J. Levine, M. C. Herzberg, M. S. Levine, S. A. Ellison, M. W. Stinson, H. C. Li, T. van Dyke

Research output: Contribution to journalArticlepeer-review

130 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)107-115
Number of pages9
JournalUnknown Journal
Volume19
Issue number1
DOIs
StatePublished - 1978

Fingerprint Dive into the research topics of 'Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans'. Together they form a unique fingerprint.

Cite this