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

Infect Immun. 1978 Jan;19(1):107-15. doi: 10.1128/iai.19.1.107-115.1978.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Agglutination*
  • Animals
  • Female
  • Glycoproteins / analysis
  • Glycoproteins / immunology*
  • Haplorhini
  • Humans
  • Macaca
  • Molecular Weight
  • Mucins / immunology
  • Salivary Proteins and Peptides / analysis
  • Salivary Proteins and Peptides / immunology*
  • Sialic Acids / immunology*
  • Streptococcus mutans / immunology*
  • Streptococcus sanguis / immunology*

Substances

  • Glycoproteins
  • Mucins
  • Salivary Proteins and Peptides
  • Sialic Acids