Salivary receptors for the proline-rich protein-binding and lectin-like adhesins of oral actinomyces and streptococci

J Dent Res. 2004 Jun;83(6):505-10. doi: 10.1177/154405910408300614.

Abstract

Colonization of the tooth surface by actinomyces and viridans group streptococci involves the attachment of these bacteria to adsorbed salivary components of the acquired enamel pellicle. The hypothesis that this attachment depends on specific adhesins has now been assessed from the binding of bacteria with well-defined adhesive properties to blots of SDS-PAGE-separated parotid and submandibular-sublingual (SM-SL) saliva. Streptococcus sanguis and type 2 fimbriated Actinomyces naeslundii, which bound terminal sialic acid and Galbeta1-3GalNAc, respectively, recognized only a few SM-SL salivary components, primarily MG2. In contrast, type 1 fimbriated A. naeslundii and S. gordonii, which bound purified proline-rich proteins (PRPs), recognized several other components from both SM-SL and parotid saliva. Significantly, bacteria that lacked PRP-binding and the lectin-like activities detected by binding to MG2 failed to bind any immobilized salivary component. These findings suggest the involvement of specific adhesins in bacterial recognition of many adsorbed salivary proteins and glycoproteins.

MeSH terms

  • Actinomyces / metabolism*
  • Adhesins, Bacterial / metabolism*
  • Bacterial Adhesion
  • Dental Pellicle / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Fimbriae, Bacterial / metabolism
  • Glycoproteins / metabolism
  • Humans
  • Lectins / metabolism*
  • Mouth / microbiology*
  • Peptides / metabolism*
  • Phosphoproteins / metabolism*
  • Proline / metabolism*
  • Proline-Rich Protein Domains
  • Protein Binding
  • Salivary Proteins and Peptides / metabolism*
  • Streptococcus / metabolism
  • Streptococcus sanguis / metabolism*

Substances

  • Adhesins, Bacterial
  • Glycoproteins
  • Lectins
  • Peptides
  • Phosphoproteins
  • Salivary Proteins and Peptides
  • Proline