Lipoprotein receptors in oral streptococci

Dev Biol Stand. 1995:85:333-41.

Abstract

Streptococcus gordonii produces cell-surface lipopolypeptides that have been implicated in the determination of cell adherence and aggregation properties. SarA lipopolypeptide produced by S. gordonii is highly similar to the oligopeptide-binding protein AmiA in Streptococcus pneumoniae and to the OppA and SpoOKA oligopeptide-binding proteins in Bacillus subtilis. Insertional mutagenesis was used to inactivate the genes encoding SarA (76kDa) lipoprotein and a related 78-kDa lipoprotein denoted SarG. SarA- mutants were defective in serum-induced aggregation, competence, growth on complex nitrogen sources, and ability to colonize the oral cavity. Conversely, SarG- mutants were unaltered in the above properties, but were deficient in growth on simple nitrogen sources. It is proposed that SarA plays a central role in environmental sensing of extracellular factors by streptococci leading to modulation of cell-surface composition and growth responses of cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / metabolism
  • Bacterial Adhesion / genetics
  • Bacterial Adhesion / physiology
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Chromosome Mapping
  • Genes, Bacterial
  • Humans
  • Lipoproteins / genetics
  • Lipoproteins / metabolism
  • Mouth / microbiology
  • Mutagenesis
  • Phenotype
  • Receptors, Lipoprotein / genetics
  • Receptors, Lipoprotein / metabolism*
  • Saliva / microbiology
  • Streptococcus / genetics
  • Streptococcus / metabolism*
  • Trans-Activators*

Substances

  • Adhesins, Bacterial
  • Bacterial Proteins
  • Lipoproteins
  • Receptors, Lipoprotein
  • SarA protein, bacterial
  • Trans-Activators