Characterization of the Streptococcus sobrinus acid-stress response by interspecies microarrays and proteomics

Mol Oral Microbiol. 2010 Oct;25(5):331-42. doi: 10.1111/j.2041-1014.2010.00580.x.

Abstract

Streptococcus mutans and Streptococcus sobrinus are considered the primary organisms responsible for human dental caries. The ability to generate acids and to adapt to low pH conditions is directly associated with the cariogenic potential of these bacteria. To survive acidic conditions, both species have been shown to mount an acid-tolerance response (ATR). However, previous characterization of the S. sobrinus ATR identified critical differences in the mechanisms of acid adaptation between S. mutans and S. sobrinus. Here, interspecies microarray and proteomic approaches were used to identify novel, previously unrecognized genes and pathways that participate in the S. sobrinus acid-stress response. The results revealed that, among other things, metabolic alterations that enhance energy generation and upregulation of the malolactic fermentation enzyme activity constitute important acid-resistance properties in S. sobrinus. Some of these acid adaptive traits are shared by S. mutans and might be considered optimal targets for therapeutic treatments designed to control dental caries.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adaptation, Physiological / genetics
  • Bacterial Proteins / genetics*
  • Gene Expression Profiling
  • Gene Expression Regulation, Bacterial*
  • Glycolysis / genetics*
  • Hydrogen-Ion Concentration
  • Lactic Acid / metabolism
  • Malate Dehydrogenase / genetics*
  • Malate Dehydrogenase / metabolism
  • Nucleic Acid Hybridization
  • Oligonucleotide Array Sequence Analysis
  • Species Specificity
  • Streptococcus mutans / genetics
  • Streptococcus mutans / metabolism
  • Streptococcus sobrinus / genetics*
  • Streptococcus sobrinus / metabolism*
  • Tandem Mass Spectrometry

Substances

  • Bacterial Proteins
  • Lactic Acid
  • malolactic enzyme
  • Malate Dehydrogenase