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pH regulation by Streptococcus mutans.

S G Dashper1, E C Reynolds

  • 1Biochemistry and Molecular Biology Unit, School of Dental Science, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Victoria, Australia.

Journal of Dental Research
|May 1, 1992
PubMed
Summary
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Streptococcus mutans glycolysis thrives internally at pH 7.0, but adapts to external acidity by maintaining a pH gradient. This process relies on potassium ion uptake, suggesting a regulated proton-translocating ATPase.

Area of Science:

  • Microbiology
  • Biochemistry
  • Cell Physiology

Background:

  • Streptococcus mutans is a key cariogenic bacterium.
  • Understanding its metabolic regulation under acidic conditions is crucial for dental caries prevention.

Purpose of the Study:

  • To determine the intracellular pH (pHi) optimum for glycolysis in S. mutans.
  • To investigate the mechanisms by which S. mutans maintains glycolytic activity at low extracellular pH (pHo).

Main Methods:

  • Utilized the ionophore gramicidin to manipulate pHi.
  • Measured glycolytic activity across a range of pHi and pHo.
  • Assessed transmembrane pH gradient (delta pH) maintenance.
  • Investigated potassium ion uptake and its dependence on ATP and proton motive force (delta p).

Related Experiment Videos

  • Examined the effect of N,N'-dicyclohexylcarbodiimide (DCCD) on delta pH.

    • Main Results:

    • The pHi optimum for glycolysis was 7.0; activity ceased at pHi 5.0.
    • Glycolysis showed a broader optimum at pHo 6.0, indicating adaptation to external acidity.
    • S. mutans maintained a significant delta pH (1.37 units) at pHo 5.0.
    • Delta pH maintenance was dependent on extracellular potassium ion concentration, with rapid uptake observed.
    • Potassium uptake required ATP and delta p; DCCD partially collapsed delta pH.

    Conclusions:

    • S. mutans actively regulates its internal pH to optimize glycolysis.
    • The bacterium employs a potassium-dependent mechanism to maintain a favorable delta pH at low pHo.
    • Results suggest the involvement of a proton-translocating F1Fo-ATPase regulated by intracellular pH and transmembrane electrical potential (delta psi).