Genetics of acid adaptation in oral streptococci

Crit Rev Oral Biol Med. 2001;12(4):301-14. doi: 10.1177/10454411010120040201.


A growing body of information has provided insights into the mechanisms by which the oral streptococci maintain their niches in the human mouth. In at least one case, Streptococcus mutans, the organism apparently uses a panel of proteins to survive in acidic conditions while it promotes the formation of dental caries. Oral streptococci, which are not as inherently resistant to acidification, use protective schemes to ameliorate acidic plaque pH values. Existing information clearly shows that while the streptococci are highly related, very different strategies have evolved for them to take advantage of their particular location in the oral cavity. The picture that emerges is that the acid-adaptive regulatory mechanisms of the oral streptococci differ markedly from those used by Gram-negative bacteria. What future research must determine is the extent and complexity of the acid-adaptive systems in these organisms and how they permit the organisms to maintain themselves in the face of a low-pH environment and the microbial competition present in their respective niches.

Publication types

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

MeSH terms

  • Acids / metabolism
  • Adaptation, Physiological / genetics
  • Adenosine Triphosphatases / biosynthesis
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / physiology
  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / genetics
  • Bacterial Proteins / physiology
  • DNA Repair
  • Gene Expression Regulation, Enzymologic
  • Genes, Bacterial
  • Humans
  • Hydrogen-Ion Concentration
  • Hydrolases / biosynthesis
  • Hydrolases / genetics
  • Hydrolases / physiology
  • Mouth / microbiology*
  • Streptococcus / enzymology
  • Streptococcus / genetics*
  • Streptococcus / physiology*
  • Urease / biosynthesis
  • Urease / genetics
  • Urease / physiology


  • Acids
  • Bacterial Proteins
  • Hydrolases
  • Urease
  • arginine deiminase
  • Adenosine Triphosphatases