Streptococcus mutans F-type H+-transporting ATPase (F-ATPase)

The Streptococcus mutans F-type H+-transporting ATPase (F-ATPase) is a multi-subunit, membrane-bound enzyme complex that serves as a primary mechanism for acid tolerance in this major dental pathogen (Biointerfaceresearch.com, 2022; ASM.org, 2021). Unlike the F-ATPases in many other organisms that primarily synthesize ATP, the S. mutans enzyme functions predominantly as a proton pump, utilizing ATP hydrolysis to extrude protons from the cytoplasm into the extracellular environment (ASM.org, 2021; NIH.gov, 1998). This activity is essential for maintaining pH homeostasis, allowing the bacterium to survive and remain metabolically active in the highly acidic conditions of dental plaque (NIH.gov, 2019; NIH.gov, 2004). Because aciduricity is a key virulence factor for the development of dental caries, the F-ATPase is a significant therapeutic target (Frontiers in Microbiology, 2022; NIH.gov, 2015). Inhibitors such as certain polyphenols (e.g., piceatannol and curcumin) and fluoride can disrupt this proton-pumping mechanism, leading to intracellular acidification and the inhibition of bacterial growth (Frontiers in Microbiology, 2022; NIH.gov, 2019; NIH.gov, 2023). Targeting this enzyme offers a strategy to selectively impair the cariogenic potential of S. mutans while potentially minimizing effects on less acid-tolerant, health-associated oral streptococci (NIH.gov, 1998; NIH.gov, 2004).

Other names

F1F0-ATPaseH+-translocating ATPaseProton-pumping ATPaseATP synthaseH+-ATPase

Inhibition of the proton-pumping activity of the F-ATPase, which prevents the extrusion of H+ ions from the cytoplasm. This leads to intracellular acidification and the loss of acid tolerance, ultimately inhibiting the growth and survival of the bacterium in the acidic environment of dental plaque.