Bacterial H+-translocating F1F0-ATPase (F-ATPase)

The bacterial H+-translocating F1F0-ATPase is a multi-subunit enzyme complex essential for the survival of cariogenic bacteria, such as Streptococcus mutans, in the low-pH environment of dental plaque (Belli & Marquis, 1991, Applied and Environmental Microbiology). Unlike mitochondrial ATP synthases that primarily generate ATP, the F-ATPase in these bacteria often functions as a proton pump, utilizing ATP hydrolysis to extrude protons and maintain a neutral internal pH (Hamilton & Buckley, 1991, Oral Microbiology and Immunology). This mechanism, known as aciduricity, allows cariogenic pathogens to outcompete commensal bacteria and continue lactic acid production, which leads to tooth enamel demineralization (Kuhnert & Quivey, 2003, Journal of Bacteriology). Targeting this enzyme offers a strategy to selectively inhibit the fitness of acid-tolerant pathogens without necessarily killing the entire oral microbiome (Jeon et al., 2011, Evidence-Based Complementary and Alternative Medicine). Various natural compounds, including specific polyphenols and flavonoids, have demonstrated inhibitory effects on this target, making it a focus for anti-caries therapeutic development (Gregoire et al., 2007, Journal of Applied Microbiology). Inhibition of this enzyme leads to the accumulation of protons within the cell, disrupting metabolic processes and eventually causing cell death under acidic conditions.

Other names

F1F0-ATPaseProton-translocating ATPaseH+-ATPaseATP synthaseF-type ATPaseStreptococcus mutans F-ATPase

Inhibition of the F1F0-ATPase enzyme complex prevents the extrusion of protons from the bacterial cytoplasm, leading to intracellular acidification and loss of viability in the acidic environment of dental plaque (Belli & Marquis, 1991, Applied and Environmental Microbiology).