Helicobacter pylori F1Fo-ATP synthase (H. pylori ATP synthase)

The Helicobacter pylori F1Fo-ATP synthase is a critical multi-subunit enzyme complex that catalyzes the synthesis of adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate (UniProt: P56161). This process is powered by the proton motive force generated across the bacterial inner membrane (PubMed: 31235518). In the highly acidic environment of the human stomach, this machinery is essential for H. pylori to maintain its internal pH and meet the energetic demands required for colonization and persistence (PubMed: 25514934). As H. pylori is the primary causative agent of chronic gastritis, peptic ulcers, and gastric cancer, its ATP synthase has emerged as a promising target for novel antimicrobial therapies (PubMed: 24343179). Drugs such as diarylquinolines or other experimental inhibitors bind to the enzyme—often targeting the c-ring of the Fo sector—to physically block the rotation of the motor, thereby halting ATP production (PubMed: 31235518). This energy depletion is bactericidal, offering a mechanism to combat multi-drug resistant strains of H. pylori. Research into this target focuses on achieving high selectivity to avoid interfering with human mitochondrial ATP synthase, which shares structural similarities (PubMed: 25514934). Consequently, this enzyme represents a cornerstone for developing next-generation narrow-spectrum antibiotics.

Other names

F-type ATPaseF1Fo-ATPaseProton-translocating ATP synthaseATP synthase complex

Inhibition of the Fo subunit rotation or F1 catalytic activity, preventing the synthesis of ATP from ADP and inorganic phosphate, thereby depleting the bacterium of its primary energy source (PubMed: 31235518).