Helicobacter pylori extracellular lipase (Hpl)

Helicobacter pylori extracellular lipase is a secreted enzyme that plays a pivotal role in the pathogenesis of H. pylori infection by degrading the protective gastric mucosal barrier (Slomiany et al., 1992, Lipids). The enzyme catalyzes the hydrolysis of triglycerides and phospholipids, which are essential components of the gastric mucus, leading to its thinning and increased susceptibility of the underlying epithelium to acid-induced injury (UniProt, HP0739). This enzymatic activity also releases fatty acids and lysophospholipids that can exert toxic effects on gastric epithelial cells and trigger inflammatory responses (Nakagawa et al., 2003, Journal of Gastroenterology and Hepatology). By compromising the integrity of the mucus layer, the lipase facilitates bacterial colonization and persistence within the harsh acidic environment of the stomach (Sharafutdinov et al., 2020, World Journal of Gastroenterology). Although not currently the primary target of standard triple therapy, this lipase is considered a significant therapeutic target for developing adjunctive treatments to mitigate mucosal damage and prevent the progression to peptic ulcers or gastric cancer. Experimental studies have demonstrated that lipase inhibitors, such as orlistat, can effectively reduce the enzyme's activity, suggesting a potential pathway for novel anti-virulence strategies (Slomiany et al., 1997, Biochemical and Molecular Medicine).

Other names

Triacylglycerol lipaseH. pylori lipaseGlycerol ester hydrolaseHP0739 lipase

Inhibition of the extracellular lipase enzyme prevents the enzymatic degradation of the gastric mucosal lipid barrier, thereby preserving the integrity of the stomach lining and reducing bacterial virulence.