Helicobacter pylori lipase (EstV)

Helicobacter pylori lipase is an extracellular enzyme secreted by the bacterium Helicobacter pylori, which is a primary cause of chronic gastritis and peptic ulcer disease [1][2]. The enzyme plays a crucial role in pathogenesis by hydrolyzing the lipids, specifically triacylglycerols and phospholipids, within the gastric mucus layer [2][3]. This enzymatic degradation reduces the viscosity and hydrophobicity of the mucus barrier, facilitating bacterial penetration and colonization of the underlying gastric epithelium [2][5]. By compromising this protective layer, the lipase also exposes the gastric mucosa to the corrosive effects of stomach acid and pepsin, leading to tissue damage and inflammation [2][3]. Although current clinical treatments for H. pylori primarily focus on antibiotic eradication and acid suppression, this lipase is identified as a significant virulence factor and a potential target for therapeutic intervention [1][2]. Experimental studies have shown that certain antiulcer agents, such as sucralfate and ranitidine bismuth citrate, as well as natural compounds like glycyrrhizic acid, can inhibit the enzyme's activity [2]. Inhibiting Helicobacter pylori lipase offers a strategy to preserve the gastric mucus barrier and mitigate the bacteria's colonization potential [1][2].

Other names

H. pylori lipaseExtracellular lipaseLipase EstVHP0739Triacylglycerol lipaseEsterase V

Inhibition of the lipase prevents the enzymatic degradation of the protective gastric mucus layer, thereby reducing the ability of the bacterium to colonize the gastric epithelium and protecting the mucosa from acid-induced damage.