Helicobacter pylori cell surface and enzymes

Helicobacter pylori cell surface and enzymes represent a complex of therapeutic targets involved in the pathogenesis of gastric infections and peptic ulcer disease. The primary bacterial target is the enzyme urease, which H. pylori uses to neutralize gastric acid by producing ammonia, thereby creating a habitable microenvironment (Ge et al., 2007). Bismuth-based drugs, such as colloidal bismuth subcitrate, interact with these targets by inhibiting urease activity through the displacement of essential nickel ions and by disrupting the bacterial cell wall and cytoplasmic membrane (Tsang et al., 2011). Furthermore, these drugs prevent bacterial adhesion to the gastric epithelium and inhibit other secreted enzymes like lipases and proteases that damage the host mucosa (Lambert, 1991). On the host side, bismuth interacts with gastric mucus and proteins at ulcer sites to form a protective coating that shields the tissue from acid and pepsin (Marshall, 1991). This multi-faceted interaction makes the H. pylori cell surface and its enzymatic repertoire critical for the efficacy of bismuth-containing eradication regimens (StatPearls, 2023).

Other names

H. pylori ureaseH. pylori cell wallGastric mucosal barrierBacterial ureaseH. pylori surface proteins

Bismuth compounds exert bactericidal effects by inhibiting essential enzymes such as urease, catalase, and lipase, while also disrupting bacterial cell wall integrity and preventing adhesion to gastric epithelial cells (Ge et al., 2007; Tsang et al., 2011). Additionally, they provide cytoprotection by forming a bismuth-protein-mucus complex that acts as a physical barrier over gastric ulcers, protecting them from further degradation by acid and pepsin (Marshall, 1991).