Helicobacter pylori surface and thiol-containing enzymes

Helicobacter pylori surface and thiol-containing enzymes represent a collective group of bacterial proteins essential for the survival, colonization, and pathogenesis of H. pylori in the human stomach. This group includes the critical enzyme urease, which neutralizes gastric acid via urea hydrolysis, and various redox-active enzymes like thioredoxin reductase (TrxR) and alkyl hydroperoxide reductase (AhpC) that protect the pathogen from oxidative stress (Tsang et al., 2011; Wang et al., 2015). These enzymes are primary targets for bismuth-containing therapeutic agents, such as bismuth subsalicylate and colloidal bismuth subcitrate, which exert antimicrobial effects by binding to functional thiol (sulfhydryl) groups (Ge & Sun, 2007). This binding leads to the irreversible inactivation of the enzymes and disrupts bacterial metabolism and cell wall integrity (Cun & Sun, 2010). Targeting these proteins is a cornerstone of multi-drug regimens used to treat peptic ulcers and prevent gastric cancer. The multi-target nature of these interactions helps reduce the likelihood of the bacterium developing resistance compared to single-target antibiotics (Ge & Sun, 2007).

Other names

H. pylori thiol-dependent enzymesBismuth-binding proteins in H. pyloriH. pylori sulfhydryl-containing enzymes

Bismuth compounds bind with high affinity to the thiol groups of these enzymes, leading to irreversible inhibition of their catalytic activity and disruption of bacterial cell wall integrity and adherence (Ge & Sun, 2007; Tsang et al., 2011).