Helicobacter pylori membrane proteins and enzymes

Helicobacter pylori membrane proteins and enzymes encompass a broad array of molecular factors that enable the bacterium to colonize the hostile, acidic environment of the human stomach. A central component is the enzyme urease, which catalyzes the hydrolysis of urea into ammonia and carbon dioxide, effectively neutralizing local gastric acid to facilitate bacterial survival (Mobley et al., 1995). Additionally, outer membrane proteins (OMPs) such as BabA and SabA serve as adhesins, allowing the pathogen to bind specifically to the gastric epithelium and resist mechanical clearance (Ishijima et al., 2011). Virulence factors like the vacuolating cytotoxin (VacA) and the cytotoxin-associated gene A (CagA) protein are also associated with the membrane or secreted via specialized systems to disrupt host cell signaling and induce tissue damage (Cover & Blanke, 2005). These proteins and enzymes are the primary targets for diagnostic assays, such as the urea breath test, and are the focus of multi-drug eradication regimens involving antibiotics and bismuth compounds (Malfertheiner et al., 2022). Understanding the structural and functional diversity of these targets is essential for addressing the global challenge of antibiotic-resistant H. pylori infections and their progression to gastric cancer.

Other names

H. pylori surface proteinsH. pylori virulence factorsH. pylori membrane-associated enzymesH. pylori outer membrane proteins

Inhibition of bacterial urease activity, disruption of cell wall synthesis via penicillin-binding proteins, inhibition of the 50S ribosomal subunit to prevent protein synthesis, DNA strand breakage, and interference with bacterial adhesion to the gastric mucosa.