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Helicobacter pylori surface adhesins and surface antigens represent a heterogeneous group of outer membrane proteins (OMPs) essential for the bacterium's survival and pathogenicity within the human stomach. Key members include the Blood group antigen-binding adhesin (BabA), Sialic acid-binding adhesin (SabA), and Outer inflammatory protein A (OipA), which facilitate high-affinity binding to the gastric epithelium (Kusters et al., 2006, PMID: 16816330). These proteins allow H. pylori to evade mechanical clearance by gastric peristalsis and mucus turnover, establishing a niche for chronic infection. Furthermore, surface antigens such as Urease and Flagellin are critical for acid neutralization and motility, respectively, while others like CagA and VacA act as virulence factors that disrupt host cell signaling (Ansari & Yamaoka, 2019, PMID: 31336613). Therapeutically, these surface components are primary targets for vaccine development and anti-adhesive agents, such as bismuth salts, which aim to prevent colonization or enhance the efficacy of antibiotic regimens (Sutton & Boag, 2019, PMID: 30631555). However, the high genetic diversity and antigenic variation among H. pylori strains present significant challenges for universal vaccine design and long-term therapeutic success.
Inhibition of bacterial attachment to gastric mucosa, neutralization of virulence factors, and induction of protective immune responses.
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