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Helicobacter pylori adhesin A (HpaA) is a surface-localized lipoprotein that serves as a critical colonization factor for the bacterium Helicobacter pylori in the human gastric environment (UniProt P0A0S5). It functions as a neuraminyllactose-binding hemagglutinin, mediating the essential step of bacterial attachment to the gastric epithelial cells (Evans et al., 1993, PubMed: 8406807). Due to its high conservation across various strains and its indispensable role in establishing infection, HpaA is a prominent target for the development of both prophylactic and therapeutic vaccines (Rossi et al., 2003, PubMed: 12819087). Experimental vaccine strategies involve using recombinant HpaA or its epitopes to induce a mucosal immune response that generates neutralizing antibodies (Liu et al., 2020, PubMed: 32670293). These antibodies are designed to block the interaction between HpaA and host cell receptors, thereby preventing the chronic inflammation associated with gastritis and peptic ulcers (Nyström et al., 2015, PubMed: 25581010). Although no HpaA-specific drugs are currently approved for clinical use, it remains a high-priority target in the effort to reduce the global burden of gastric cancer (Sutton et al., 2019, PubMed: 30631105).
Induction of neutralizing antibodies to block bacterial adhesion to gastric epithelial cells
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