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**Helicobacter pylori blood group antigen binding adhesin (BabA)** is a highly conserved outer membrane protein of *H. pylori* classified as an adhesin and virulence factor. BabA enables the bacterium to attach to human gastric epithelial cells by specifically recognizing and binding to blood group antigens (notably the Lewis b antigen) and associated glycans. This adhesion is essential for bacterial colonization, persistence, and the delivery of other virulence factors via the type IV secretion system, resulting in chronic gastritis, peptic ulcer development, and increased risk of gastric cancer. Disruption of BabA function impairs H. pylori’s ability to establish infection. As such, BabA serves as a promising candidate for vaccine development and as a target for adhesion-inhibiting drugs, although as of yet, such interventions remain experimental[1][2][3][4][5][7]. **Note:** - The term “H. pylori adhesion factor” is too generic, as H. pylori expresses multiple adhesins. By prevalence and characterization, BabA is widely cited as the *canonical* adhesion factor. Another notable adhesin is SabA, but BabA is considered the primary and best-studied target for therapeutic intervention in this context[1][4][5]. - If you require structured information on other specific adhesins (SabA, HpaA, AlpA, etc.), please specify.
Facilitates bacterial binding to host gastric mucosa via specific interaction with Lewis b antigens and glycans on epithelial cells; disruption of this interaction impairs colonization and pathogenesis[1][4][5].
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