Blood group antigen-binding adhesin (BabA) (BabA)

Blood group antigen-binding adhesin (BabA) is a major outer membrane protein of the bacterium Helicobacter pylori that mediates the attachment of the pathogen to the human gastric mucosa [1, 3, 5]. It specifically recognizes and binds to the Lewis b (Leb) blood group antigens and related fucosylated glycans on the surface of gastric epithelial cells [1, 4, 9]. This adhesion is a critical first step for the colonization and long-term persistence of H. pylori in the stomach, allowing the bacteria to resist mechanical clearance by mucus shedding [5, 10]. Furthermore, BabA-mediated binding facilitates the delivery of bacterial virulence factors, such as the CagA oncoprotein, into host cells via the type IV secretion system, thereby promoting chronic inflammation and tissue damage [8, 11]. Strains expressing BabA are strongly associated with an increased risk of developing severe clinical outcomes, including peptic ulcers, atrophic gastritis, and gastric adenocarcinoma [4, 6, 9]. Consequently, BabA is considered a promising therapeutic target for the development of vaccines and anti-adhesion drugs designed to prevent or treat H. pylori infections [1, 2, 5]. Current research focuses on using BabA-based vaccines or small-molecule inhibitors to disrupt the interaction between the adhesin and host receptors, potentially offering a strategy to combat antibiotic-resistant strains [1, 2].

Other names

BabABabA2Blood group antigen-binding adhesin ALeb-binding adhesinBlood group antigen-binding adhesion

Inhibition of bacterial adhesion to the gastric mucosa by blocking the interaction between BabA and host Lewis b (Leb) antigens.