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Helicobacter pylori adhesins are a specialized group of outer membrane proteins (OMPs) that mediate the critical first step of bacterial attachment to the human gastric mucosa [1, 10]. The most prominent members of this family include the blood group antigen-binding adhesin (BabA), which recognizes Lewis b antigens, and the sialic acid-binding adhesin (SabA), which binds to sialyl-Lewis x antigens [4, 14]. These factors allow the bacterium to anchor itself against the mechanical forces of gastric peristalsis and mucus shedding, facilitating long-term colonization and persistent infection [8, 11]. Beyond simple attachment, these adhesins also play a role in the delivery of virulence factors, such as the CagA oncoprotein, into host epithelial cells, thereby driving the progression of gastritis, peptic ulcers, and gastric cancer [3, 12]. Given their essential role in pathogenesis, H. pylori adhesins are significant therapeutic targets for the development of anti-adhesion drugs, including carbohydrate mimetics and specific antibodies [2, 5]. Additionally, certain probiotics and mucoprotective agents like rebamipide have been shown to interfere with these adhesion mechanisms to reduce bacterial load and mucosal damage [5, 13].
Anti-adhesion agents inhibit the attachment of H. pylori to the gastric mucosa by competitively binding to bacterial adhesins or host glycan receptors, or by downregulating the expression of adhesin genes.
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