Helicobacter pylori adhesin

**Helicobacter pylori adhesins** are a group of bacterial outer membrane proteins essential for the initial and sustained attachment of H. pylori to gastric epithelial cells, enabling persistent colonization of the host stomach and promoting pathogenesis. Major characterized adhesins include BabA (which binds to Lewis b blood group antigens), SabA (binds sialyl-Lewis x antigens), AlpA/B, HopQ, OipA, HopZ, and HpaA. Each adhesin typically has specific host glycan or protein binding activity, facilitating firm bacterial attachment and contributing to immune evasion and chronic infection[4][6][7]. Pathogenesis roles of these adhesins extend to gastric inflammation, peptic ulcer disease, and gastric cancer. Vaccines and drugs are in development targeting these molecules or their glycosylation, though no adhesin-targeting drugs are currently in clinical use[1][5]. **Note:** - "Helicobacter pylori adhesins" as a plural/generic term is *not* a single molecular entity, but refers to several related proteins (BabA, SabA, AlpA, AlpB, HopQ, OipA, HopZ, HpaA, etc.), each with distinct structure and binding specificity[4][6][7]. - The *enzymes* responsible for glycosylating these adhesins (e.g., WecA, Wzk, WaaL) are also potential drug targets for anti-adhesion therapy, perhaps more so than the adhesins themselves[1]. - For best structured information, each adhesin (e.g., BabA, SabA, HpaA) should have a separate entry; grouping all "Helicobacter pylori adhesins" together is nonstandard and less precise—hence, is_incorrect: true.

Other names

BabA (Blood group antigen-binding adhesin)SabA (Sialic acid-binding adhesin)AlpAAlpBHopQOipAHopZHpaA

Inhibiting adhesion prevents colonization and persistence of H. pylori in the gastric mucosa (e.g., vaccine-induced neutralizing antibodies, inhibitors of glycosylation pathways essential for adhesin function)