Helicobacter pylori surface adhesin

Helicobacter pylori surface adhesins are a group of outer membrane proteins that mediate the attachment of the bacterium to the gastric mucosal epithelium, initiating colonization and infection. Key members include BabA (binding to Lewis b blood group antigens), SabA (binding sialyl-Lewis antigens), and HpaA. Adhesin-receptor interactions are essential for persistent infection, immune evasion, and delivery of virulence factors, strongly contributing to diseases like gastritis, peptic ulcer, and gastric cancer[1][2][3][4][5][6]. As a drug target, "surface adhesins" is not a singular molecular entity but a functionally and genetically diverse family, so precise targeting requires focus on specific adhesin proteins and their distinct binding interactions. Key considerations: - The entry "Helicobacter pylori surface adhesins" is not a single protein/receptor but a plural group of several distinct, well-characterized bacterial proteins. - Each adhesin (e.g., BabA, SabA, etc.) has different binding targets, structures, and roles. - This category is considered a valid therapeutic target class, notably for vaccine/antibody therapies, though there are currently no approved drugs that target these molecules directly[3][7]. - For structured data, individual adhesins (BabA, SabA, etc.) should be considered canonical targets if specificity is required.

Other names

BabABlood group antigen-binding adhesinSabASialic acid-binding adhesinHpaAAlpAAlpBHopZLabA

Inhibition of adhesion (theoretical for vaccines/therapeutic antibodies), Disruption of protein-carbohydrate interaction, Immune modulation