Helicobacter pylori adhesion to gastric mucosal glycolipid receptors

Helicobacter pylori adhesion to gastric mucosal glycolipid receptors is a fundamental mechanism for the colonization and chronic infection of the human stomach (Saitoh et al., 1991). This interaction is primarily mediated by bacterial surface adhesins, such as the Blood group antigen-binding adhesin (BabA) and the Sialic acid-binding adhesin (SabA), which recognize specific carbohydrate motifs on host glycolipids and glycoproteins (Ilver et al., 1998; Mahdavi et al., 2002). BabA targets the Lewis b (Leb) antigen, while SabA binds to sialyl-Lewis X (sLeX), motifs that are often upregulated during inflammation (Aspholm-Hurtig et al., 2004). Additionally, H. pylori binds to other glycolipids such as sulfatide and GM3, which may facilitate initial attachment (Saitoh et al., 1991). \n\nBy anchoring to the gastric mucosa, H. pylori avoids elimination by gastric peristalsis and mucus turnover, allowing for the localized delivery of toxins like CagA and VacA that drive gastritis, peptic ulcers, and gastric adenocarcinoma (Backert et al., 2016). Therapeutic targeting of this adhesion process, known as anti-adhesive therapy, aims to prevent or disrupt bacterial attachment using decoy receptors, carbohydrate mimetics, or natural products like bismuth subsalicylate and cranberry proanthocyanidins (Signorello et al., 2021). This approach offers a potential alternative or adjunct to traditional antibiotic regimens, particularly in the face of rising multi-drug resistance in H. pylori strains (Oleastro & Ménard, 2013).

Other names

H. pylori adhesionHelicobacter pylori-host cell interactionAnti-adhesive therapy targetBabA-Lewis b bindingSabA-sialyl-Lewis X bindingBacterial attachment to gastric glycolipids

Competitive inhibition of bacterial adhesins (e.g., BabA, SabA) from binding to host gastric mucosal glycolipid receptors (e.g., Lewis b, sialyl-Lewis X), thereby preventing bacterial colonization and persistence.