Helicobacter pylori adhesion to gastric mucosal glycolipids

Helicobacter pylori adhesion to gastric mucosal glycolipids is a fundamental process in the colonization and persistence of H. pylori within the human stomach. This interaction is primarily mediated by bacterial outer membrane proteins, 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. BabA typically binds to Lewis b (Leb) antigens in healthy tissue, while SabA targets sialyl-Lewis X (sLeX) antigens that are upregulated during inflammation. By facilitating stable attachment to the gastric epithelium, this adhesion prevents the bacteria from being cleared by gastric motility and allows for the localized delivery of virulence factors. Consequently, this process is a major driver of chronic gastritis, peptic ulcers, and gastric adenocarcinoma. Therapeutic strategies targeting this interaction, known as anti-adhesion therapies, aim to block these binding sites using glycan mimetics or natural inhibitors like polyphenols and pectins. Such approaches offer a potential alternative or adjunct to traditional antibiotics, particularly in addressing the challenge of multi-drug resistant H. pylori strains.

Other names

Helicobacter pylori adhesin-receptor interactionH. pylori attachment to gastric mucosaBabA-mediated adhesionSabA-mediated adhesionHelicobacter pylori-host glycan interaction

Inhibition of bacterial adhesion to host gastric mucosal cells by blocking adhesin-glycan interactions, competitive binding to bacterial adhesins, and enhancement of the gastric mucosal barrier.