Helicobacter pylori adhesion system

The Helicobacter pylori adhesion system is a complex network of bacterial outer membrane proteins (adhesins) and their corresponding host receptors on the gastric mucosa, essential for the bacterium's ability to colonize and persist in the human stomach [1.1.2, 1.1.3]. Primary adhesins include the Blood group antigen-binding adhesin (BabA), which targets Lewis b antigens, and the Sialic acid-binding adhesin (SabA), which binds to inflammation-associated sialyl-Lewis X antigens [1.1.2, 1.3.2]. Other critical components include HopQ, which interacts with host Carcinoembryonic Antigen-Related Cell Adhesion Molecules (CEACAMs), and CagL, which binds to host integrins to facilitate the delivery of the CagA virulence factor [1.1.1, 1.3.3]. This adhesion process allows H. pylori to resist mechanical clearance by gastric peristalsis and mucus shedding, while also triggering host signaling pathways that lead to chronic inflammation, peptic ulcers, and gastric adenocarcinoma [1.1.3, 1.3.4]. Therapeutic strategies targeting these adhesion sites, such as glycan mimetics like 3'-sialyllactose, anti-adhesin antibodies, and probiotics, aim to prevent colonization and reduce the pathogenic burden [1.2.1, 1.2.3, 1.3.1]. This system represents a promising therapeutic target, particularly for addressing the challenge of rising antibiotic resistance in H. pylori infections [1.2.2, 1.2.5].

Other names

Helicobacter pylori adhesion sites on gastric mucosa and bacterial surface receptorsH. pylori adhesinsH. pylori-host cell interactionsH. pylori outer membrane proteins (OMPs)H. pylori adhesion molecules

Competitive inhibition of bacterial adhesin binding to host glycan receptors, steric hindrance of adhesin-receptor complexes, and modulation of bacterial outer membrane protein expression [1.2.1, 1.2.2].