Helicobacter pylori adherence mechanisms to gastric epithelium

Helicobacter pylori adherence mechanisms to the gastric epithelium involve a sophisticated array of bacterial outer membrane proteins (adhesins) that interact with specific host glycan receptors to facilitate colonization and persistence [4, 11]. The primary adhesins include the Blood group antigen-binding adhesin (BabA), which binds to Lewis b antigens on healthy mucosa, and the Sialic acid-binding adhesin (SabA), which targets sialyl-Lewis X antigens induced during inflammation [5, 12]. Other critical components include HopQ, which interacts with host CEACAMs, and the adherence-associated lipoproteins AlpA and AlpB [1, 6]. These interactions are vital for the bacterium to resist mechanical clearance and to enable the injection of virulence factors, such as CagA, into host cells via the Type IV secretion system [4, 10]. This process triggers chronic inflammation, leading to gastritis, peptic ulcers, and an increased risk of gastric cancer [8, 15]. Therapeutic strategies targeting these mechanisms, known as anti-adhesion therapies, aim to prevent or disrupt bacterial attachment using glycan mimetics or competitive inhibitors, providing a potential antibiotic-independent treatment for resistant infections [2, 13, 14].

Other names

H. pylori adhesin-receptor interactionsH. pylori colonization factorsH. pylori attachment mechanismsAnti-adhesion therapy for H. pylori

Competitive inhibition of bacterial adhesins (e.g., BabA, SabA, HopQ) binding to host gastric epithelial receptors (e.g., Lewis b, sialyl-Lewis X, CEACAMs).