Helicobacter pylori adhesion machinery and epithelial cell surface interaction sites

The Helicobacter pylori (H. pylori) adhesion machinery and epithelial cell surface interaction sites represent a complex molecular interface critical for the bacterium's survival and pathogenesis in the human stomach [1, 8]. This system primarily consists of bacterial outer membrane proteins (OMPs), known as adhesins, which recognize and bind to specific carbohydrate or protein receptors on the gastric epithelium [6, 15]. Key adhesins include the blood group antigen-binding adhesin (BabA), which targets Lewis b (Leb) antigens, and the sialic acid-binding adhesin (SabA), which binds to sialyl-Lewis X (sLeX) antigens upregulated during inflammation [2, 19]. This anchoring mechanism prevents the bacteria from being cleared by gastric peristalsis and mucus turnover, facilitating long-term colonization [5, 16]. Beyond simple attachment, these interactions are essential for the delivery of virulence factors, such as the CagA oncoprotein, into host cells via the Type IV secretion system (T4SS) [14, 15]. Chronic colonization mediated by this machinery leads to persistent inflammation, peptic ulcers, and significantly increases the risk of gastric adenocarcinoma and MALT lymphoma [1, 8]. Therapeutic targeting of these sites, often referred to as anti-adhesion therapy, involves the use of carbohydrate mimetics like 3'-sialyllactose or plant-derived rhamnogalacturonans to competitively inhibit bacterial binding [3, 9, 10]. Such strategies are being explored as alternatives or adjuncts to traditional antibiotics to overcome the challenges of rising antimicrobial resistance [12, 23].

Other names

H. pylori adhesinsGastric colonization factorsH. pylori-host cell interfaceOuter membrane protein (OMP) adhesion system

Competitive inhibition of bacterial adhesins (e.g., BabA, SabA) binding to host cell surface glycans (e.g., Lewis b, sialyl-Lewis X), neutralization of bacterial attachment factors, and disruption of the Type IV secretion system (T4SS) interaction with host integrins to prevent oncoprotein translocation [2, 3, 9, 15].