Gastric epithelial cell adhesion receptors for Helicobacter pylori

Helicobacter pylori adhesion sites on gastric epithelial cells represent a diverse set of host surface molecules, primarily glycans and glycoproteins, that the bacterium exploits to establish chronic infection [Aspholm et al., 2006, PubMed: 16439610]. The most well-characterized interactions involve the bacterial adhesin BabA binding to the Lewis b (Leb) blood group antigen and SabA binding to sialylated glycans like Sialyl-Lewis x (sLex), which are often upregulated during chronic inflammation [Mahdavi et al., 2002, PubMed: 12130785]. Another critical interaction occurs between the bacterial HopQ protein and host Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs), which is essential for the translocation of the CagA toxin via a Type IV secretion system [Javaheri et al., 2016, PubMed: 27787450]. These interactions allow the bacteria to remain close to the epithelial surface, avoiding clearance by gastric acid and mucus turnover, while triggering intracellular signaling pathways that lead to inflammation and tissue damage [Backert et al., 2016, PubMed: 27083486]. Therapeutic strategies targeting these adhesion sites aim to disrupt the initial stages of infection using non-antibiotic agents such as glycan mimetics, bismuth salts, or specific antibodies [PubMed: 10448316, PubMed: 15810945]. This approach is particularly relevant given the rising rates of antibiotic resistance in H. pylori strains globally.

Other names

H. pylori gastric receptorsLewis b antigen (Leb)Sialyl-Lewis x antigen (sLex)CEACAM receptorsGastric mucosal adhesion sitesBlood group antigen-binding adhesin receptorsSialic acid-binding adhesin receptorsCEACAM1CEACAM5CEACAM6LacDiNAc

Competitive inhibition of bacterial adhesins (e.g., BabA, SabA, HopQ) from binding to their respective host cell surface receptors (e.g., Lewis b, Sialyl-Lewis x, CEACAMs), thereby preventing colonization and subsequent inflammatory signaling.