Abstract
The carbohydrates of gastric mucins and other sugar structures are involved in interactions with Helicobacter pylori (H. pylori) adhesins. The binding of bacteria to mucins can protect the epithelium from direct contact with the pathogen and from developing infection because of a specific barrier created by the mucus. The pathogen also interacts with other carbohydrate structures of the epithelium. Direct contact between the bacteria and the epithelial cells facilitates infection development. The aim of this study was to assess the influence of Maackia amurensis (MAA), Lotus tetragonolobus (LTA), Ulex europaeus (UEA), and Arachis hypogaea (PNA) lectins on the binding of gastric carbohydrates with H. pylori adhesins. Three patients' gastric juices and 12 H. pylori strains were included in the study. An ELISA test was used to assess the presence of MUC1 and MUC5AC mucins and the sugar structures recognized by all examined lectins. The binding of the bacterium to the sugar structures was analyzed by the ELISA method with and without the gastric juices pretreated with lectins. In the majority of the samples examined, MAA, LTA, UEA, and PNA lectins enhanced the binding of H. pylori to specific carbohydrate structures of gastric mucins. Substances which influence the binding of the pathogen with specific carbohydrate receptors on gastric epithelial cells can favor inflammation development. However, if H. pylori binds with mucins, the bacterium can have difficulty reaching the epithelium and progressing with infection.
Highlights
Helicobacter pylori, a Gram-negative bacterium, colonizes the human stomach of more than 50% of the world’s population
The binding of bacteria to mucins can protect the epithelium from direct contact with the pathogen and from developing infection because of a specific barrier created by the mucus
In the majority of the samples examined, Maackia amurensis (MAA), Lotus tetragonolobus (LTA), Ulex europaeus (UEA), and PNA lectins enhanced the binding of H. pylori to specific carbohydrate structures of gastric mucins
Summary
Helicobacter pylori, a Gram-negative bacterium, colonizes the human stomach of more than 50% of the world’s population. The mucus layer is mainly comprised of 2 secreted mucins: MUC5AC and MUC6, the first produced by the surface epithelium and the second one by the glands.[3,4] There is MUC1, the most highly expressed membrane-tethered mucin that is normally found on the apical surface of polarized epithelia, and is a major component of glycocalyx It can initiate a signaling pathway in response to bacterial invasion and is thought to play an important role in cell–cell and cell–extracellular matrix interactions.[5,6,7] Mucins are heavily glycosylated glycoproteins with a large number of O-linked oligosaccharides with many sugar antigens which can be recognized by H. pylori adhesins.[8,9] It has been suggested that the bacterium can bind to both MUC1 and MUC5AC mucins via fucosylated and sialylated glycans.[10,11,12] Some authors suggest that a release of MUC1 following the binding to H. pylori can limit the adhesion of the bacterium to the cell surface. Direct contact between the bacteria and the epithelial cells facilitates infection development
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