Helicobacter pylori glycosidase

Helicobacter pylori glycosidase refers to a group of enzymes produced by the bacterium Helicobacter pylori that catalyze the hydrolysis of glycosidic bonds in complex carbohydrates (Source: PubMed, PMID: 15657238). These enzymes, including alpha-L-fucosidases and peptidoglycan hydrolases, are essential for the bacterium's ability to colonize the human gastric mucosa and maintain cell wall integrity (Source: UniProt, P0C680). By cleaving fucose from host Lewis antigens, the bacterium can utilize host sugars as a nutrient source and facilitate adhesion to the stomach lining (Source: Journal of Biological Chemistry, doi:10.1074/jbc.M411143200). In addition, glycosidases involved in peptidoglycan turnover are critical for bacterial growth and division, making them attractive targets for novel antimicrobial therapy (Source: Microbiology, doi:10.1099/mic.0.2006/001859-0). Targeting these enzymes with specific inhibitors, such as iminosugars like deoxyfuconojirimycin, has shown potential in reducing bacterial fitness and virulence in preclinical studies (Source: Bioorganic & Medicinal Chemistry, doi:10.1016/j.bmc.2010.06.098). As antibiotic resistance in H. pylori becomes a global health concern, these glycosidases represent a promising avenue for developing non-traditional treatments that disrupt the pathogen's metabolic and structural stability (Source: World Journal of Gastroenterology, doi:10.3748/wjg.v20.i30.10212).

Other names

Helicobacter pylori glycoside hydrolaseH. pylori carbohydrate-active enzymeHpGHPeptidoglycan glycosidaseAlpha-L-fucosidase (Afc1)

Competitive inhibition of bacterial glycoside hydrolases, preventing the cleavage of host-derived glycans and disrupting bacterial cell wall remodeling.