Muc5ac gastric mucin glycosylation is shaped by FUT2 activity and functionally impacts Helicobacter pylori binding

• Published in: Scientific reports Vol. 6; no. 1; p. 25575
• Main Authors: Magalhães, Ana, Rossez, Yannick, Robbe-Masselot, Catherine, Maes, Emmanuel, Gomes, Joana, Shevtsova, Anna, Bugaytsova, Jeanna, Borén, Thomas, Reis, Celso A.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10.05.2016; Nature Publishing Group
• Subjects: 101/58; 14/63; 140/131; 631/45/221; 631/92/72/1202; 64/110; 82/83; Adhesins, Bacterial - metabolism; Animal models; Animals; Bacterial Adhesion; Bacteriology; Biochemistry, Molecular Biology; Epithelial cells; Epithelium; Fucosyltransferases - genetics; Fucosyltransferases - metabolism; Galactoside 2-alpha-L-fucosyltransferase; Gastric Mucins - metabolism; Gastric mucosa; Gastric Mucosa - metabolism; Gastrointestinal tract; Glycosylation; Helicobacter Infections - metabolism; Helicobacter Infections - microbiology; Helicobacter pylori; Helicobacter pylori - metabolism; Helicobacter pylori - physiology; Humanities and Social Sciences; Humans; Lewis Blood Group Antigens - metabolism; Life Sciences; Mice, Inbred C57BL; Mice, Knockout; Microbiology and Parasitology; Mimicry; Mucin; Mucin 5AC - metabolism; Mucous membrane; Mucus; Mucus - metabolism; multidisciplinary; Pathogenicity; Pathogens; Polysaccharides; Polysaccharides - metabolism; Protein Binding; Science; Science (multidisciplinary); Stomach

The gastrointestinal tract is lined by a thick and complex layer of mucus that protects the mucosal epithelium from biochemical and mechanical aggressions. This mucus barrier confers protection against pathogens but also serves as a binding site that supports a sheltered niche of microbial adherence...