title: Duodenal intraepithelial lymphocytes of children with cow milk allergy preferentially bind the glycan-binding protein galectin-3.
abstract: A breakdown in intestinal homeostasis results in inflammatory bowel diseases including coeliac disease and allergy. Galectins, evolutionarily conserved beta-galactoside-binding proteins, can modulate immune-epithelial cell interactions by influencing immune cell fate and cytokine secretion. In this study we investigated the glycosylation signature, as well as the regulated expression of galectin-1 and -3 in human duodenal samples of allergic and non-allergic children. Whereas galectin-1 was predominantly localized in the epithelial compartment (epithelial cells and intraepithelial lymphocytes) and the underlying lamina propria (T cells, macrophages and plasma cells), galectin-3 was mainly expressed by crypt epithelial cells and macrophages in the lamina propria. Remarkably, expression of these galectins was not significantly altered in allergic versus non-allergic patients. Investigation of the glycophenotype of the duodenal inflammatory microenvironment revealed substantial alpha2-6-linked sialic acid bound to galactose in lamina propria plasma cells, macrophages and intraepithelial lymphocytes and significant levels of asialo core 1 O-glycans in CD68+ macrophages and enterocytes. Galectin-1 preferentially bound to neutrophils, plasma cells and enterocytes, while galectin-3 binding sites were mainly distributed on macrophages and intraepithelial lymphocytes. Notably, galectin-3, but not galectin-1 binding, was substantially increased in intraepithelial gut lymphocytes of allergic patients compared to non-allergic subjects, suggesting a potential role of galectin-3-glycan interactions in shaping epithelial-immune cell connections during allergic inflammatory processes.
authors.affiliation: Laboratory of Investigations of the Immune System, Department of Biological Sciences, School of Sciences, University of La Plata, Argentina.
authors.forename: N
authors.initials: N
authors.lastname: Mercer
authors.forename: L
authors.initials: L
authors.lastname: Guzman
authors.forename: E
authors.initials: E
authors.lastname: Cueto Rua
authors.forename: R
authors.initials: R
authors.lastname: Drut
authors.forename: H
authors.initials: H
authors.lastname: Ahmed
authors.forename: G R
authors.initials: GR
authors.lastname: Vasta
authors.forename: M A
authors.initials: MA
authors.lastname: Toscano
authors.forename: G A
authors.initials: GA
authors.lastname: Rabinovich
authors.forename: G H
authors.initials: GH
authors.lastname: Docena
mesh_terms: D001665:Binding Sites; D002675:Child, Preschool; D004386:Duodenum / Q000737:chemistry / Q000276:immunology*; D005260:Female; D037483:Galectin 1 / Q000032:analysis / Q000378:metabolism; D037502:Galectin 3 / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D007223:Infant; D008214:Lymphocytes / Q000378:metabolism*; D008297:Male; D016269:Milk Hypersensitivity / Q000209:etiology / Q000276:immunology*; D019887:Peanut Agglutinin / Q000378:metabolism; D037121:Plant Lectins / Q000378:metabolism; D054788:Ribosome Inactivating Proteins / Q000378:metabolism
chemical_list: D037483:Galectin 1; D037502:Galectin 3; C445499:LGALS1 protein, human; D019887:Peanut Agglutinin; D037121:Plant Lectins; C050600:Sambucus nigra lectins; D054788:Ribosome Inactivating Proteins