Galectin binding to cells and glycoproteins with genetically modified glycosylation reveals galectin-glycan specificities in a natural context.

ABSTRACT: Galectins compose a protein family defined by a conserved sequence motif conferring affinity for β-galactose-containing glycans. Moreover, galectins gain higher affinity and fine-tune specificity by glycan interactions at sites adjacent to their β-galactoside-binding site, as revealed by extensive testing against panels of purified glycans. However, in cells, galectins bind glycans on glycoproteins and glycolipids in the context of other cellular components, such as at the cell surface. Because of difficulties in characterizing natural cellular environments, we currently lack a detailed understanding of galectin-binding specificities in the cellular context. To address this challenge, we used a panel of genetically stable glycosylation mutated CHO cells that express defined glycans to eval

SUBMITTER: Nielsen MI 

PROVIDER: S-EPMC6311502 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature