Terminal β-galactose moieties on cell-surface glycoconjugates (Terminal β-Gal)

Terminal β-galactose moieties are carbohydrate structures located at the non-reducing ends of glycans on cell-surface glycoproteins and glycolipids (Cummings et al., 2017). These moieties serve as essential ligands for the galectin family of proteins, which are soluble lectins that regulate cell-cell adhesion, immune responses, and apoptosis (Johannes et al., 2018). In pathological conditions like cancer, the presentation of terminal galactose is often altered—either masked by hypersialylation or overexpressed—facilitating tumor progression, metastasis, and immune evasion by interacting with Galectin-3 (Liu et al., 2014). Furthermore, these residues are specifically recognized by the asialoglycoprotein receptor (ASGPR) in the liver, making them a primary target for liver-specific drug delivery systems (Stockert, 1995). Therapeutic strategies involving these moieties include the use of galectin inhibitors, such as Belapectin, which mimic these structures to block aberrant signaling, and the development of galactose-conjugated therapeutics for targeted uptake (Chahal et al., 2015). Additionally, certain bacterial and viral pathogens utilize terminal β-galactose as an attachment point to infect host cells (Varki et al., 2015).

Other names

Terminal β-D-galactosyl residuesβ-galactoside moietiesNon-reducing terminal galactoseGalactose-terminated glycansDesialylated glycans

Competitive inhibition of galectin-glycan interactions or receptor-mediated endocytosis via the asialoglycoprotein receptor (ASGPR)