Terminal galactose-containing glycan

Terminal galactose-containing glycans are carbohydrate structures located at the non-reducing ends of glycoproteins and glycolipids on the surface of host cells. These glycans are often exposed following the enzymatic removal of terminal sialic acids by neuraminidases, a process that occurs during cellular aging, inflammation, and viral infection (Varki, A., 2008, Trends in Molecular Medicine). They serve as the primary ligands for galectins, a family of endogenous lectins that play pivotal roles in immune response modulation, cell adhesion, and apoptosis (Cummings, R.D., et al., 2017, Essentials of Glycobiology). In infectious diseases, terminal galactose residues act as critical attachment receptors for various pathogens, including specific strains of Rotavirus and Streptococcus pneumoniae (Lopez, S., & Arias, C.F., 2004, Virus Research). In oncology, the aberrant expression of these glycans, such as the Thomsen-Friedenreich antigen, is associated with tumor progression and metastasis (Yu, L.G., 2007, Glycoconjugate Journal). Therapeutic strategies targeting this axis primarily involve galectin inhibitors and glycomimetics designed to block these carbohydrate-protein interactions in conditions like fibrosis, cancer, and chronic inflammation.

Other names

Galactose-terminated glycansTerminal Gal residuesDesialylated glycansGalactose-exposed oligosaccharidesBeta-galactoside-containing glycansTerminal galactose-containing glycans on host cell surfacesThomsen-Friedenreich antigen

Competitive inhibition of the interaction between terminal galactose residues and galectins or pathogen-associated lectins