Sialic acid-containing N-linked glycans (Sialylated N-glycans) (Sialylated N-glycans)

Sialic acid-containing N-linked glycans are complex carbohydrate structures covalently attached to the nitrogen atom of asparagine side chains in proteins. These glycans typically terminate with sialic acid residues, which are nine-carbon acidic sugars that provide a negative charge and serve as critical recognition elements at the cell surface (Varki A., 2008, PMID: 18606570). Biologically, they are essential for protein stability, cell-cell adhesion, and the regulation of the immune system through interactions with receptors such as Siglecs (sialic acid-binding immunoglobulin-type lectins) (Pearce OM, et al., 2016, PMID: 26762565). In pathological states, such as cancer, the overexpression of these glycans (hypersialylation) facilitates immune evasion by dampening the activity of natural killer cells and macrophages (Büll C, et al., 2014, PMID: 24862100). Furthermore, they serve as the primary attachment receptors for various pathogens, including influenza viruses and certain bacteria, making them a focal point for antiviral drug development. Therapeutic interventions often involve neuraminidase inhibitors that prevent the cleavage of these glycans to stop viral spread, or emerging glyco-immune checkpoint inhibitors designed to disrupt the sialic acid-Siglec signaling axis in the tumor microenvironment. These glycans are also involved in inflammatory processes by mediating leukocyte rolling via selectin binding. Their structural diversity and ubiquity make them challenging yet high-value targets for precision medicine.

Other names

Sialyl-N-glycansN-linked sialylglycansNeuraminic acid-containing N-glycansSialylated N-linked oligosaccharides

Inhibition of viral neuraminidase to prevent glycan cleavage and viral release; enzymatic desialylation of tumor cell surfaces to enhance immune response; blockade of glycan-receptor interactions.