N-linked sialic acid-containing glycans (N-linked sialoglycans)

N-linked sialic acid-containing glycans are complex oligosaccharides attached to the asparagine residues of proteins, characterized by terminal sialic acid (neuraminic acid) residues. These structures are essential components of the cellular glycocalyx and play pivotal roles in biological processes such as cell-cell adhesion, protein stability, and the regulation of the immune system through interactions with Siglec (Sialic acid-binding immunoglobulin-type lectin) receptors (Varki, 2017, Essentials of Glycobiology). In the context of infectious diseases, these glycans serve as the primary attachment points for various pathogens, most notably the influenza virus, which utilizes its hemagglutinin protein to bind terminal sialic acids for cell entry (Gubareva et al., 2000, Lancet). In oncology, the upregulation of sialylated N-glycans, known as hypersialylation, is a hallmark of malignant transformation that facilitates tumor metastasis and provides a mechanism for immune evasion by dampening the activity of natural killer cells and T cells (Pearce & Läubli, 2016, Glycobiology). Therapeutic interventions targeting these glycans include neuraminidase inhibitors that prevent viral release by blocking the cleavage of these glycans, and emerging glyco-immune checkpoint inhibitors designed to strip sialic acids from tumor surfaces or block their interaction with inhibitory immune receptors (Büll et al., 2016, Angewandte Chemie).

Other names

Sialylated N-glycansN-linked neuraminic acid-containing glycansSialic acid-capped N-glycansN-glycan sialosides

Inhibition of viral neuraminidase to prevent the cleavage of terminal sialic acid residues from host cell glycans; enzymatic degradation of sialic acid receptors on respiratory epithelium to prevent viral attachment; blockade of the Siglec-sialic acid signaling axis to enhance anti-tumor immunity.