Cell-surface complex-type N-glycans (Complex N-glycans)

Cell-surface complex-type N-glycans are a major class of oligosaccharides attached to the amide nitrogen of asparagine residues within the consensus sequence Asn-X-Ser/Thr of proteins (Moremen et al., 2012). These structures are characterized by a conserved trimannosyl core (Man3GlcNAc2) that is further elongated with various monosaccharides like N-acetylglucosamine, galactose, fucose, and terminal sialic acids, forming multiple antennae (Varki et al., 2017). They play indispensable roles in biological processes including cell-cell recognition, protein folding quality control in the endoplasmic reticulum, and the modulation of immune responses (Stanley et al., 2022). In pathological contexts, aberrant N-glycosylation—such as increased branching or hypersialylation—is a hallmark of cancer progression, facilitating tumor cell migration and evasion of the immune system (Pinho & Reis, 2015). Furthermore, many pathogens, including influenza and coronaviruses, utilize these cell-surface glycans as receptors or attachment factors for host cell entry (Watanabe et al., 2020). Therapeutic interventions targeting these glycans include neuraminidase inhibitors that prevent viral release, selectin antagonists that block glycan-mediated leukocyte trafficking, and lectin-based agents designed to neutralize glycan-shielded viruses (Ohtsubo & Marth, 2006).

Other names

Complex-type N-linked oligosaccharidesN-linked glycansAsparagine-linked glycansComplex N-glycan antennae

Inhibition of viral neuraminidase to prevent cleavage of terminal sialic acids from N-glycans (Gubareva et al., 2000); competitive inhibition of selectin-glycan binding to reduce inflammation and cell adhesion (DeAngelo et al., 2022; Ataga et al., 2017); and direct binding to glycan motifs to neutralize pathogens (O'Keefe et al., 2009).