Sialic acid–containing glycan structure

Sialic acid–containing glycan structures are complex carbohydrate motifs found at the termini of glycoproteins and glycolipids on the surface of virtually all vertebrate cells[1][3][4]. These glycans play crucial roles in mediating cell–cell and cell–matrix interactions, regulating immune recognition (notably through their interaction with lectins such as selectins and Siglecs), and determining the biophysical properties and hydration of the cell surface[1][2][4][5]. They are also key attachment factors for many pathogens, including influenza viruses (via hemagglutinin), certain bacteria, and parasites, which recognize or exploit sialylated glycan structures for entry and immune evasion[2][6][7]. In cancer, increased sialylation is associated with enhanced metastasis and resistance to immune clearance[1][4]. Sialic acid–containing glycans are not a single molecule or receptor but rather a diverse family of terminal structures with broad biological significance and important roles as therapeutic targets, biomarker candidates, and mediators of both normal physiology and disease[1][3][4][5][6][7].

Other names

sialylated glycansialoglycansialylated glycoproteinsialylated glycolipidterminal sialic acid–containing glycansialylated structure

Blocking viral or bacterial attachment by inhibiting recognition of sialylated glycans (e.g., neuraminidase inhibitors prevent virus release and entry by targeting sialic acid cleavage/recognition) Modifying immune recognition by masking/unmasking cell surface receptors (e.g., inhibition of sialylation or use of recombinant sialidase to expose hidden antigens) Disruption of cell adhesion and metastasis by altering sialylation patterns