Cell surface sialylated glycoconjugates (Sia-glycoconjugates)

Cell surface sialylated glycoconjugates are terminal sugar residues, primarily N-acetylneuraminic acid, attached to glycoproteins and glycolipids on the plasma membrane of host cells and the envelopes of certain viruses. These molecules function as critical biological signatures involved in cell-cell recognition, immune system modulation, and as receptors for pathogen attachment (Varki, A. 2008, Trends in Molecular Medicine). In viral infections such as influenza, the viral hemagglutinin protein binds to these sialic acids to initiate entry into the host cell (Byrd-Leotis, L., et al. 2017, Genes). Conversely, the viral neuraminidase enzyme must cleave these sialic acid residues to allow newly formed virions to detach from the host cell and prevent self-aggregation (Von Itzstein, M. 2007, Nature Reviews Drug Discovery). Therapeutic strategies targeting this system include neuraminidase inhibitors like oseltamivir, which prevent viral release, and host-directed sialidases like DAS181, which enzymatically remove the receptors from the respiratory epithelium to block infection (Moss, R. B., et al. 2012, Antiviral Research). Beyond infectious disease, aberrant sialylation is a hallmark of cancer progression, where it contributes to immune evasion and metastasis.

Other names

Sialic acid-containing glycansSialylated glycoproteinsSialylated glycolipidsSialic acid receptorsN-acetylneuraminic acid (Neu5Ac) conjugates

Neuraminidase inhibitors prevent the cleavage of sialic acid residues to block viral release; sialidases (like DAS181) enzymatically remove terminal sialic acids from host cells to prevent viral attachment.