Sialyl-glycoconjugate

Sialyl-glycoconjugates are a diverse class of macromolecules, including glycoproteins and glycolipids, characterized by the presence of terminal sialic acid residues. These molecules are essential components of the cell surface glycocalyx and secreted proteins, where they mediate critical biological processes such as cell-cell recognition, molecular trafficking, and immune system regulation (Varki, 2008, Trends Mol Med). In human health, sialyl-glycoconjugates serve as primary attachment points for various pathogens; for example, the influenza virus utilizes its hemagglutinin protein to bind these glycans for host cell entry (Air, 2012, Influenza Other Respir Viruses). Furthermore, aberrant sialylation is a hallmark of cancer progression, where hypersialylation (such as the expression of sialyl-Lewis X) promotes tumor metastasis and immune evasion by interacting with selectins and Siglec receptors (Fuster & Esko, 2005, Nat Rev Cancer). Therapeutic strategies targeting these molecules include the use of recombinant sialidases like DAS181 to remove viral receptors, glycomimetics like uproleselan to block selectin-mediated adhesion, and monoclonal antibodies like dinutuximab that target specific sialylated gangliosides on tumor cells (Büll et al., 2014, Mol Cancer Res).

Other names

Sialylated glycanSialo-glycoconjugateSialic acid-containing glycoconjugateSialyl-glycanSialylated glycoproteinSialylated glycolipid

Enzymatic cleavage of terminal sialic acid residues to prevent viral attachment and entry; competitive inhibition of sialyl-glycan binding to selectins to disrupt leukocyte extravasation; antibody-mediated targeting of specific sialylated gangliosides for tumor cell lysis.