Host cell surface sialylated glycoconjugates

Host cell surface sialylated glycoconjugates are a diverse group of glycoproteins and glycolipids that terminate in sialic acid residues, most commonly N-acetylneuraminic acid (Neu5Ac) (Varki, 2008, Trends in Molecular Medicine). These molecules are ubiquitous on vertebrate cell surfaces and are essential for mediating cell-cell recognition, stabilizing protein structures, and regulating immune responses through interactions with Siglecs (sialic acid-binding immunoglobulin-type lectins) (Crocker et al., 2007, Nature Reviews Immunology). In infectious diseases, these sialylated substrates act as critical receptors for various pathogens; for instance, influenza viruses utilize hemagglutinin to bind specific alpha-2,3 or alpha-2,6 sialic acid linkages on host cells to initiate infection (Cohen et al., 2013, Glycobiology). Therapeutic interventions include the use of sialidases like DAS181 (Fludase), which enzymatically cleave these terminal residues to prevent viral entry, and neuraminidase inhibitors that prevent the release of new virions by blocking the cleavage of these substrates (Triana-Baltzer et al., 2010, Antiviral Research). Furthermore, aberrant sialylation is a known hallmark of cancer, where hypersialylation facilitates immune evasion and promotes metastasis, making these glycans significant targets for diagnostic and therapeutic development in oncology (Pinho and Reis, 2015, Nature Reviews Cancer).

Other names

Host cell surface sialylated substratesSialic acid-containing glycansSialylated glycoconjugatesCell surface sialosidesNeu5Ac-containing substrates

Enzymatic removal of terminal sialic acid residues to block pathogen entry; inhibition of viral neuraminidase to prevent cleavage of these substrates during viral egress; or inhibition of sialyltransferases to reduce the density of these substrates on the cell surface.