Host cell surface sialic acid-containing glycoprotein and glycolipid receptors (Sia-receptors)

Host cell surface sialic acid-containing glycoprotein and glycolipid receptors are terminal carbohydrate structures found on the outermost ends of glycan chains on the plasma membrane (Varki, 2008, Trends in Molecular Medicine). These molecules, primarily N-acetylneuraminic acid (Neu5Ac), play a critical role in mediating cell-cell interactions, signaling, and immune system regulation by serving as ligands for Siglecs (sialic acid-binding immunoglobulin-type lectins) (Schauer, 2009, Current Opinion in Structural Biology). In the context of infectious diseases, these receptors are exploited by a wide range of pathogens, including influenza viruses, paramyxoviruses, and certain bacteria, as primary attachment sites for host cell entry (Matrosovich et al., 2013, Topics in Current Chemistry). For instance, the influenza virus hemagglutinin protein specifically recognizes and binds to these sialic acids to initiate infection, with human-adapted viruses preferring alpha-2,6 linkages and avian viruses preferring alpha-2,3 linkages (Triana-Falo et al., 2022, Frontiers in Molecular Biosciences). Therapeutic strategies targeting these receptors include the use of sialidases like DAS181 to enzymatically remove the sialic acid residues from the respiratory epithelium, thereby blocking viral attachment, or the development of neuraminidase inhibitors to prevent the release of viral progeny from these receptors (Malakhov et al., 2006, Antimicrobial Agents and Chemotherapy).

Other names

Sialylated glycoconjugatesSialic acid-containing receptorsNeu5Ac receptorsSialyl-glycansSialoside receptorsSialic acid-containing glycoproteins and glycolipids

Enzymatic cleavage of terminal sialic acid residues from the host cell surface to prevent viral attachment and entry (e.g., DAS181); inhibition of viral neuraminidase to prevent the cleavage of these receptors, thereby trapping progeny virions on the host cell surface (e.g., Oseltamivir).