Sialic acid residue on host cell glycoprotein

Sialic acid residues are a family of nine-carbon acidic monosaccharides commonly found as terminal modifications on the glycan chains of glycoproteins and glycolips at the surfaces of animal and human cells[2][3][5]. These residues confer a negative charge, influence hydration, and are involved in multiple recognition, adhesion, and regulatory processes, including mediating cell-cell communication and masking antigenic determinants[3][4][5]. Sialic acid residues act as crucial ligands for host immune lectins (e.g., selectins, siglecs) and are recognized or exploited by many pathogens—including influenza viruses and some bacteria—to facilitate host cell binding and entry[1][2][3][7]. Overexpression or altered sialylation of surface proteins is frequent in cancers, supporting tumor progression and immune evasion[5][7]. Antiviral drugs, such as neuraminidase inhibitors (zanamivir, oseltamivir, peramivir), selectively interact with viral neuraminidase but use sialic acid as a natural ligand, targeting viral replication by preventing release of new viral particles[3][4][5]. Sialic acid residues are not receptors or classical drug targets themselves but rather functional epitopes present on many host cell surface macromolecules. The phrasing "Sialic acid residues on host cell glycoproteins" is not a single protein or molecular target, but a recurring functional motif that plays key biological roles and serves as a binding site for certain drugs, pathogens, and immune molecules[1][2][3][5]. **Note:** - The stated target is not a classical single-molecule "target" like a receptor or enzyme, but instead refers to a structural motif present on many glycoproteins[4][5][7]. - This motif is exploited as a target in infection, particularly for influenza, and in some therapeutic or diagnostic contexts, but it does not correspond to a specific gene, receptor, or protein product[3][5][7]. - Return `is_incorrect: true` because it is a structural feature rather than a distinct molecular entity.

Other names

Sialic acidSialyl residueSialylated glycoproteinSiaN-acetylneuraminic acid (Neu5Ac)Sialoglycan

Inhibition of sialidase (neuraminidase) to block release of viral particles (influenza antiviral drugs)