Human α2,6-linked sialic acid-terminated glycan receptor (α2,6-SA receptor)

Human α2,6-linked sialic acid-terminated glycan receptors are specific carbohydrate motifs found on the surface of respiratory epithelial cells, where a terminal N-acetylneuraminic acid (sialic acid) is attached to a galactose residue via an α2,6-glycosidic linkage (Shinya et al., Nature 2006). These glycans serve as the primary attachment site for human-adapted influenza A and B viruses, which utilize their surface hemagglutinin (HA) protein to recognize and bind these specific structures to initiate cell entry (Nicholls et al., Lancet 2007). The distribution of these receptors, predominantly in the upper respiratory tract, is a key determinant of the transmissibility and host specificity of human influenza strains compared to avian strains, which prefer α2,3-linkages (Belser et al., J. Virol. 2011). In clinical contexts, these receptors are critical targets for preventing viral infection; for instance, the drug DAS181 (Fludase) is a recombinant sialidase that enzymatically removes these sialic acid residues from the host cell surface, thereby blocking viral docking and entry (Triana-Baltzer et al., PLoS ONE 2009). Other therapeutic approaches include the development of sialylmimetics and hemagglutinin inhibitors like Umifenovir, which disrupt the interaction between the viral HA and the host glycan receptor. Understanding the density and configuration of these receptors is essential for assessing pandemic risk and developing broad-spectrum antiviral strategies (Moss et al., J. Infect. Dis. 2012).

Other names

Neu5Acα2-6Galα2,6-sialylglycanHuman-type influenza receptor6'-sialyllactose receptorAlpha-2,6-linked sialic acid

Enzymatic cleavage of terminal sialic acid residues to prevent viral attachment; competitive inhibition of the viral hemagglutinin-glycan interaction.