Human α2,6-linked sialic acid receptor (α2,6-Sia) (α2,6-Sia)

Human α2,6-linked sialic acid receptors are terminal glycan structures found on the surface of epithelial cells, particularly in the human upper respiratory tract. These receptors consist of N-acetylneuraminic acid (Neu5Ac) attached to a galactose residue via an α2,6-glycosidic bond, a linkage synthesized by the enzyme beta-galactoside alpha-2,6-sialyltransferase 1 (ST6Gal-I) (Shinya, K., et al. Nature, 2006). They serve as the primary attachment point for human-adapted influenza viruses, such as H1N1 and H3N2, which utilize their hemagglutinin protein to recognize and bind these specific configurations (Varki, A. Nature, 2007). Beyond viral entry, these receptors play roles in cell-cell recognition and the modulation of immune responses through interactions with Siglecs (sialic acid-binding immunoglobulin-type lectins) (Nicholls, J. M., et al. The Lancet, 2007). In oncology, altered expression of α2,6-linked sialic acids is often associated with tumor progression, immune evasion, and metastasis (Belser, J. A., et al. Journal of Virology, 2004). Therapeutic strategies include the use of sialidases like DAS181 to enzymatically remove these receptors or decoy molecules to block viral binding (Moss, R. B., et al. Journal of Infectious Diseases, 2012).

Other names

Neu5Acα2-6Galα2,6-SiaCD756'-SialyllactoseSiaα2-6Gal

Enzymatic removal of terminal α2,6-linked sialic acid residues from the host cell surface to prevent viral attachment and entry (Moss, R. B., et al. Journal of Infectious Diseases, 2012).