Human alpha-2,6-linked sialic acid receptor (alpha-2,6-SA receptor)

Human alpha-2,6-linked sialic acid receptors are terminal glycan structures found on host glycoproteins and glycolipids, characterized by a sialic acid residue attached to galactose via an alpha-2,6-glycosidic bond (Shinya et al., Nature, 2006). These receptors are predominantly expressed in the human upper respiratory tract, including the trachea and bronchi, and serve as the primary attachment site for human-adapted influenza A and B viruses through the viral hemagglutinin protein (NIH, 2023). Beyond viral entry, these glycans play significant roles in cell-cell recognition, immune system modulation, and tumor biology, where their overexpression by enzymes like ST6Gal-I is often linked to increased metastatic potential and poor prognosis in various cancers (Pietrobono et al., Journal of Experimental & Clinical Cancer Research, 2020). Therapeutic strategies targeting these receptors include the use of recombinant sialidases like DAS181 (Fludase), which enzymatically remove the sialic acid to block viral infection, and neuraminidase inhibitors like Oseltamivir that prevent the virus from detaching from these receptors during the budding process (Moss et al., Journal of Infectious Diseases, 2012). Understanding the distribution and density of these receptors is crucial for assessing viral pandemic potential and developing broad-spectrum antiviral therapies (Long et al., Nature Communications, 2019).

Other names

Neu5Ac alpha-2,6-GalHuman-type influenza receptoralpha-2,6-sialylated glycanSialic acid alpha-2,6-galactoseNeu5Ac alpha-2,6-Gal-beta-1,4-GlcNAc

Enzymatic desialylation of the host cell surface to remove terminal alpha-2,6-linked sialic acid residues, thereby preventing viral attachment and entry (e.g., DAS181), or inhibition of viral neuraminidase to prevent the cleavage of these receptors during viral budding, which traps the virus on the host cell surface (e.g., Oseltamivir).