Human respiratory epithelial cell sialic acid receptors (SA receptors) (SA receptors)

Human respiratory epithelial cell sialic acid receptors are terminal carbohydrate structures, primarily N-acetylneuraminic acid (Neu5Ac), found on the surface of the respiratory tract (Shinya et al., 2006, Nature). These receptors are categorized by their glycosidic linkages, specifically α2,3 and α2,6 linkages, which determine the tissue tropism of various respiratory pathogens (Nicholls et al., 2007, Am J Respir Cell Mol Biol). In humans, α2,6-linked sialic acids are prevalent in the upper respiratory tract and are the primary attachment site for human influenza viruses, whereas α2,3-linked sialic acids are more common in the lower respiratory tract and are preferred by avian influenza strains (Shinya et al., 2006, Nature). These receptors play a critical role in the initial stages of viral infection by mediating the binding of viral hemagglutinin proteins to the host cell (Triana-Falo et al., 2019, ACS Chem Biol). Therapeutic strategies targeting these receptors include the use of sialidases, such as DAS181 (Fludase), which enzymatically remove the sialic acid residues to prevent viral attachment and entry (Belser et al., 2007, J Virol). Beyond viral entry, these receptors are involved in cell-cell interactions and the regulation of the immune response within the respiratory environment (Varki, 2008, Glycobiology). The density and distribution of these receptors can vary based on age and underlying health conditions, influencing susceptibility to different viral strains (Walther et al., 2013, PLoS Pathogens). Monitoring the expression of these receptors is often performed using lectin-based assays to assess viral risk and therapeutic efficacy (Matrosovich et al., 2004, PNAS).

Other names

α2,6-linked sialic acidsα2,3-linked sialic acidsN-acetylneuraminic acid receptorsNeu5Ac receptorsInfluenza virus receptorsSialyl-glycoconjugates

Enzymatic cleavage of terminal sialic acid residues from the host cell surface to prevent viral hemagglutinin binding and subsequent entry.