Host cell sialic acid receptor (SA receptor)

Host cell sialic acid receptors are terminal carbohydrate residues, specifically N-acetylneuraminic acid (Neu5Ac), located on the glycans of glycoproteins and glycolipids on the surface of host cells (Varki, 2008). These receptors serve as the critical attachment point for the Influenza B virus hemagglutinin (HA) protein, which facilitates viral entry into the respiratory epithelium (Ni et al., 2013). Influenza B virus HA exhibits a binding preference for alpha-2,6-linked sialic acids, which are the predominant linkage type in the human upper respiratory tract, although it can also bind to alpha-2,3-linked sialic acids found in the lower respiratory tract (Velkov et al., 2013). The interaction between HA and these receptors triggers receptor-mediated endocytosis, a vital step in the viral life cycle. Therapeutic interventions targeting this interaction include the development of sialidases like DAS181 (Fludase), which cleave the sialic acid residues from the host cell surface to prevent viral docking (Belser et al., 2007). Because sialic acids are involved in numerous physiological processes, including cell signaling and immune regulation, therapeutic targeting must balance antiviral efficacy with potential impacts on normal cellular functions.

Other names

N-acetylneuraminic acid receptorNeu5Ac receptorInfluenza B virus receptorAlpha-2,6-sialylglycanAlpha-2,3-sialylglycanHost cell sialic acid receptors recognized by Influenza B virus hemagglutinin

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