Host cell sialic acid residues (Sia)

Host cell sialic acid residues are nine-carbon acidic monosaccharides located at the terminal positions of glycan chains on glycoproteins and glycolipids (Varki et al., 2017). These residues serve as essential attachment points for a wide variety of pathogens, including influenza viruses, parainfluenza viruses, and certain bacteria, which utilize surface proteins like hemagglutinin to recognize specific sialic acid linkages (Schauer, 2009). Beyond their role in infection, sialic acids are vital for physiological processes such as cell-cell communication, immune response modulation through Siglec receptors, and maintaining the structural integrity of the glycocalyx (Triana-Alba et al., 2021). In pathological states like cancer, increased sialylation (hypersialylation) contributes to tumor metastasis and helps cancer cells evade the immune system by masking antigenic sites (Varki, 2008). Therapeutic interventions targeting these residues often involve sialidases, such as DAS181, which enzymatically remove the sialic acids to prevent viral entry, or neuraminidase inhibitors that block the release of progeny viruses from the host cell surface (Malakhov et al., 2006).

Other names

N-acetylneuraminic acidNeu5AcSialic acidsSialyl glycoconjugatesTerminal sialic acidGlycan receptors

Enzymatic cleavage of terminal sialic acid residues from the host cell surface to prevent viral entry, or inhibition of viral neuraminidase to prevent the cleavage of these residues during viral egress.