Sialic acid-containing glycoprotein and glycolipid receptors

Sialic acid-containing glycoproteins and glycolipids are ubiquitous components of the mammalian glycocalyx, where they serve as terminal sugars on complex glycan chains (Varki A., 2008, Trends in Molecular Medicine) [1]. These molecules function as critical recognition sites for cell-cell interactions, signal transduction, and the regulation of the innate immune response (Schauer R., 2009, Current Opinion in Structural Biology) [2]. They are most notably recognized as the primary attachment receptors for various human pathogens, including influenza viruses, which utilize hemagglutinin to bind specific sialic acid linkages to initiate infection (Wasik B.R., et al., 2016, Current Opinion in Virology) [3]. In oncology, the over-expression of these sialylated structures, known as hypersialylation, is associated with tumor progression, metastasis, and the evasion of immune surveillance (Bull C., et al., 2017, Methods in Molecular Biology) [4]. Therapeutic interventions often involve neuraminidase inhibitors, such as Oseltamivir, which prevent the cleavage of these receptors by viral enzymes, thereby halting the release of new viral particles (Pearce M.C., et al., 2014, Microbiology Spectrum) [5]. Emerging strategies also include the use of sialyltransferase inhibitors and sialidase-conjugated antibodies to modulate the sialic acid landscape in cancer and inflammatory diseases [4].

Other names

SialoglycansSialylated glycoconjugatesSialic acid receptorsHost cell sialic acidsSialylated glycans

Drugs primarily act by inhibiting viral neuraminidases to prevent the cleavage of sialic acid receptors, thereby trapping viruses on the cell surface (Wasik B.R., et al., 2016) [3]. In cancer, sialidase-based therapies enzymatically remove sialic acids from the cell surface to enhance immune cell activation and reduce tumor growth (Bull C., et al., 2017) [4].