Host sialic acid-containing glycoconjugate receptor

Host sialic acid-containing glycoconjugate receptors are a diverse class of glycoproteins and glycolipids on the surface of mammalian cells that feature terminal sialic acid residues, primarily N-acetylneuraminic acid (Neu5Ac) (Ansun Biopharma, 2025). These molecules serve as the primary attachment points for numerous human pathogens, including influenza A, B, and C viruses, parainfluenza viruses, and certain coronaviruses like MERS-CoV and SARS-CoV-2 (NIH, 2018; MDPI, 2022). Pathogens utilize viral surface proteins, such as hemagglutinin or spike proteins, to recognize specific sialic acid linkages, such as α2,3-linked or α2,6-linked residues, which determine host range and tissue tropism (NIH, 2023). Beyond their role in infection, these sialoglycans act as self-associated molecular patterns (SAMPs) that interact with host immune receptors, specifically the Siglec family, to regulate immune responses and maintain self-tolerance (NIH, 2024). In oncology, the hypersialylation of these receptors on tumor cells is a known mechanism of immune evasion, as it engages inhibitory Siglecs on myeloid and lymphoid cells (NIH, 2022). Therapeutic interventions include the recombinant sialidase DAS181 (Fludase), which enzymatically cleaves these receptors to prevent viral entry, and experimental masking agents designed to block pathogen access (Ansun Biopharma, 2025; NIH, 2023).

Other names

Sialic acid receptorsSialoglycansSialoglycoconjugatesNeu5Ac-containing receptorsHost cell sialoglycoproteinsHost cell sialoglycolipidsSialic acid-containing glycans

Enzymatic desialylation of host cell surfaces to prevent viral attachment and entry; reduction of receptor expression; and competitive masking of sialic acid residues to block pathogen access (Ansun Biopharma, 2025; NIH, 2023).