Host cell-surface sialic acid-containing glycan receptor (Sia-glycan receptor)

Host cell-surface sialic acid-containing glycan receptors are terminal carbohydrate structures found on glycoproteins and glycolipids of the eukaryotic cell membrane [1.1.1, 1.4.3]. These sialoglycans play a fundamental role in biological processes such as cell-cell recognition, immune system regulation via Siglec receptors, and maintaining the structural integrity of the glycocalyx [1.1.2, 1.4.2]. They are critically exploited by a wide range of pathogens, including influenza viruses, coronaviruses, and various bacteria, which utilize specific sialic acid linkages (e.g., alpha2-3 or alpha2-6) as primary attachment points for cell entry [1.1.4, 1.2.2]. In oncology, hypersialylation of tumor cells serves as an immune evasion mechanism by engaging inhibitory Siglec receptors on immune cells, thereby dampening the anti-tumor response [1.1.1, 1.4.5]. Therapeutic strategies targeting these receptors include the use of recombinant sialidases like DAS181 to enzymatically remove the terminal sugars, effectively blocking viral infection by destroying the host-cell receptor [1.3.1, 1.3.4]. Additionally, the sialic acid-Siglec axis is being explored for the development of immunotherapies in cancer and autoimmune diseases [1.1.2, 1.4.1]. These receptors also participate in cardiovascular health and neurodevelopment, where they modulate leukocyte recruitment and synaptic plasticity [1.4.2, 1.4.4]. Understanding the diversity of these glycan structures is essential for developing broad-spectrum antivirals and targeted cancer therapies [1.2.3, 1.4.5].

Other names

Sialic acid receptorSialoglycanSialylated glycoconjugateN-acetylneuraminic acid (Neu5Ac) receptorSiglec ligandSialic acid-containing glycan

Enzymatic removal of terminal sialic acid residues (desialylation) to prevent pathogen attachment; competitive inhibition of viral binding using decoy receptors; modulation of Siglec-mediated immune signaling pathways.