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Host glycan and lectin-mediated SARS-CoV-2 entry. Sialylated glycans and glycolipids, including gangliosides (GM1, GM2, GM3) and mucin-associated sialoglycans, serve as low-affinity but multivalent attachment factors that engage the spike via the RBD and NTD. HSPGs on the host cell surface bind to the SARS-CoV-2 spike through electrostatic interactions involving a basic patch in the RBD and the S1/S2 PRRAR, thereby immobilizing virions and enhancing ACE2 encounter. Siglec-1, expressed on dendritic cells and macrophages, captures virions through host-derived sialylated gangliosides incorporated into the viral envelope, enabling the trans-infection of ACE2-positive target cells. Soluble galectins (Gal-3, Gal-9) and membrane-bound C-type lectin receptors (DC-SIGN, L-SIGN, MR) bind spike N-glycans, promoting virion retention, cross-linking, and immune cell-mediated dissemination. ABO(H) blood group antigens expressed on mucosal epithelial surfaces modulate spike attachment, with preferential recognition of blood group A trisaccharides and minimal binding to the unmodified H(O) antigen. Together, these interactions form a multivalent glycan–lectin network that enhances viral attachment and cell-associated spread prior to ACE2-dependent membrane fusion. Created in BioRender. Oh, H. (2026) https://BioRender.com/59lcolt , accessed on 3 February 2026.

Journal: International Journal of Molecular Sciences

Article Title: Host Glycan–Lectin Interplay in SARS-CoV-2 Infection

doi: 10.3390/ijms27031608

Figure Lengend Snippet: Host glycan and lectin-mediated SARS-CoV-2 entry. Sialylated glycans and glycolipids, including gangliosides (GM1, GM2, GM3) and mucin-associated sialoglycans, serve as low-affinity but multivalent attachment factors that engage the spike via the RBD and NTD. HSPGs on the host cell surface bind to the SARS-CoV-2 spike through electrostatic interactions involving a basic patch in the RBD and the S1/S2 PRRAR, thereby immobilizing virions and enhancing ACE2 encounter. Siglec-1, expressed on dendritic cells and macrophages, captures virions through host-derived sialylated gangliosides incorporated into the viral envelope, enabling the trans-infection of ACE2-positive target cells. Soluble galectins (Gal-3, Gal-9) and membrane-bound C-type lectin receptors (DC-SIGN, L-SIGN, MR) bind spike N-glycans, promoting virion retention, cross-linking, and immune cell-mediated dissemination. ABO(H) blood group antigens expressed on mucosal epithelial surfaces modulate spike attachment, with preferential recognition of blood group A trisaccharides and minimal binding to the unmodified H(O) antigen. Together, these interactions form a multivalent glycan–lectin network that enhances viral attachment and cell-associated spread prior to ACE2-dependent membrane fusion. Created in BioRender. Oh, H. (2026) https://BioRender.com/59lcolt , accessed on 3 February 2026.

Article Snippet: Indeed, Ryzhikov et al. reported that SARS-CoV-2 Spike binds poly-N-acetyllactosamine (LacNAc) chains after desialylation, exposing Galβ1-4GlcNAc units, the canonical ligands for galectin-3 and galectin-9 (Gal-9) [ ].

Techniques: Glycoproteomics, Derivative Assay, Infection, Membrane, Binding Assay

Human galectin-4C inhibits A antigen-dependent enhancement of SARS-CoV-2 entry. ( a ) Enhanced SARS-CoV-2 pseudovirus infection when presenting A-type glycans. The spike RBD preferentially recognizes the blood group A trisaccharide expressed on mucosal epithelial glycoconjugates, with weaker binding to B antigens and unmodified H(O) antigen . ( b ) Galectin-4C, which selectively binds blood group A determinants, inhibits viral entry in A-expressing cells. Galectin-4C hinders glycan attachment sites, reducing virus entry at the epithelial surface. Created in BioRender. Oh, H. (2026) https://biorender.com/w0woy23 (accessed on 3 February 2026).

Journal: International Journal of Molecular Sciences

Article Title: Host Glycan–Lectin Interplay in SARS-CoV-2 Infection

doi: 10.3390/ijms27031608

Figure Lengend Snippet: Human galectin-4C inhibits A antigen-dependent enhancement of SARS-CoV-2 entry. ( a ) Enhanced SARS-CoV-2 pseudovirus infection when presenting A-type glycans. The spike RBD preferentially recognizes the blood group A trisaccharide expressed on mucosal epithelial glycoconjugates, with weaker binding to B antigens and unmodified H(O) antigen . ( b ) Galectin-4C, which selectively binds blood group A determinants, inhibits viral entry in A-expressing cells. Galectin-4C hinders glycan attachment sites, reducing virus entry at the epithelial surface. Created in BioRender. Oh, H. (2026) https://biorender.com/w0woy23 (accessed on 3 February 2026).

Article Snippet: Indeed, Ryzhikov et al. reported that SARS-CoV-2 Spike binds poly-N-acetyllactosamine (LacNAc) chains after desialylation, exposing Galβ1-4GlcNAc units, the canonical ligands for galectin-3 and galectin-9 (Gal-9) [ ].

Techniques: Infection, Binding Assay, Expressing, Glycoproteomics, Virus