Cell-surface glycoprotein carbohydrate structures

Cell-surface glycoprotein carbohydrate structures, commonly known as glycans, are complex sugar chains covalently attached to proteins on the plasma membrane. These structures are fundamental to life, mediating essential biological processes such as cell-cell recognition, adhesion, and the modulation of signal transduction pathways [1][2]. In pathological states, particularly malignancy, the cellular glycosylation machinery is often dysregulated, resulting in the presentation of truncated or hypersialylated glycans known as tumor-associated carbohydrate antigens (TACAs) [3]. These aberrant structures contribute to cancer progression by promoting metastasis and enabling immune evasion through the recruitment of inhibitory receptors on immune cells [2][4]. Therapeutically, these carbohydrate structures are targeted by monoclonal antibodies, glycan-mimetic drugs, and vaccines designed to elicit an immune response against specific glycan motifs [3][5]. Furthermore, many pathogens, including the influenza virus, utilize cell-surface glycans as receptors for entry, making these structures vital targets for antiviral and antibacterial interventions [1][6]. References: [1] Varki A, et al. Essentials of Glycobiology. 3rd edition. 2015. [2] Pinho SS, Reis CA. Nat Rev Cancer. 2015;15(9):540-55. [3] Fuster MM, Esko JD. Nat Rev Cancer. 2005;5(7):526-42. [4] Rodriguez E, et al. Cancer Immunol Immunother. 2018;67(12):1965-1976. [5] Heimburg-Molinaro J, et al. Vaccine. 2011;29(48):8802-26. [6] Imberty A, Varrot A. Curr Opin Struct Biol. 2008;18(5):567-71.

Other names

GlycansCell surface oligosaccharidesTumor-associated carbohydrate antigens (TACAs)Glycosylation patternsSurface glycoconjugatesN-linked glycansO-linked glycans

Competitive inhibition of glycan-lectin interactions, enzymatic cleavage of terminal saccharides, antibody-mediated targeting of carbohydrate epitopes, and blockade of pathogen-host glycan interactions.