Glycan-binding protein (GBP)

Glycan receptors, more formally known as glycan-binding proteins (GBPs) or lectins, are a diverse class of proteins that recognize and bind to specific carbohydrate structures (glycans) on cell surfaces or within the extracellular matrix [1.1.5, 1.2.5]. These receptors, which include families such as selectins, siglecs, and galectins, are essential for mediating cell-cell adhesion, leukocyte trafficking, and immune system regulation by decoding the biological information stored in the glycome [1.1.3, 1.3.4]. In pathological states, glycan receptors are frequently involved in cancer metastasis, chronic inflammation, and the entry of pathogens like viruses and bacteria into host cells [1.3.1, 1.4.2]. Therapeutic strategies targeting these receptors include monoclonal antibodies and glycomimetics designed to disrupt pathological interactions, such as the P-selectin inhibitor crizanlizumab used in sickle cell disease [1.3.1, 1.3.5]. Additionally, some glycan receptors are exploited for targeted drug delivery, such as the asialoglycoprotein receptor (ASGPR) in the liver [1.3.2]. Despite their therapeutic potential, the widespread distribution of glycans and the low affinity of individual binding events present significant challenges in achieving high specificity and efficacy [1.4.1].

Other names

Glycan receptorsLectinsCarbohydrate-binding proteinsGBPsSelectinsSiglecsGalectinsC-type lectin receptors

Inhibition of carbohydrate-protein interactions to block pathological cell adhesion or modulate immune signaling; exploitation of receptor-mediated endocytosis for targeted drug delivery (e.g., GalNAc-conjugates).