Fucose-binding lectin (FBL)

Fucose-binding lectins are a diverse group of proteins that specifically recognize and bind to L-fucose residues on glycoconjugates, playing essential roles in cell-cell communication and pathogen adhesion (Varki et al., 2017). In humans, the selectin family (E-, L-, and P-selectin) represents the most clinically significant fucose-binding lectins, mediating the recruitment of leukocytes to sites of inflammation and contributing to cancer metastasis (Ley et al., 2007; Munkley, 2020). Pathogenic bacteria, most notably Pseudomonas aeruginosa, utilize fucose-binding lectins like LecB (PA-IIL) to adhere to host tissues and stabilize biofilm architecture, which protects the bacteria from antibiotics and the immune system (Sommer et al., 2018). Therapeutic strategies targeting these lectins involve glycomimetic drugs, such as Uproleselan (GMI-1271), which act as competitive inhibitors of the carbohydrate recognition domain to block pathological interactions (DeAngelo et al., 2022). These agents are currently being investigated for treating acute myeloid leukemia, sickle cell disease, and chronic respiratory infections. Challenges in targeting fucose-binding lectins include achieving high specificity to avoid off-target effects on endogenous glycosylation and overcoming the pharmacokinetic limitations of carbohydrate-based molecules.

Other names

Fucophilic lectinL-fucose-binding proteinFucose-specific lectinLecBPA-IILSelectin

Competitive inhibition of the carbohydrate recognition domain (CRD) to prevent glycan-mediated adhesion