Carbohydrate-binding enzymes and lectins

Carbohydrate-binding enzymes and lectins represent a broad functional class of proteins that recognize, bind, or modify glycan structures (Essentials of Glycobiology [NCBI]). Lectins are non-enzymatic proteins, such as selectins and galectins, that facilitate cell-cell communication, adhesion, and immune signaling by binding specific carbohydrate moieties (Gabius et al., 2011). Carbohydrate-binding enzymes, often categorized as Carbohydrate-Active Enzymes (CAZymes), include glycoside hydrolases and glycosyltransferases that catalyze the synthesis and degradation of complex sugars (Lombard et al., 2014). These proteins are critical in numerous physiological processes, including the inflammatory response and metabolic regulation, but are also exploited by pathogens for host entry. Therapeutic strategies targeting this group include small-molecule inhibitors of viral neuraminidases to treat influenza, monoclonal antibodies against selectins to prevent vaso-occlusive crises in sickle cell disease, and enzyme replacement therapies for lysosomal storage disorders (Ataga et al., 2017; FDA, 2019).

Other names

Glycan-binding proteinsCarbohydrate-active enzymesCAZymesLectinsSugar-binding proteins

Inhibition of enzymatic glycan processing (e.g., neuraminidase or glucosidase inhibition) or competitive antagonism of carbohydrate-binding sites on lectins to prevent cell adhesion and pathological signaling.