Biotechnological Applications of C-Type Lectins Isolated from Snake Venoms

Snake venoms are rich sources of molecules with pharmacological potential, with approximately 90% of their composition consisting of proteins and peptides responsible for their biological activities. These proteins are classified as enzymatic or non-enzymatic. Enzymatic proteins function as catalysts in regulatory chemical reactions, whereas non-enzymatic proteins, despite lacking catalytic activity, play essential roles in physiological processes. Lectins are non-enzymatic proteins of non-immune origin characterized by carbohydrate- and glycoprotein-binding domains, enabling their ability to agglutinate erythrocytes. C-type lectins and C-type lectin-like proteins are commonly found in snake venoms and are associated with hemostatic disturbances, particularly bleeding and coagulation disorders. This review provides a comprehensive analysis of studies published over the past decade on lectins isolated from snake venom, addressing their definitions, classifications, structural characteristics, and mechanisms of action, as well as their relevance in biotechnological applications. Although progress has been made in elucidating their pharmacological properties, most studies have focused on plant lectins. In contrast, research on snake venom lectins remains limited, particularly regarding their heterologous activities. This gap, especially compared to other venom-derived molecules, highlights the need to further expand research on this class of proteins.