Snake venom galactoside-binding lectin from Bothrops jararacussu: Special role in leukocytes activation and function

Snake venom galactoside-binding lectins (SVgalLs) comprise a group of toxins with the ability to bind specifically, reversibly, and non-covalently to galactose-containing carbohydrates in a Ca²⁺-dependent manner. Several SVgalLs have been identified and isolated from Bothrops snake venoms, presenting highly similar structures and biological functions. BjcuL is a galactoside binding C-type lectin isolated from the venom of South America Bothrops jararacussu and consists of the most investigated lectin. Previous studies have deeply investigated the participation of BjcuL in physiopathological events, especially involving its participation in inflammation. The lectin has been demonstrated as a pro-inflammatory agent, capable of triggering inflammatory events related to local and systemic leukocyte function. This activity is mediated by its binding to galactose-containing glycans on the cell surface to trigger different intracellular signaling and promote functional activation as rolling, adhesion, and migration of leukocytes, production of inflammatory mediators, and a killing profile of phagocytes. Furthermore, this review highlights not only the current understanding of snake venom lectins in pathophysiology and inflammation research but also explores potential future advancements, including the application of emerging technologies such as structural bioinformatics, high-throughput screening, and advanced omics approaches to uncover novel therapeutic targets and biotechnological applications.