A C-type lectin from Bothrops jararacussu venom reprograms endothelial cell biology

• Published in: Angiogenesis (London)
• Main Authors: Baudou, Federico G, Charó, Nancy L, Scheidegger, Marco A, Stupirski, Juan C, Pérez Sáez, Juan M, Troncoso, María F, Massaro, Mora, de Roodt, Adolfo R, De Marzi, Mauricio C, Schattner, Mirta, Rabinovich, Gabriel A
• Format: Journal Article
• Language: English
• Published: Germany 15.06.2024
• Subjects: Galectin-1; Snake venom; Inflammation; Endothelial cells; C-type lectin
• ISSN: 1573-7209; 1573-7209
• DOI: 10.1007/s10456-024-09931-x

Snake venoms are intricate mixtures of enzymes and bioactive factors that induce a range of detrimental effects in afflicted hosts. Certain Viperids, including Bothrops jararacussu, harbor C-type lectins (CTLs) known for their modulation of a variety of host cellular responses. In this study, we isolated and purified BjcuL, a CTL from B. jararacussu venom and investigated its impact on endothelial cell behavior, contrasting it with human galectin-1 (Gal-1), a prototype member of the galectin family with shared β-galactoside-binding activity. We found that BjcuL binds to human dermal microvascular endothelial cells (HMECs) in a concentration- and carbohydrate-dependent fashion and reprograms the function of these cells, favoring a pro-inflammatory and pro-coagulant endothelial phenotype. In light of the quest for universal antagonists capable of mitigating the harmful consequences of snake venoms, BjcuL emerges as a promising target to be blocked in order to regulate pathological endothelial cell responses.