Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from Bothrops jararacussu venom

Utilizing fluorescence microscopy, we observed that biotinylated-BJcuL was evenly distributed on the neutrophil surface, selectively inhibited by D-galactose. Lectin was able to induce modification in the neutrophil morphology in a spherical shape for a polarized observed by optical microscopy and exposure to BJcuL in a Boyden chamber assay resulted in cell migration. After 30 minutes of incubation with BJcuL we found enhanced neutrophil functions, such as respiratory burst, zymozan phagocytosis and an increase in lissosomal volume. In addition, BJcuL delays late apoptosis neutrophils.These results demonstrate that BJcuL can be implicated in a wide variety of immunological functions including first-line defense against pathogens, cell trafficking and induction of the innate immune response since lectin was capable of inducing potent neutrophil activation.Neutrophils are key players in the innate immune response and their recruitment from the microvasculature to inflammation sites includes rolling, firm adhesion, and transmigration through the vessel wall [1]. Neutrophil activation leads to directed migration with changes in cell morphology from rounded cells covered with microvilli to elongated ruffled cells [2,3]. Neutrophils exert their bactericidal activity at the inflammatory site through recognition and phagocytosis of the infectious agent, generation of toxic oxygen derivatives, and release of microbicidal molecules from their specialized lysosomes and granules [4]. This sequential process relies on neutrophil interaction with chemoattractants, cytokines and other inflammatory mediators [5].Viperid and elapid snake venoms contain complex mixtures of pharmacologically active molecules, including enzymes and proteins without enzymatic activity, such as C-type lectins. Based on their structural and functional properties snake venom C-type lectins have been classified as true C-type lectins, which contain a carbohydrate recognition domain (CRD) and bind to a speci