Abstract
Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent manner. The binding was partially inhibited in the presence of D-galactose. BjcuL (1.25-10µg/30µl) potential was investigated for leukocyte rolling and adhesion to endothelial cells in living microvessels using intravital microscopy, which showed that it induced a dose-dependent increase in rolling and adherence of leukocytes, acting directly on endothelial cells of postcapillary venules. The specific association between lectins and their ligands, either on the cell surface or on the ECM, is related to a variety of biological processes. The complementary characterization of BjcuL, shown here, is useful to further understand the venom effects and as a background for future investigation for therapeutic strategies.
Highlights
Bothrops species, known as jararacas, are widely found from the South to the Northeast of Brazil and in Bolivia, Paraguay and Northern Argentina [2]
Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039–5.0μg/100μl) was capable of binding to fibronectin and vitronectin in a dose-dependent manner
We demonstrated the capacity of the lectin to interact in vitro with fibronectin and vitronectin and to promote in vivo migration of leukocytes
Summary
Known as jararacas, are widely found from the South to the Northeast of Brazil and in Bolivia, Paraguay and Northern Argentina [2]. ABSTRACT: Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039–5.0μg/100μl) was capable of binding to fibronectin and vitronectin in a dose-dependent manner.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Journal of Venomous Animals and Toxins including Tropical Diseases
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.