Biological activities of a lectin from Bothrops jararacussu snake venom.

Abstract Snake venoms contain saccharide-binding lectins. In this work, we examined the biological activities of a lectin (BjcuL) purified from Bothrops jararacussu snake venom by chromatography on non-derivatized Sepharose 4B and Sephacryl S-200 HR. The protein, a homodimer with subunits of 14.5 kDa, gave a single immunoprecipitin line in immunoelectrophoresis and cross-reacted in ELISA with antivenoms raised against Bothrops spp. (lanceheads), Micrurus spp. (coral snakes), Crotalus durissus terrificus (South American rattlesnake), and arthropod ( Loxosceles gaucho, Phoneutria nigriventer and Tityus serrulatus ) venoms. BjcuL agglutinated human formaldehyde-fixed erythrocytes at ≥100 ng/ml and was inhibited by lactose and EDTA (≥2 mM) and high concentrations (>100 mM) of glucose and sucrose, but not by N -acetylglucosamine. BjcuL had no direct hemolytic activity and was devoid of esterase, PLA 2 and proteolytic activities. The lectin (up to 200 μg/ml) did not aggregate human platelet-rich plasma (PRP) or washed platelets (WP), nor did it alter the aggregation induced by ADP in PRP or by thrombin in WP. When injected into mouse hind paws, BjcuL (10–100 μg/paw) caused edema and increased vascular permeability, with a maximum effect after 1 h that persisted for up to 6 h (edema) or gradually decreased after the peak interval (vascular permeability). No hemorrhage was observed in BjcuL-injected paws. In anesthetized rats, B. jararacussu venom (200 μg/kg, i.v.) produced sustained hypotension (maximum decrease of ∼60%) whereas a similar dose of BjcuL decreased the blood pressure by ∼15%, with a rapid return to the resting level.