ABSTRACT
Snake venoms contain various proteins, especially phospholipases A(2) (PLA(2)s), which present potential applications in diverse areas of health and medicine. In this study, a new basic PLA(2) from Bothrops marajoensis with parasiticidal activity was purified and characterized biochemically and biologically. B. marajoensis venom was fractionated through cation exchange followed by reverse phase chromatographies. The isolated toxin, BmajPLA(2)-II, was structurally characterized with MALDI-TOF (Matrix-assisted laser desorption/ionization-time of flight) mass spectrometry, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), followed by two-dimensional electrophoresis, partial amino acid sequencing, an enzymatic activity assay, circular dichroism, and dynamic light scattering assays. These structural characterization tests presented BmajPLA(2)-II as a basic Lys49 PLA(2) homologue, compatible with other basic snake venom PLA(2)s (svPLA(2)), with a tendency to form aggregations. The in vitro anti-parasitic potential of B. marajoensis venom and of BmajPLA(2)-II was evaluated against Leishmania infantum promastigotes and Trypanosoma cruzi epimastigotes, showing significant activity at a concentration of 100 mu g/mL. The venom and BmajPLA(2)-II presented IC50 of 0.14 +/- 0.08 and 6.41 +/- 0.64 mu g/mL, respectively, against intraerythrocytic forms of Plasmodium falciparum with CC50 cytotoxicity values against HepG2 cells of 43.64 +/- 1 7.94 and >150 mu g/mL, respectively. The biotechnological potential of these substances in relation to leishmaniasis, Chagas disease and malaria should be more deeply investigated.
