Abstract:
:Snake venoms contain various proteins, especially phospholipases A2 (PLA2s), which present potential applications in diverse areas of health and medicine. In this study, a new basic PLA2 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, BmajPLA2-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 BmajPLA2-II as a basic Lys49 PLA2 homologue, compatible with other basic snake venom PLA2s (svPLA2), with a tendency to form aggregations. The in vitro anti-parasitic potential of B. marajoensis venom and of BmajPLA2-II was evaluated against Leishmania infantum promastigotes and Trypanosoma cruzi epimastigotes, showing significant activity at a concentration of 100μg/mL. The venom and BmajPLA2-II presented IC50 of 0.14±0.08 and 6.41±0.64μg/mL, respectively, against intraerythrocytic forms of Plasmodium falciparum with CC50 cytotoxicity values against HepG2 cells of 43.64±7.94 and >150μg/mL, respectively. The biotechnological potential of these substances in relation to leishmaniasis, Chagas disease and malaria should be more deeply investigated.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Grabner AN,Alfonso J,Kayano AM,Moreira-Dill LS,Dos Santos APA,Caldeira CAS,Sobrinho JC,Gómez A,Grabner FP,Cardoso FF,Zuliani JP,Fontes MRM,Pimenta DC,Gómez CV,Teles CBG,Soares AM,Calderon LAdoi
10.1016/j.ijbiomac.2017.04.013subject
Has Abstractpub_date
2017-09-01 00:00:00pages
571-581eissn
0141-8130issn
1879-0003pii
S0141-8130(16)30677-8journal_volume
102pub_type
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