BmajPLA 2 -II, a basic Lys49-phospholipase A 2 homologue from Bothrops marajoensis snake venom with parasiticidal potential
| Autor: | Celeste Vega Gómez, Daniel C. Pimenta, Marcos R.M. Fontes, Leandro S. Moreira-Dill, Andreimar M. Soares, Ana Gómez, Anderson M. Kayano, Jorge Alfonso, Amy N. Grabner, Fábio F. Cardoso, Fernando P. Grabner, Leonardo A. Calderon, Ana Paula de Azevedo dos Santos, Carolina Bioni Garcia Teles, Cleópatra A.S. Caldeira, Juliana P. Zuliani, Juliana C. Sobrinho |
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| Přispěvatelé: | UNIR, CEDIC, Fiocruz Rondônia, FSL, Universidade Estadual Paulista (Unesp), Instituto Butantan |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Chagas disease Snake venoms Venom medicine.disease_cause Biochemistry 03 medical and health sciences chemistry.chemical_compound Phospholipase A2 Structural Biology Bothrops marajoensis medicine Sodium dodecyl sulfate Cytotoxicity Trypanosoma cruzi Leishmaniasis Molecular Biology Polyacrylamide gel electrophoresis 030102 biochemistry & molecular biology biology Toxin General Medicine biology.organism_classification Malaria 030104 developmental biology chemistry Snake venom Immunology Leishmania infantum |
| Zdroj: | Scopus Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2017.04.013 |
| Popis: | Made available in DSpace on 2018-12-11T16:47:04Z (GMT). No. of bitstreams: 0 Previous issue date: 2017-09-01 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 100 μg/mL. The venom and BmajPLA2-II presented IC50 of 0.14 ± 0.08 and 6.41 ± 0.64 μg/mL, respectively, against intraerythrocytic forms of Plasmodium falciparum with CC50 cytotoxicity values against HepG2 cells of 43.64 ± 7.94 and >150 μg/mL, respectively. The biotechnological potential of these substances in relation to leishmaniasis, Chagas disease and malaria should be more deeply investigated. Centro de Estudos de Biomoléculas Aplicadas à Saúde CEBio Fundação Oswaldo Cruz FIOCRUZ Fiocruz Rondônia Departamento de Medicina Universidade Federal de Rondônia UNIR Centro para el Desarrollo de la Investigación Científica CEDIC Laboratório da Plataforma de Bioensaios de Malária e Leishmaniose Fiocruz Rondônia Faculdade São Lucas FSL Departamento de Física e Biofísica Universidade Estadual Paulista UNESP Laboratório de Bioquímica e Biofísica Instituto Butantan Departamento de Física e Biofísica Universidade Estadual Paulista UNESP |
| Databáze: | OpenAIRE |
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