BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.ijbiomac.2017.04.013 http://hdl.handle.net/11449/169663 |
Resumo: | 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. |
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BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potentialBothrops marajoensisChagas diseaseLeishmaniasisMalariaPhospholipase A2Snake venomsSnake 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 UNIRCentro para el Desarrollo de la Investigación Científica CEDICLaboratório da Plataforma de Bioensaios de Malária e Leishmaniose Fiocruz RondôniaFaculdade São Lucas FSLDepartamento de Física e Biofísica Universidade Estadual Paulista UNESPLaboratório de Bioquímica e Biofísica Instituto ButantanDepartamento de Física e Biofísica Universidade Estadual Paulista UNESPUNIRCEDICFiocruz RondôniaFSLUniversidade Estadual Paulista (Unesp)Instituto ButantanGrabner, Amy N.Alfonso, JorgeKayano, Anderson M.Moreira-Dill, Leandro S.dos Santos, Ana Paula de A.Caldeira, Cleópatra A.S.Sobrinho, Juliana C.Gómez, AnaGrabner, Fernando P.Cardoso, Fabio F. [UNESP]Zuliani, Juliana PavanFontes, Marcos R.M. [UNESP]Pimenta, Daniel C.Gómez, Celeste VegaTeles, Carolina B.G.Soares, Andreimar M.Calderon, Leonardo A.2018-12-11T16:47:04Z2018-12-11T16:47:04Z2017-09-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article571-581application/pdfapplication/pdfhttp://dx.doi.org/10.1016/j.ijbiomac.2017.04.013International Journal of Biological Macromolecules, v. 102, p. 571-581.1879-00030141-8130http://hdl.handle.net/11449/16966310.1016/j.ijbiomac.2017.04.0132-s2.0-850185591492-s2.0-85018559149.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInternational Journal of Biological Macromolecules0,917info:eu-repo/semantics/openAccess2023-10-18T06:03:47Zoai:repositorio.unesp.br:11449/169663Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:12:42.607067Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
title |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
spellingShingle |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential Grabner, Amy N. Bothrops marajoensis Chagas disease Leishmaniasis Malaria Phospholipase A2 Snake venoms |
title_short |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
title_full |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
title_fullStr |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
title_full_unstemmed |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
title_sort |
BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential |
author |
Grabner, Amy N. |
author_facet |
Grabner, Amy N. Alfonso, Jorge Kayano, Anderson M. Moreira-Dill, Leandro S. dos Santos, Ana Paula de A. Caldeira, Cleópatra A.S. Sobrinho, Juliana C. Gómez, Ana Grabner, Fernando P. Cardoso, Fabio F. [UNESP] Zuliani, Juliana Pavan Fontes, Marcos R.M. [UNESP] Pimenta, Daniel C. Gómez, Celeste Vega Teles, Carolina B.G. Soares, Andreimar M. Calderon, Leonardo A. |
author_role |
author |
author2 |
Alfonso, Jorge Kayano, Anderson M. Moreira-Dill, Leandro S. dos Santos, Ana Paula de A. Caldeira, Cleópatra A.S. Sobrinho, Juliana C. Gómez, Ana Grabner, Fernando P. Cardoso, Fabio F. [UNESP] Zuliani, Juliana Pavan Fontes, Marcos R.M. [UNESP] Pimenta, Daniel C. Gómez, Celeste Vega Teles, Carolina B.G. Soares, Andreimar M. Calderon, Leonardo A. |
author2_role |
author author author author author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
UNIR CEDIC Fiocruz Rondônia FSL Universidade Estadual Paulista (Unesp) Instituto Butantan |
dc.contributor.author.fl_str_mv |
Grabner, Amy N. Alfonso, Jorge Kayano, Anderson M. Moreira-Dill, Leandro S. dos Santos, Ana Paula de A. Caldeira, Cleópatra A.S. Sobrinho, Juliana C. Gómez, Ana Grabner, Fernando P. Cardoso, Fabio F. [UNESP] Zuliani, Juliana Pavan Fontes, Marcos R.M. [UNESP] Pimenta, Daniel C. Gómez, Celeste Vega Teles, Carolina B.G. Soares, Andreimar M. Calderon, Leonardo A. |
dc.subject.por.fl_str_mv |
Bothrops marajoensis Chagas disease Leishmaniasis Malaria Phospholipase A2 Snake venoms |
topic |
Bothrops marajoensis Chagas disease Leishmaniasis Malaria Phospholipase A2 Snake venoms |
description |
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. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-09-01 2018-12-11T16:47:04Z 2018-12-11T16:47:04Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.ijbiomac.2017.04.013 International Journal of Biological Macromolecules, v. 102, p. 571-581. 1879-0003 0141-8130 http://hdl.handle.net/11449/169663 10.1016/j.ijbiomac.2017.04.013 2-s2.0-85018559149 2-s2.0-85018559149.pdf |
url |
http://dx.doi.org/10.1016/j.ijbiomac.2017.04.013 http://hdl.handle.net/11449/169663 |
identifier_str_mv |
International Journal of Biological Macromolecules, v. 102, p. 571-581. 1879-0003 0141-8130 10.1016/j.ijbiomac.2017.04.013 2-s2.0-85018559149 2-s2.0-85018559149.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
International Journal of Biological Macromolecules 0,917 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
571-581 application/pdf application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128481117077504 |