BmajPLA2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential

Detalhes bibliográficos
Autor(a) principal: Grabner, Amy N.
Data de Publicação: 2017
Outros Autores: 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.
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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spelling 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
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