In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper

ABSTRACT: The antimicrobial and antiparasite activity of phospholipase A2 (PLA2) from snakes and bees has been extensively explored. We studied the antiplasmodial effect of the whole venom of the snake Bothrops asper and of two fractions purified by ion-exchange chromatography: one containing cataly...

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Autores:
Quintana Castillo, Juan Carlos
Vargas Muñoz, Leidy Johana
Segura Latorre, Cesar
Gutiérrez, José María
Alarcón Pérez, Juan Carlos
Tipo de recurso:
Article of investigation
Fecha de publicación:
2012
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/23807
Acceso en línea:
http://hdl.handle.net/10495/23807
Palabra clave:
Venenos de Serpiente
Plasmodium falciparum
Snake Venoms
Actividad enzimática
Enzyme activity
Bothrops asper
Phospholipase A2
http://aims.fao.org/aos/agrovoc/c_2604
Rights
openAccess
License
http://creativecommons.org/licenses/by/2.5/co/
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oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/23807
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
title In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
spellingShingle In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
Venenos de Serpiente
Plasmodium falciparum
Snake Venoms
Actividad enzimática
Enzyme activity
Bothrops asper
Phospholipase A2
http://aims.fao.org/aos/agrovoc/c_2604
title_short In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
title_full In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
title_fullStr In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
title_full_unstemmed In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
title_sort In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asper
dc.creator.fl_str_mv Quintana Castillo, Juan Carlos
Vargas Muñoz, Leidy Johana
Segura Latorre, Cesar
Gutiérrez, José María
Alarcón Pérez, Juan Carlos
dc.contributor.author.none.fl_str_mv Quintana Castillo, Juan Carlos
Vargas Muñoz, Leidy Johana
Segura Latorre, Cesar
Gutiérrez, José María
Alarcón Pérez, Juan Carlos
dc.subject.decs.none.fl_str_mv Venenos de Serpiente
Plasmodium falciparum
topic Venenos de Serpiente
Plasmodium falciparum
Snake Venoms
Actividad enzimática
Enzyme activity
Bothrops asper
Phospholipase A2
http://aims.fao.org/aos/agrovoc/c_2604
dc.subject.agrovoc.none.fl_str_mv Snake Venoms
Actividad enzimática
Enzyme activity
dc.subject.proposal.spa.fl_str_mv Bothrops asper
Phospholipase A2
dc.subject.agrovocuri.none.fl_str_mv http://aims.fao.org/aos/agrovoc/c_2604
description ABSTRACT: The antimicrobial and antiparasite activity of phospholipase A2 (PLA2) from snakes and bees has been extensively explored. We studied the antiplasmodial effect of the whole venom of the snake Bothrops asper and of two fractions purified by ion-exchange chromatography: one containing catalytically-active phospholipases A2 (PLA2) (fraction V) and another containing a PLA2 homologue devoid of enzymatic activity (fraction VI). The antiplasmodial effect was assessed on in vitro cultures of Plasmodium falciparum. The whole venom of B. asper, as well as its fractions V and VI, were active against the parasite at 0.13 ± 0.01 μg/mL, 1.42 ± 0.56 μg/mL and 22.89 ± 1.22 μg/mL, respectively. Differences in the cytotoxic activity on peripheral blood mononuclear cells between the whole venom and fractions V and VI were observed, fraction V showing higher toxicity than total venom and fraction VI. Regarding toxicity in mice, the whole venom showed the highest lethal effect in comparison to fractions V and VI. These results suggest that B. asper PLA2 and its homologue have antiplasmodial potential.
publishDate 2012
dc.date.issued.none.fl_str_mv 2012
dc.date.accessioned.none.fl_str_mv 2021-11-05T23:15:11Z
dc.date.available.none.fl_str_mv 2021-11-05T23:15:11Z
dc.type.spa.fl_str_mv info:eu-repo/semantics/article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.hasversion.spa.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
dc.type.redcol.spa.fl_str_mv https://purl.org/redcol/resource_type/ART
dc.type.local.spa.fl_str_mv Artículo de investigación
format http://purl.org/coar/resource_type/c_2df8fbb1
status_str publishedVersion
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10495/23807
dc.identifier.doi.none.fl_str_mv 10.3390/toxins4121500
dc.identifier.eissn.none.fl_str_mv 2072-6651
url http://hdl.handle.net/10495/23807
identifier_str_mv 10.3390/toxins4121500
2072-6651
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Toxins
dc.rights.spa.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.uri.*.fl_str_mv http://creativecommons.org/licenses/by/2.5/co/
dc.rights.accessrights.spa.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.creativecommons.spa.fl_str_mv https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/co/
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
dc.format.extent.spa.fl_str_mv 17
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv MDPI
dc.publisher.group.spa.fl_str_mv Grupo Malaria
Toxinología Alternativas Terapéuticas y Alimentarias
dc.publisher.place.spa.fl_str_mv Basilea, Suiza
institution Universidad de Antioquia
bitstream.url.fl_str_mv http://bibliotecadigital.udea.edu.co/bitstream/10495/23807/2/license_rdf
http://bibliotecadigital.udea.edu.co/bitstream/10495/23807/3/license.txt
http://bibliotecadigital.udea.edu.co/bitstream/10495/23807/1/QuintanaJuan_2012_InVitroAntiplasmodialActivityPhospholipasesA2.pdf
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spelling Quintana Castillo, Juan CarlosVargas Muñoz, Leidy JohanaSegura Latorre, CesarGutiérrez, José MaríaAlarcón Pérez, Juan Carlos2021-11-05T23:15:11Z2021-11-05T23:15:11Z2012http://hdl.handle.net/10495/2380710.3390/toxins41215002072-6651ABSTRACT: The antimicrobial and antiparasite activity of phospholipase A2 (PLA2) from snakes and bees has been extensively explored. We studied the antiplasmodial effect of the whole venom of the snake Bothrops asper and of two fractions purified by ion-exchange chromatography: one containing catalytically-active phospholipases A2 (PLA2) (fraction V) and another containing a PLA2 homologue devoid of enzymatic activity (fraction VI). The antiplasmodial effect was assessed on in vitro cultures of Plasmodium falciparum. The whole venom of B. asper, as well as its fractions V and VI, were active against the parasite at 0.13 ± 0.01 μg/mL, 1.42 ± 0.56 μg/mL and 22.89 ± 1.22 μg/mL, respectively. Differences in the cytotoxic activity on peripheral blood mononuclear cells between the whole venom and fractions V and VI were observed, fraction V showing higher toxicity than total venom and fraction VI. Regarding toxicity in mice, the whole venom showed the highest lethal effect in comparison to fractions V and VI. These results suggest that B. asper PLA2 and its homologue have antiplasmodial potential.COL0014476COL000752417application/pdfengMDPIGrupo MalariaToxinología Alternativas Terapéuticas y AlimentariasBasilea, Suizainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARTArtículo de investigaciónhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/co/http://purl.org/coar/access_right/c_abf2https://creativecommons.org/licenses/by/4.0/In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake bothrops asperVenenos de SerpientePlasmodium falciparumSnake VenomsActividad enzimáticaEnzyme activityBothrops asperPhospholipase A2http://aims.fao.org/aos/agrovoc/c_2604ToxinsToxins15001516412CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927http://bibliotecadigital.udea.edu.co/bitstream/10495/23807/2/license_rdf1646d1f6b96dbbbc38035efc9239ac9cMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/23807/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD53ORIGINALQuintanaJuan_2012_InVitroAntiplasmodialActivityPhospholipasesA2.pdfQuintanaJuan_2012_InVitroAntiplasmodialActivityPhospholipasesA2.pdfArtículo de investigaciónapplication/pdf1678179http://bibliotecadigital.udea.edu.co/bitstream/10495/23807/1/QuintanaJuan_2012_InVitroAntiplasmodialActivityPhospholipasesA2.pdf59f6476d9bae3c1e5ce7816ff0e7d459MD5110495/23807oai:bibliotecadigital.udea.edu.co:10495/238072021-11-05 18:15:11.529Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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