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...
- 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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UDEA2 |
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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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bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositorio Institucional Universidad de Antioquia |
repository.mail.fl_str_mv |
andres.perez@udea.edu.co |
_version_ |
1812173156144644096 |
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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 |