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In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper
The antimicrobial and antiparasite activity of phospholipase A(2) (PLA(2)) 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 catalyticall...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3528259/ https://www.ncbi.nlm.nih.gov/pubmed/23242318 http://dx.doi.org/10.3390/toxins4121500 |
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author | Castillo, Juan Carlos Quintana Vargas, Leidy Johana Segura, Cesar Gutiérrez, José María Pérez, Juan Carlos Alarcón |
author_facet | Castillo, Juan Carlos Quintana Vargas, Leidy Johana Segura, Cesar Gutiérrez, José María Pérez, Juan Carlos Alarcón |
author_sort | Castillo, Juan Carlos Quintana |
collection | PubMed |
description | The antimicrobial and antiparasite activity of phospholipase A(2) (PLA(2)) 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 A(2) (PLA(2)) (fraction V) and another containing a PLA(2) 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 PLA(2) and its homologue have antiplasmodial potential. |
format | Online Article Text |
id | pubmed-3528259 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-35282592013-01-02 In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper Castillo, Juan Carlos Quintana Vargas, Leidy Johana Segura, Cesar Gutiérrez, José María Pérez, Juan Carlos Alarcón Toxins (Basel) Article The antimicrobial and antiparasite activity of phospholipase A(2) (PLA(2)) 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 A(2) (PLA(2)) (fraction V) and another containing a PLA(2) 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 PLA(2) and its homologue have antiplasmodial potential. MDPI 2012-12-14 /pmc/articles/PMC3528259/ /pubmed/23242318 http://dx.doi.org/10.3390/toxins4121500 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Castillo, Juan Carlos Quintana Vargas, Leidy Johana Segura, Cesar Gutiérrez, José María Pérez, Juan Carlos Alarcón In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper |
title | In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper |
title_full | In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper |
title_fullStr | In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper |
title_full_unstemmed | In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper |
title_short | In Vitro Antiplasmodial Activity of Phospholipases A(2) and a Phospholipase Homologue Isolated from the Venom of the Snake Bothrops asper |
title_sort | in vitro antiplasmodial activity of phospholipases a(2) and a phospholipase homologue isolated from the venom of the snake bothrops asper |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3528259/ https://www.ncbi.nlm.nih.gov/pubmed/23242318 http://dx.doi.org/10.3390/toxins4121500 |
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