In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asper
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-ac...
- Autores:
-
Quintana Castillo, Juan Carlos
Vargas L.J.
Segura C.
Gutiérrez J.M.
Pérez J.C.A.
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2012
- Institución:
- Universidad Cooperativa de Colombia
- Repositorio:
- Repositorio UCC
- Idioma:
- OAI Identifier:
- oai:repository.ucc.edu.co:20.500.12494/42902
- Acceso en línea:
- https://doi.org/10.7149/OPA.51.3.50306
https://www.sciencedirect.com/science/article/abs/pii/S0034745014601463
https://hdl.handle.net/20.500.12494/42902
- Palabra clave:
- phospholipase
phospholipase A2
snake venom
acute toxicity
amino acid sequence
antimalarial activity
antiplasmodial activity
article
bothrops asper
cell fractionation
controlled study
cytotoxicity
drug activity
enzyme active site
enzyme activity
hemolysis
IC 50
in vitro study
ion exchange chromatography
LD 50
lethality
nonhuman
nucleotide sequence
peripheral blood mononuclear cell
Plasmodium falciparum
sequence alignment
snake
toxicity testing
Amino Acid Sequence
Animals
Antiprotozoal Agents
Bothrops
Cell Survival
Cells
Cultured
Crotalid Venoms
Erythrocytes
Humans
Lethal Dose 50
Leukocytes
Mononuclear
Mice
Molecular Sequence Data
Phospholipases
Plasmodium falciparum
Sequence Alignment
- Rights
- closedAccess
- License
- http://purl.org/coar/access_right/c_14cb
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Quintana Castillo, Juan CarlosVargas L.J.Segura C.Gutiérrez J.M.Pérez J.C.A.2021-12-16T22:16:36Z2021-12-16T22:16:36Z2012https://doi.org/10.7149/OPA.51.3.50306https://www.sciencedirect.com/science/article/abs/pii/S003474501460146320726651https://hdl.handle.net/20.500.12494/42902Castillo JCQ,Vargas LJ,Segura C,Gutiérrez JM,Pérez JCA. In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asper. Toxins (Basel). 2012. 4. (12):p. 1500-1516. .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. © 2012 by the authors; licensee MDPI, Basel, Switzerland.juan.quintanac@campusucc.edu.co1516-1500MDPI AGphospholipasephospholipase A2snake venomacute toxicityamino acid sequenceantimalarial activityantiplasmodial activityarticlebothrops aspercell fractionationcontrolled studycytotoxicitydrug activityenzyme active siteenzyme activityhemolysisIC 50in vitro studyion exchange chromatographyLD 50lethalitynonhumannucleotide sequenceperipheral blood mononuclear cellPlasmodium falciparumsequence alignmentsnaketoxicity testingAmino Acid SequenceAnimalsAntiprotozoal AgentsBothropsCell SurvivalCellsCulturedCrotalid VenomsErythrocytesHumansLethal Dose 50LeukocytesMononuclearMiceMolecular Sequence DataPhospholipasesPlasmodium falciparumSequence AlignmentIn vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asperArtículohttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/publishedVersionToxinsinfo:eu-repo/semantics/closedAccesshttp://purl.org/coar/access_right/c_14cbPublication20.500.12494/42902oai:repository.ucc.edu.co:20.500.12494/429022024-08-20 16:16:15.815metadata.onlyhttps://repository.ucc.edu.coRepositorio Institucional Universidad Cooperativa de Colombiabdigital@metabiblioteca.com |
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 phospholipase phospholipase A2 snake venom acute toxicity amino acid sequence antimalarial activity antiplasmodial activity article bothrops asper cell fractionation controlled study cytotoxicity drug activity enzyme active site enzyme activity hemolysis IC 50 in vitro study ion exchange chromatography LD 50 lethality nonhuman nucleotide sequence peripheral blood mononuclear cell Plasmodium falciparum sequence alignment snake toxicity testing Amino Acid Sequence Animals Antiprotozoal Agents Bothrops Cell Survival Cells Cultured Crotalid Venoms Erythrocytes Humans Lethal Dose 50 Leukocytes Mononuclear Mice Molecular Sequence Data Phospholipases Plasmodium falciparum Sequence Alignment |
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 L.J. Segura C. Gutiérrez J.M. Pérez J.C.A. |
dc.contributor.author.none.fl_str_mv |
Quintana Castillo, Juan Carlos Vargas L.J. Segura C. Gutiérrez J.M. Pérez J.C.A. |
dc.subject.spa.fl_str_mv |
phospholipase phospholipase A2 snake venom acute toxicity amino acid sequence antimalarial activity antiplasmodial activity article bothrops asper cell fractionation controlled study cytotoxicity drug activity enzyme active site enzyme activity hemolysis IC 50 in vitro study ion exchange chromatography LD 50 lethality nonhuman nucleotide sequence peripheral blood mononuclear cell Plasmodium falciparum sequence alignment snake toxicity testing Amino Acid Sequence Animals Antiprotozoal Agents Bothrops Cell Survival Cells Cultured Crotalid Venoms Erythrocytes Humans Lethal Dose 50 Leukocytes Mononuclear Mice Molecular Sequence Data Phospholipases Plasmodium falciparum Sequence Alignment |
topic |
phospholipase phospholipase A2 snake venom acute toxicity amino acid sequence antimalarial activity antiplasmodial activity article bothrops asper cell fractionation controlled study cytotoxicity drug activity enzyme active site enzyme activity hemolysis IC 50 in vitro study ion exchange chromatography LD 50 lethality nonhuman nucleotide sequence peripheral blood mononuclear cell Plasmodium falciparum sequence alignment snake toxicity testing Amino Acid Sequence Animals Antiprotozoal Agents Bothrops Cell Survival Cells Cultured Crotalid Venoms Erythrocytes Humans Lethal Dose 50 Leukocytes Mononuclear Mice Molecular Sequence Data Phospholipases Plasmodium falciparum Sequence Alignment |
description |
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. © 2012 by the authors; licensee MDPI, Basel, Switzerland. |
publishDate |
2012 |
dc.date.issued.none.fl_str_mv |
2012 |
dc.date.accessioned.none.fl_str_mv |
2021-12-16T22:16:36Z |
dc.date.available.none.fl_str_mv |
2021-12-16T22:16:36Z |
dc.type.none.fl_str_mv |
Artículo |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
dc.type.coar.none.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.coarversion.none.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.driver.none.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.redcol.none.fl_str_mv |
http://purl.org/redcol/resource_type/ART |
dc.type.version.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
http://purl.org/coar/resource_type/c_6501 |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
https://doi.org/10.7149/OPA.51.3.50306 https://www.sciencedirect.com/science/article/abs/pii/S0034745014601463 |
dc.identifier.issn.spa.fl_str_mv |
20726651 |
dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/20.500.12494/42902 |
dc.identifier.bibliographicCitation.spa.fl_str_mv |
Castillo JCQ,Vargas LJ,Segura C,Gutiérrez JM,Pérez JCA. In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asper. Toxins (Basel). 2012. 4. (12):p. 1500-1516. . |
url |
https://doi.org/10.7149/OPA.51.3.50306 https://www.sciencedirect.com/science/article/abs/pii/S0034745014601463 https://hdl.handle.net/20.500.12494/42902 |
identifier_str_mv |
20726651 Castillo JCQ,Vargas LJ,Segura C,Gutiérrez JM,Pérez JCA. In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asper. Toxins (Basel). 2012. 4. (12):p. 1500-1516. . |
dc.relation.ispartofjournal.spa.fl_str_mv |
Toxins |
dc.rights.accessrights.none.fl_str_mv |
info:eu-repo/semantics/closedAccess |
dc.rights.coar.none.fl_str_mv |
http://purl.org/coar/access_right/c_14cb |
eu_rights_str_mv |
closedAccess |
rights_invalid_str_mv |
http://purl.org/coar/access_right/c_14cb |
dc.format.extent.spa.fl_str_mv |
1516-1500 |
dc.publisher.spa.fl_str_mv |
MDPI AG |
institution |
Universidad Cooperativa de Colombia |
repository.name.fl_str_mv |
Repositorio Institucional Universidad Cooperativa de Colombia |
repository.mail.fl_str_mv |
bdigital@metabiblioteca.com |
_version_ |
1814246621435658240 |