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...

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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
id COOPER2_21c3cd9067b29acfef5062d18688e608
oai_identifier_str oai:repository.ucc.edu.co:20.500.12494/42902
network_acronym_str COOPER2
network_name_str Repositorio UCC
repository_id_str
spelling 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
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