Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom
ABSTRACT: Myotoxic phospholipases A2 (PLA2) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA2 (BaCol PLA2) was isolated from Colombian Bothrops asper venom using reverse-phase high performance liquid chromatography (RP-HPLC). BaCol...
- Autores:
-
Posada Arias, Silvia
Rey Suárez, Paola
Pereañez Jiménez, Jaime Andrés
Acosta Silva, Cristian Javier
Rojas López, Mauricio
Delazari dos Santos, Lucilene
Ferreira Jr, Rui Seabra
Núñez Rangel, Vitelbina
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2017
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/23806
- Acceso en línea:
- http://hdl.handle.net/10495/23806
- Palabra clave:
- Venenos de Serpiente
Snake Venoms
Edema
Miotoxicidad
Myotoxicity
Phospholipases A2
Bothrops asper
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by/2.5/co/
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oai:bibliotecadigital.udea.edu.co:10495/23806 |
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UDEA2 |
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Repositorio UdeA |
repository_id_str |
|
dc.title.spa.fl_str_mv |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
title |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
spellingShingle |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom Venenos de Serpiente Snake Venoms Edema Miotoxicidad Myotoxicity Phospholipases A2 Bothrops asper |
title_short |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
title_full |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
title_fullStr |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
title_full_unstemmed |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
title_sort |
Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venom |
dc.creator.fl_str_mv |
Posada Arias, Silvia Rey Suárez, Paola Pereañez Jiménez, Jaime Andrés Acosta Silva, Cristian Javier Rojas López, Mauricio Delazari dos Santos, Lucilene Ferreira Jr, Rui Seabra Núñez Rangel, Vitelbina |
dc.contributor.author.none.fl_str_mv |
Posada Arias, Silvia Rey Suárez, Paola Pereañez Jiménez, Jaime Andrés Acosta Silva, Cristian Javier Rojas López, Mauricio Delazari dos Santos, Lucilene Ferreira Jr, Rui Seabra Núñez Rangel, Vitelbina |
dc.subject.decs.none.fl_str_mv |
Venenos de Serpiente Snake Venoms Edema Miotoxicidad Myotoxicity |
topic |
Venenos de Serpiente Snake Venoms Edema Miotoxicidad Myotoxicity Phospholipases A2 Bothrops asper |
dc.subject.proposal.spa.fl_str_mv |
Phospholipases A2 Bothrops asper |
description |
ABSTRACT: Myotoxic phospholipases A2 (PLA2) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA2 (BaCol PLA2) was isolated from Colombian Bothrops asper venom using reverse-phase high performance liquid chromatography (RP-HPLC). BaCol PLA2 had a molecular mass of 14,180.69 Da (by mass spectrometry) and an isoelectric point of 4.4. The complete amino acid sequence was obtained by cDNA cloning (GenBank accession No. MF319968) and revealed a mature product of 124 amino acids with Asp at position 49. BaCol PLA2 showed structural homology with other acidic PLA2 isolated from Bothrops venoms, including a non-myotoxic PLA2 from Costa Rican B. asper. In vitro studies showed cell membrane damage without exposure of phosphatidylserine, an early apoptosis hallmark. BaCol PLA2 had high indirect hemolytic activity and moderate anticoagulant action. In mice, BaCol PLA2 caused marked edema and myotoxicity, the latter seen as an increase in plasma creatine kinase and histological damage to gastrocnemius muscle fibers that included vacuolization and hyalinization necrosis of the sarcoplasm. |
publishDate |
2017 |
dc.date.issued.none.fl_str_mv |
2017 |
dc.date.accessioned.none.fl_str_mv |
2021-11-05T23:08:31Z |
dc.date.available.none.fl_str_mv |
2021-11-05T23:08:31Z |
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/10495/23806 |
dc.identifier.doi.none.fl_str_mv |
10.3390/toxins9110342 |
dc.identifier.eissn.none.fl_str_mv |
2072-6651 |
url |
http://hdl.handle.net/10495/23806 |
identifier_str_mv |
10.3390/toxins9110342 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 |
15 |
dc.format.mimetype.spa.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
MDPI |
dc.publisher.group.spa.fl_str_mv |
Grupo de Inmunología Celular e Inmunogenética 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/10495/23806/2/license_rdf http://bibliotecadigital.udea.edu.co/bitstream/10495/23806/3/license.txt http://bibliotecadigital.udea.edu.co/bitstream/10495/23806/1/PosadaSilvia_2017_IsolationFunctionalAcidicMyotoxicPhospholipase.pdf |
bitstream.checksum.fl_str_mv |
1646d1f6b96dbbbc38035efc9239ac9c 8a4605be74aa9ea9d79846c1fba20a33 f9f0fd21c958bd710718e63da9226678 |
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_ |
1812173073938382848 |
spelling |
Posada Arias, SilviaRey Suárez, PaolaPereañez Jiménez, Jaime AndrésAcosta Silva, Cristian JavierRojas López, MauricioDelazari dos Santos, LucileneFerreira Jr, Rui SeabraNúñez Rangel, Vitelbina2021-11-05T23:08:31Z2021-11-05T23:08:31Z2017http://hdl.handle.net/10495/2380610.3390/toxins91103422072-6651ABSTRACT: Myotoxic phospholipases A2 (PLA2) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA2 (BaCol PLA2) was isolated from Colombian Bothrops asper venom using reverse-phase high performance liquid chromatography (RP-HPLC). BaCol PLA2 had a molecular mass of 14,180.69 Da (by mass spectrometry) and an isoelectric point of 4.4. The complete amino acid sequence was obtained by cDNA cloning (GenBank accession No. MF319968) and revealed a mature product of 124 amino acids with Asp at position 49. BaCol PLA2 showed structural homology with other acidic PLA2 isolated from Bothrops venoms, including a non-myotoxic PLA2 from Costa Rican B. asper. In vitro studies showed cell membrane damage without exposure of phosphatidylserine, an early apoptosis hallmark. BaCol PLA2 had high indirect hemolytic activity and moderate anticoagulant action. In mice, BaCol PLA2 caused marked edema and myotoxicity, the latter seen as an increase in plasma creatine kinase and histological damage to gastrocnemius muscle fibers that included vacuolization and hyalinization necrosis of the sarcoplasm.COL0014476COL000863915application/pdfengMDPIGrupo de Inmunología Celular e InmunogenéticaToxinología 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/Isolation and functional characterization of an acidic myotoxic phospholipase A2 from Colombian bothrops asper venomVenenos de SerpienteSnake VenomsEdemaMiotoxicidadMyotoxicityPhospholipases A2Bothrops asperToxinsToxins115911CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927http://bibliotecadigital.udea.edu.co/bitstream/10495/23806/2/license_rdf1646d1f6b96dbbbc38035efc9239ac9cMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/23806/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD53ORIGINALPosadaSilvia_2017_IsolationFunctionalAcidicMyotoxicPhospholipase.pdfPosadaSilvia_2017_IsolationFunctionalAcidicMyotoxicPhospholipase.pdfArtículo de investigaciónapplication/pdf4155936http://bibliotecadigital.udea.edu.co/bitstream/10495/23806/1/PosadaSilvia_2017_IsolationFunctionalAcidicMyotoxicPhospholipase.pdff9f0fd21c958bd710718e63da9226678MD5110495/23806oai:bibliotecadigital.udea.edu.co:10495/238062021-11-05 18:08:31.986Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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 |