Isolation and Functional Characterization of an Acidic Myotoxic Phospholipase A₂ from Colombian Bothrops asper Venom
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.3390/toxins9110342 http://hdl.handle.net/11449/177154 |
Resumo: | 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. |
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Isolation and Functional Characterization of an Acidic Myotoxic Phospholipase A₂ from Colombian Bothrops asper Venomacidic myotoxic phospholipase A2Bothrops asperedemamyotoxicitysnake venomMyotoxic 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.Programa de Ofidismo y Escorpionismo, Universidad de Antioquia, Medellín 050010, ColombiaResearch Group in Veterinary Medicine GIVET, School of Veterinary Medicine, Corporación Universitaria Lasallista, Caldas-Antioquia 055440, ColombiaPrograma de Ofidismo y Escorpionismo, Universidad de Antioquia, Medellín 050010, Colombia. ofidpa@gmail.comPrograma de Ofidismo y Escorpionismo, Universidad de Antioquia, Medellín 050010, Colombia. andrespj20@gmail.comGrupo de Inmunología Celular e Inmunogenética (GICIG), Universidad de Antioquia, Medellín 050010, ColombiaCenter for the Study of Venoms and Venomous Animals (CEVAP), Universidad Estadual Paulista (UNESP) and Graduate Program in Tropical Diseases, Botucatu Medical School (FMB), Botucatu, São Paulo 18610-307, BrazilCenter for the Study of Venoms and Venomous Animals (CEVAP), Universidad Estadual Paulista (UNESP) and Graduate Program in Tropical Diseases, Botucatu Medical School (FMB), Botucatu, São Paulo 18610-307, Brazil. rui.ead@gmail.comEscuela de Microbiología, Universidad de Antioquia, Medellín 050010, ColombiaUniversidade Estadual Paulista (Unesp)Posada Arias, SilviaRey-Suárez, PaolaPereáñez J, AndrésAcosta, CristianRojas, MauricioDelazari Dos Santos, LucileneFerreira, Rui SeabraNúñez, Vitelbina2018-12-11T17:24:15Z2018-12-11T17:24:15Z2017-10-26info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.3390/toxins9110342Toxins, v. 9, n. 11, 2017.2072-6651http://hdl.handle.net/11449/17715410.3390/toxins91103422-s2.0-850490818072-s2.0-85049081807.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengToxins0,955info:eu-repo/semantics/openAccess2024-04-11T15:28:16Zoai:repositorio.unesp.br:11449/177154Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T14:38:09.030699Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.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 Posada Arias, Silvia acidic myotoxic phospholipase A2 Bothrops asper edema myotoxicity snake venom |
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 |
author |
Posada Arias, Silvia |
author_facet |
Posada Arias, Silvia Rey-Suárez, Paola Pereáñez J, Andrés Acosta, Cristian Rojas, Mauricio Delazari Dos Santos, Lucilene Ferreira, Rui Seabra Núñez, Vitelbina |
author_role |
author |
author2 |
Rey-Suárez, Paola Pereáñez J, Andrés Acosta, Cristian Rojas, Mauricio Delazari Dos Santos, Lucilene Ferreira, Rui Seabra Núñez, Vitelbina |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Posada Arias, Silvia Rey-Suárez, Paola Pereáñez J, Andrés Acosta, Cristian Rojas, Mauricio Delazari Dos Santos, Lucilene Ferreira, Rui Seabra Núñez, Vitelbina |
dc.subject.por.fl_str_mv |
acidic myotoxic phospholipase A2 Bothrops asper edema myotoxicity snake venom |
topic |
acidic myotoxic phospholipase A2 Bothrops asper edema myotoxicity snake venom |
description |
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.none.fl_str_mv |
2017-10-26 2018-12-11T17:24:15Z 2018-12-11T17:24:15Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.3390/toxins9110342 Toxins, v. 9, n. 11, 2017. 2072-6651 http://hdl.handle.net/11449/177154 10.3390/toxins9110342 2-s2.0-85049081807 2-s2.0-85049081807.pdf |
url |
http://dx.doi.org/10.3390/toxins9110342 http://hdl.handle.net/11449/177154 |
identifier_str_mv |
Toxins, v. 9, n. 11, 2017. 2072-6651 10.3390/toxins9110342 2-s2.0-85049081807 2-s2.0-85049081807.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Toxins 0,955 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1808128391320174592 |