Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants

Autores
Bustillo, Soledad; Fernández, Julián; Chaves-Araya, Stephanie; Angulo, Yamileth; Leiva, Laura C.; Lomonte, Bruno
Año de publicación
2019
Idioma
español castellano
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Bustillo, Soledad. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.
Fil: Fernández, Julián. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Fil: Stephanie Chaves-Araya. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Fil: Yamileth Angulo. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Fil: Laura C. Leiva.Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.
Fil: Bruno Lomonte. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically relevant viperid in Northeastern Argentina. The venom of this species causes local tissue damage characterized by myonecrosis, hemorrhage, blistering, and edema. In the present study, two basic phospholipases A2 (PLA2-I and PLA2-II) were isolated from this venom, and their pathological effects upon murine skeletal muscle and myogenic cells in culture were analyzed. Partial amino acid sequencing showed that PLA2-I and PLA2-II are Asp49 and Lys49 PLA2s, respectively. In agreement with this, PLA2-I showed PLA2 activity, whereas PLA2-II did not. Functional assays revealed differences in their myotoxicity, cytotoxicity, and anti-adhesion activity, and in the ability to inhibit cell migration, all of which were greater for the Lys49 variant. Native electrophoresis showed that PLA2-I was less basic than PLA2-II. The two proteins act synergistically to affect the integrity of C2C12 myogenic cells, providing a further example of the concerted action of coexisting snake venom components. PLA2-I and PLA2-II, together with additional basic PLA2s revealed by RP-HPLC, probably play an important role in myonecrosis after envenomation by B. diporus.
Fuente
Toxicon, 2019, vol. 168, p. 113-121.
Materia
Snake venom
Bothrops diporus
Phospholipase A2
Synergism
Myotoxicity
Cytotoxicity
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
Institución
Universidad Nacional del Nordeste
OAI Identificador
oai:repositorio.unne.edu.ar:123456789/58045
Acceder
id RIUNNE_d1850db31630666e598756e8aa9c46c9
oai_identifier_str oai:repositorio.unne.edu.ar:123456789/58045
network_acronym_str RIUNNE
repository_id_str 4871
network_name_str Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
spelling Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variantsBustillo, SoledadFernández, JuliánChaves-Araya, StephanieAngulo, YamilethLeiva, Laura C.Lomonte, BrunoSnake venomBothrops diporusPhospholipase A2SynergismMyotoxicityCytotoxicityFil: Bustillo, Soledad. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.Fil: Fernández, Julián. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.Fil: Stephanie Chaves-Araya. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.Fil: Yamileth Angulo. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.Fil: Laura C. Leiva.Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.Fil: Bruno Lomonte. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically relevant viperid in Northeastern Argentina. The venom of this species causes local tissue damage characterized by myonecrosis, hemorrhage, blistering, and edema. In the present study, two basic phospholipases A2 (PLA2-I and PLA2-II) were isolated from this venom, and their pathological effects upon murine skeletal muscle and myogenic cells in culture were analyzed. Partial amino acid sequencing showed that PLA2-I and PLA2-II are Asp49 and Lys49 PLA2s, respectively. In agreement with this, PLA2-I showed PLA2 activity, whereas PLA2-II did not. Functional assays revealed differences in their myotoxicity, cytotoxicity, and anti-adhesion activity, and in the ability to inhibit cell migration, all of which were greater for the Lys49 variant. Native electrophoresis showed that PLA2-I was less basic than PLA2-II. The two proteins act synergistically to affect the integrity of C2C12 myogenic cells, providing a further example of the concerted action of coexisting snake venom components. PLA2-I and PLA2-II, together with additional basic PLA2s revealed by RP-HPLC, probably play an important role in myonecrosis after envenomation by B. diporus.Elsevier Ltd.2019-10-16info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfp. 113-121application/pdfBustillo, Soledad, et. al, 2019. Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants. Toxicon: Países Bajos, Elsevier Ltd., p. 113-121, ISSN 0041-0101.0041-0101http://repositorio.unne.edu.ar/handle/123456789/58045Toxicon, 2019, vol. 168, p. 113-121.reponame:Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)instname:Universidad Nacional del Nordestespahttps://doi.org/10.1016/j.toxicon.2019.07.004info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/2.5/ar/Atribución-NoComercial-SinDerivadas 2.5 Argentina2025-10-16T10:07:44Zoai:repositorio.unne.edu.ar:123456789/58045instacron:UNNEInstitucionalhttp://repositorio.unne.edu.ar/Universidad públicaNo correspondehttp://repositorio.unne.edu.ar/oaiososa@bib.unne.edu.ar;sergio.alegria@unne.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:48712025-10-16 10:07:44.307Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) - Universidad Nacional del Nordestefalse
dc.title.none.fl_str_mv Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
title Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
spellingShingle Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
Bustillo, Soledad
Snake venom
Bothrops diporus
Phospholipase A2
Synergism
Myotoxicity
Cytotoxicity
title_short Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
title_full Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
title_fullStr Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
title_full_unstemmed Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
title_sort Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants
dc.creator.none.fl_str_mv Bustillo, Soledad
Fernández, Julián
Chaves-Araya, Stephanie
Angulo, Yamileth
Leiva, Laura C.
Lomonte, Bruno
author Bustillo, Soledad
author_facet Bustillo, Soledad
Fernández, Julián
Chaves-Araya, Stephanie
Angulo, Yamileth
Leiva, Laura C.
Lomonte, Bruno
author_role author
author2 Fernández, Julián
Chaves-Araya, Stephanie
Angulo, Yamileth
Leiva, Laura C.
Lomonte, Bruno
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Snake venom
Bothrops diporus
Phospholipase A2
Synergism
Myotoxicity
Cytotoxicity
topic Snake venom
Bothrops diporus
Phospholipase A2
Synergism
Myotoxicity
Cytotoxicity
dc.description.none.fl_txt_mv Fil: Bustillo, Soledad. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.
Fil: Fernández, Julián. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Fil: Stephanie Chaves-Araya. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Fil: Yamileth Angulo. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Fil: Laura C. Leiva.Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.
Fil: Bruno Lomonte. Universidad de Costa Rica. Facultad de Microbiología; Costa Rica.
Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically relevant viperid in Northeastern Argentina. The venom of this species causes local tissue damage characterized by myonecrosis, hemorrhage, blistering, and edema. In the present study, two basic phospholipases A2 (PLA2-I and PLA2-II) were isolated from this venom, and their pathological effects upon murine skeletal muscle and myogenic cells in culture were analyzed. Partial amino acid sequencing showed that PLA2-I and PLA2-II are Asp49 and Lys49 PLA2s, respectively. In agreement with this, PLA2-I showed PLA2 activity, whereas PLA2-II did not. Functional assays revealed differences in their myotoxicity, cytotoxicity, and anti-adhesion activity, and in the ability to inhibit cell migration, all of which were greater for the Lys49 variant. Native electrophoresis showed that PLA2-I was less basic than PLA2-II. The two proteins act synergistically to affect the integrity of C2C12 myogenic cells, providing a further example of the concerted action of coexisting snake venom components. PLA2-I and PLA2-II, together with additional basic PLA2s revealed by RP-HPLC, probably play an important role in myonecrosis after envenomation by B. diporus.
description Fil: Bustillo, Soledad. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura.; Argentina.
publishDate 2019
dc.date.none.fl_str_mv 2019-10-16
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv Bustillo, Soledad, et. al, 2019. Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants. Toxicon: Países Bajos, Elsevier Ltd., p. 113-121, ISSN 0041-0101.
0041-0101
http://repositorio.unne.edu.ar/handle/123456789/58045
identifier_str_mv Bustillo, Soledad, et. al, 2019. Isolation of two basic phospholipases A2 from Bothrops diporus snake venom : Comparative characterization and synergism between Asp49 and Lys49 variants. Toxicon: Países Bajos, Elsevier Ltd., p. 113-121, ISSN 0041-0101.
0041-0101
url http://repositorio.unne.edu.ar/handle/123456789/58045
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv https://doi.org/10.1016/j.toxicon.2019.07.004
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Atribución-NoComercial-SinDerivadas 2.5 Argentina
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Atribución-NoComercial-SinDerivadas 2.5 Argentina
dc.format.none.fl_str_mv application/pdf
p. 113-121
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ltd.
publisher.none.fl_str_mv Elsevier Ltd.
dc.source.none.fl_str_mv Toxicon, 2019, vol. 168, p. 113-121.
reponame:Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
instname:Universidad Nacional del Nordeste
reponame_str Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
collection Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
instname_str Universidad Nacional del Nordeste
repository.name.fl_str_mv Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) - Universidad Nacional del Nordeste
repository.mail.fl_str_mv ososa@bib.unne.edu.ar;sergio.alegria@unne.edu.ar
_version_ 1846146012160196608
score 12.712165

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