Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom

Detalhes bibliográficos
Autor(a) principal: Almeida, José Rafael de, 1989-
Data de Publicação: 2016
Outros Autores: Resende, Letícia Monteiro de, 1990-, Marangoni, Sergio, 1951-
Tipo de documento: Artigo
Título da fonte: Repositório da Produção Científica e Intelectual da Unicamp
Texto Completo: https://hdl.handle.net/20.500.12733/8783
Resumo: Agradecimentos: The authors express their gratitude to CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior) and CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnologico), FAPESP (Fundação de Amparo a Pesquisa do Estado de São Paulo) for financial support
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spelling Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venomVenenos de serpentesSnake venomsPhospholipase A2MyotoxinCrotalus oreganus lutosusBiological activitiesArtigo originalAgradecimentos: The authors express their gratitude to CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior) and CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnologico), FAPESP (Fundação de Amparo a Pesquisa do Estado de São Paulo) for financial supportAbstract: Commonly, phospholipases A2 (PLA2s) play key roles in the pathogenesis of the local tissue damage characteristic of crotaline and viperine snake envenomations. Crotalus oreganus lutosus snake venom has not been extensively studied; therefore, the characterization of its components represents a valuable biotechnological tool for studying pathophysiological processes of envenoming and for gaining a deeper understanding of its biological effects. In this study, for the first time, a basic PLA2 myotoxin, ColTx-I, was purified from C. o. lutosus through two chromatographic steps. ColTx-I is monomeric with calculated molecular mass weight (Mw) of 14,145 Da and a primary structure closely related to basic PLA2s from viperid venoms. The pure enzyme has a specific activity of 15.87 ± 0.65 nmol/min/mg at optimal conditions (pH 8.0 and 37 °C). ColTx-I activity was found to be dependent on Ca2+, as its substitution by other ionic species as well as the addition of chelating agents significantly reduced its phospholipase activity. In vivo, ColTx-I triggered dose-dependent inflammatory responses, measured using the paw edema model, with an increase in IL-6 levels, systemic and local myotoxicity, characterized by elevated plasma creatine kinase activity. ColTx-I induced a complex series of degenerative events associated with edema, inflammatory infiltrate and skeletal muscle necrosis. These biochemical and functional results suggest that ColTx-I, a myotoxic and inflammatory mediator, plays a relevant role in C. o. lutosus envenomation. Thus, detailed studies on its mechanism of action, such as evaluating the synergism between ColTx-I and other venom components may reveal targets for the development of more specific and effective therapiesCONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPFechadoUNIVERSIDADE ESTADUAL DE CAMPINASAlmeida, José Rafael de, 1989-Resende, Letícia Monteiro de, 1990-Marangoni, Sergio, 1951-2016info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.12733/8783ALMEIDA, José Rafael de; RESENDE, Letícia Monteiro de; MARANGONI, Sergio. Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom. Toxicon: an interdisciplinary journal on the toxins derived from animals, plants and microorganisms. Oxford : Elsevier, 2016. Vol. 117 (July, 2016), p. 1-12. Disponível em: https://hdl.handle.net/20.500.12733/8783. Acesso em: 24 mai. 2023.Inglêshttps://repositorio.unicamp.br/acervo/detalhe/1168292reponame:Repositório da Produção Científica e Intelectual da Unicampinstname:Universidade Estadual de Campinas (UNICAMP)instacron:UNICAMPinfo:eu-repo/semantics/openAccess2023-04-25T17:29:00Zoai:https://www.repositorio.unicamp.br/:1168292Repositório InstitucionalPUBhttp://repositorio.unicamp.br/oai/requestreposip@unicamp.bropendoar:2023-04-25T17:29Repositório da Produção Científica e Intelectual da Unicamp - Universidade Estadual de Campinas (UNICAMP)false
dc.title.none.fl_str_mv Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
title Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
spellingShingle Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
Almeida, José Rafael de, 1989-
Venenos de serpentes
Snake venoms
Phospholipase A2
Myotoxin
Crotalus oreganus lutosus
Biological activities
Artigo original
title_short Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
title_full Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
title_fullStr Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
title_full_unstemmed Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
title_sort Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom
author Almeida, José Rafael de, 1989-
author_facet Almeida, José Rafael de, 1989-
Resende, Letícia Monteiro de, 1990-
Marangoni, Sergio, 1951-
author_role author
author2 Resende, Letícia Monteiro de, 1990-
Marangoni, Sergio, 1951-
author2_role author
author
dc.contributor.none.fl_str_mv UNIVERSIDADE ESTADUAL DE CAMPINAS
dc.contributor.author.fl_str_mv Almeida, José Rafael de, 1989-
Resende, Letícia Monteiro de, 1990-
Marangoni, Sergio, 1951-
dc.subject.por.fl_str_mv Venenos de serpentes
Snake venoms
Phospholipase A2
Myotoxin
Crotalus oreganus lutosus
Biological activities
Artigo original
topic Venenos de serpentes
Snake venoms
Phospholipase A2
Myotoxin
Crotalus oreganus lutosus
Biological activities
Artigo original
description Agradecimentos: The authors express their gratitude to CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior) and CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnologico), FAPESP (Fundação de Amparo a Pesquisa do Estado de São Paulo) for financial support
publishDate 2016
dc.date.none.fl_str_mv 2016
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 https://hdl.handle.net/20.500.12733/8783
ALMEIDA, José Rafael de; RESENDE, Letícia Monteiro de; MARANGONI, Sergio. Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom. Toxicon: an interdisciplinary journal on the toxins derived from animals, plants and microorganisms. Oxford : Elsevier, 2016. Vol. 117 (July, 2016), p. 1-12. Disponível em: https://hdl.handle.net/20.500.12733/8783. Acesso em: 24 mai. 2023.
url https://hdl.handle.net/20.500.12733/8783
identifier_str_mv ALMEIDA, José Rafael de; RESENDE, Letícia Monteiro de; MARANGONI, Sergio. Biochemical and functional studies of ColTx-I, a new myotoxic phospholipase A2 isolated from crotalus oreganus lutosus (great basin rattlesnake) snake venom. Toxicon: an interdisciplinary journal on the toxins derived from animals, plants and microorganisms. Oxford : Elsevier, 2016. Vol. 117 (July, 2016), p. 1-12. Disponível em: https://hdl.handle.net/20.500.12733/8783. Acesso em: 24 mai. 2023.
dc.language.iso.fl_str_mv Inglês
language_invalid_str_mv Inglês
dc.relation.none.fl_str_mv https://repositorio.unicamp.br/acervo/detalhe/1168292
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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instname:Universidade Estadual de Campinas (UNICAMP)
instacron:UNICAMP
instname_str Universidade Estadual de Campinas (UNICAMP)
instacron_str UNICAMP
institution UNICAMP
reponame_str Repositório da Produção Científica e Intelectual da Unicamp
collection Repositório da Produção Científica e Intelectual da Unicamp
repository.name.fl_str_mv Repositório da Produção Científica e Intelectual da Unicamp - Universidade Estadual de Campinas (UNICAMP)
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