Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)

Detalhes bibliográficos
Autor(a) principal: Higa, André Miasato
Data de Publicação: 2008
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da Universidade do Estado do Amazonas (UEA)
Texto Completo: http://repositorioinstitucional.uea.edu.br//handle/riuea/2264
Resumo: Scorpion venoms show a complex mixture of neurotoxic protein and peptides wich causes toxic effects in mammals and insects. Brotheas amazonicus scorpion is an abundant specimen in Manaus rural areas and feeds of insects. Clinical evidences suggest very low toxicity from his venom for humans. In this work we are introducing results about chemical composition, biological and immunological properties of toxins from B. amazonicus venom. Proteomic methods (gradient SDS PAGE, tris-tricine SDS-PAGE and 2D) showed constituents 7 and 80 kDa molecular mass range, mainly toxins with Ip 4 – 7 range. The venom showed phospholipasic A2 activity that was not inhibited by antiscorpion, antiaracnide, antilonomia, antielapidic and antiophydian antivenoms, suggesting exclusive toxin epitopes of the specie. Venom also showed serineproteases toxins with 70 kDa molecular mass, wich degradates Aα and Bβ bovine fibrinogen chain, and without fibrin coagulation. Serineproteinase activity was inhibited by antiscorpion antivenom. Bleeding and blood incoagulation was not detected in mice after intravenous venom injection. Lethal activity with 100 µg of venom was not observed in mice after intracranial and intravenous venom injection. Formalin and acetic acid test to pain induction showed that, in nervous central system level, venom toxins have a potent analgesic activity of pain of inflammatory origin but in minor level to pain of neurogenic origin, and euphoria signals were not observed. Western blotting test showed antigen-antibody interaction between B. amazonicus venom toxins and IgG antibody antiscorpionic and antiaracnide antivenoms, but both antivenoms were not detected at 7kDa venom toxins. Venom has very low toxicity in mice (mammals), and a potent analgesic activity of toxins from B. amazonicus venom suggest a high biotechnological application to development of analgesic drugs.
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spelling Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)VenenoEscorpiãoBrotheas amazonicus scorpionBiotecnologiaScorpion venoms show a complex mixture of neurotoxic protein and peptides wich causes toxic effects in mammals and insects. Brotheas amazonicus scorpion is an abundant specimen in Manaus rural areas and feeds of insects. Clinical evidences suggest very low toxicity from his venom for humans. In this work we are introducing results about chemical composition, biological and immunological properties of toxins from B. amazonicus venom. Proteomic methods (gradient SDS PAGE, tris-tricine SDS-PAGE and 2D) showed constituents 7 and 80 kDa molecular mass range, mainly toxins with Ip 4 – 7 range. The venom showed phospholipasic A2 activity that was not inhibited by antiscorpion, antiaracnide, antilonomia, antielapidic and antiophydian antivenoms, suggesting exclusive toxin epitopes of the specie. Venom also showed serineproteases toxins with 70 kDa molecular mass, wich degradates Aα and Bβ bovine fibrinogen chain, and without fibrin coagulation. Serineproteinase activity was inhibited by antiscorpion antivenom. Bleeding and blood incoagulation was not detected in mice after intravenous venom injection. Lethal activity with 100 µg of venom was not observed in mice after intracranial and intravenous venom injection. Formalin and acetic acid test to pain induction showed that, in nervous central system level, venom toxins have a potent analgesic activity of pain of inflammatory origin but in minor level to pain of neurogenic origin, and euphoria signals were not observed. Western blotting test showed antigen-antibody interaction between B. amazonicus venom toxins and IgG antibody antiscorpionic and antiaracnide antivenoms, but both antivenoms were not detected at 7kDa venom toxins. Venom has very low toxicity in mice (mammals), and a potent analgesic activity of toxins from B. amazonicus venom suggest a high biotechnological application to development of analgesic drugs.Venenos de escorpiões apresentam uma mistura complexa de proteínas e peptídeos neurotóxicos, que são os responsáveis pelos efeitos tóxicos nos mamíferos e insetos. O escorpião Brotheas amazonicus é uma espécie muito comum nas florestas das áreas rurais de Manaus, alimentando-se de insetos, mas evidencias clínicas sugerem baixa toxicidade de suas toxinas em caso de acidente em humanos. Neste trabalho estamos apresentando dados sobre a composição química, propriedades biológicas e imunológicas das toxinas do veneno de B. amazonicus. Técnicas proteômicas (SDS-PAGE gradiente, SDS-PAGE tris-tricina e 2D) indicam constituintes com massas moleculares de 7 a 80 kDa, principalmente toxinas com pI de 4 a 7. No veneno foi detectada atividade fosfolipásica A2 que não foi inibida pelos antivenenos antiescorpiônico, antiaracnídeo, antielapídico, antilonomia e antiofídico, sugerindo epitopos próprios da espécie. Foi detectada a atividade de serinoproteases com massa molecular de 70 kDa que degrada as cadeias Aα e Bβ do fibrinogênio bovino sem produzir coágulo de fibrina. A atividade da serinoprotease foi inibida pelo soro antiescorpiônico. Quando injetado intravenosamente em camundongos, o veneno não produz hemorragia e o sangue não se torna incoagulável. Com a dose máxima testada (100 µg), via intracranial e endovenosa, não foi observada letalidade em camundongos. Os testes de indução da dor com a formalina e o ácido acético indicam, ao nível do sistema nervoso central, uma potente atividade inibitória do veneno sobre a dor de origem inflamatória e em menor grau sobre a dor de origem neurogênica, e não foram observados sintomas de euforia. Análises por Western Blotting demostraram a formação de complexo antígeno-anticorpos entre as toxinas de B. amazonicus e as IgG dos antivenenos antiescorpiônico e antiaracnídeo, mas nenhum desses antivenenos reconheceu as toxinas de 7 kDa do veneno. A baixa toxicidade do veneno e o potente efeito analgésico das toxinas do veneno de B. amazonicus sugerem um grande potencial biotecnológico para o desenvolvimento de novas drogas analgésicas.Universidade do Estado do AmazonasBrasilPrograma de Pós-Graduação em Biotecnologia e Recursos NaturaisUEALópez-Lozano, Jorge Luishttp://lattes.cnpq.br/6251525203051399López-Lozano, Jorge Luishttp://lattes.cnpq.br/6251525203051399Carvalho, Rosany PicollotoAndrade, Edmar Vaz dehttp://lattes.cnpq.br/4691893433367918Higa, André Miasato2020-03-132020-03-12T15:09:24Z2008-12-302020-03-12T15:09:24Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://repositorioinstitucional.uea.edu.br//handle/riuea/2264porABBOT, Frances V.; FRANKLIN, K. B. J.; WESTBROOK, R. F. The formalin test: scoring properties of the first and second phases of the pain response in rats. Pain, n. 60, p. 91-102, 1995. AIRES, M. de M.; BALDO, M. V. et al. Fisiologia. Pag. 224-225. 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dc.title.none.fl_str_mv Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
title Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
spellingShingle Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
Higa, André Miasato
Veneno
Escorpião
Brotheas amazonicus scorpion
Biotecnologia
title_short Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
title_full Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
title_fullStr Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
title_full_unstemmed Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
title_sort Propriedades moleculares, atividades biológicas e imunológicas das toxinas protéicas do veneno de Brotheas amazonicus Lourenço, 1988 (Chactidae, Scorpiones)
author Higa, André Miasato
author_facet Higa, André Miasato
author_role author
dc.contributor.none.fl_str_mv López-Lozano, Jorge Luis
http://lattes.cnpq.br/6251525203051399
López-Lozano, Jorge Luis
http://lattes.cnpq.br/6251525203051399
Carvalho, Rosany Picolloto
Andrade, Edmar Vaz de
http://lattes.cnpq.br/4691893433367918
dc.contributor.author.fl_str_mv Higa, André Miasato
dc.subject.por.fl_str_mv Veneno
Escorpião
Brotheas amazonicus scorpion
Biotecnologia
topic Veneno
Escorpião
Brotheas amazonicus scorpion
Biotecnologia
description Scorpion venoms show a complex mixture of neurotoxic protein and peptides wich causes toxic effects in mammals and insects. Brotheas amazonicus scorpion is an abundant specimen in Manaus rural areas and feeds of insects. Clinical evidences suggest very low toxicity from his venom for humans. In this work we are introducing results about chemical composition, biological and immunological properties of toxins from B. amazonicus venom. Proteomic methods (gradient SDS PAGE, tris-tricine SDS-PAGE and 2D) showed constituents 7 and 80 kDa molecular mass range, mainly toxins with Ip 4 – 7 range. The venom showed phospholipasic A2 activity that was not inhibited by antiscorpion, antiaracnide, antilonomia, antielapidic and antiophydian antivenoms, suggesting exclusive toxin epitopes of the specie. Venom also showed serineproteases toxins with 70 kDa molecular mass, wich degradates Aα and Bβ bovine fibrinogen chain, and without fibrin coagulation. Serineproteinase activity was inhibited by antiscorpion antivenom. Bleeding and blood incoagulation was not detected in mice after intravenous venom injection. Lethal activity with 100 µg of venom was not observed in mice after intracranial and intravenous venom injection. Formalin and acetic acid test to pain induction showed that, in nervous central system level, venom toxins have a potent analgesic activity of pain of inflammatory origin but in minor level to pain of neurogenic origin, and euphoria signals were not observed. Western blotting test showed antigen-antibody interaction between B. amazonicus venom toxins and IgG antibody antiscorpionic and antiaracnide antivenoms, but both antivenoms were not detected at 7kDa venom toxins. Venom has very low toxicity in mice (mammals), and a potent analgesic activity of toxins from B. amazonicus venom suggest a high biotechnological application to development of analgesic drugs.
publishDate 2008
dc.date.none.fl_str_mv 2008-12-30
2020-03-13
2020-03-12T15:09:24Z
2020-03-12T15:09:24Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://repositorioinstitucional.uea.edu.br//handle/riuea/2264
url http://repositorioinstitucional.uea.edu.br//handle/riuea/2264
dc.language.iso.fl_str_mv por
language por
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dc.rights.driver.fl_str_mv Atribuição-NãoComercial-SemDerivados 3.0 Brasil
http://creativecommons.org/licenses/by-nc-nd/3.0/br/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Atribuição-NãoComercial-SemDerivados 3.0 Brasil
http://creativecommons.org/licenses/by-nc-nd/3.0/br/
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Universidade do Estado do Amazonas
Brasil
Programa de Pós-Graduação em Biotecnologia e Recursos Naturais
UEA
publisher.none.fl_str_mv Universidade do Estado do Amazonas
Brasil
Programa de Pós-Graduação em Biotecnologia e Recursos Naturais
UEA
dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade do Estado do Amazonas (UEA)
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reponame_str Repositório Institucional da Universidade do Estado do Amazonas (UEA)
collection Repositório Institucional da Universidade do Estado do Amazonas (UEA)
repository.name.fl_str_mv Repositório Institucional da Universidade do Estado do Amazonas (UEA) - Universidade do Estado do Amazonas (UEA)
repository.mail.fl_str_mv bibliotecacentral@uea.edu.br
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