Caracterização do Pythium insidiosum por abordagem proteômica

Detalhes bibliográficos
Autor(a) principal: Chechi, Jéssica Luana [UNESP]
Data de Publicação: 2016
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://hdl.handle.net/11449/138145
Resumo: Pythiosis, whose etiologic agent is the oomycete Pythium insidiosum, is a disease that affects several animal species, including human, being more prevalent in horses. The disease has difficult diagnosis and treatment. Studies on protein characterization of P. insidiosum are scarce. The objective of this study was to determine the protein profile of Pythium insidiosum by mass spectrometry and bioinformatics strategies aiming to identify virulence factors. To this end, an extraction was standardized technique of total proteins of P. insidiosum, which were quantitated. From the protein extraction protocol it was obtained the profile of proteins expressed by the oomycete P. insidiosum through analysis by two-dimensional electrophoresis. The gels had 186 spots analyzed with molecular weight 12-89 kDa and an isoelectric point of 4-7, 103 of these were cut and sequenced. A total of 36 proteins were identified and grouped according to their functions, six of them were classified as proteins related to virulence - β 1,3 glucan synthase, Hsp 70, enolase, peroxiredoxin 2, G protein and the proteasome β unit. The results of this work will contribute to better understanding of the pathogenic mechanisms of P. insidiosum as well as for further studies in the therapeutic field and diagnosis.
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spelling Caracterização do Pythium insidiosum por abordagem proteômicaCharacterization of Pythium insidiosum by proteomics approachPythium insidiosumPythiosisProteomicsTwo-dimensional electrophoresisPythium insidiosumPitioseProteômicaEletroforese bidimensionalPythiosis, whose etiologic agent is the oomycete Pythium insidiosum, is a disease that affects several animal species, including human, being more prevalent in horses. The disease has difficult diagnosis and treatment. Studies on protein characterization of P. insidiosum are scarce. The objective of this study was to determine the protein profile of Pythium insidiosum by mass spectrometry and bioinformatics strategies aiming to identify virulence factors. To this end, an extraction was standardized technique of total proteins of P. insidiosum, which were quantitated. From the protein extraction protocol it was obtained the profile of proteins expressed by the oomycete P. insidiosum through analysis by two-dimensional electrophoresis. The gels had 186 spots analyzed with molecular weight 12-89 kDa and an isoelectric point of 4-7, 103 of these were cut and sequenced. A total of 36 proteins were identified and grouped according to their functions, six of them were classified as proteins related to virulence - β 1,3 glucan synthase, Hsp 70, enolase, peroxiredoxin 2, G protein and the proteasome β unit. The results of this work will contribute to better understanding of the pathogenic mechanisms of P. insidiosum as well as for further studies in the therapeutic field and diagnosis.A pitiose, cujo agente etiológico é o oomiceto Pythium insidiosum, é uma doença que acomete diversas espécies animais, incluindo-se a humana, sendo mais prevalente em equinos. A doença é de difícil diagnóstico e tratamento. Estudos sobre a caracterização proteica de P. insidiosum são escassos. O objetivo deste estudo foi determinar o perfil proteico de Pythium insidiosum por meio da estratégia espectrometria de massas e bioinformática, a fim de identificar fatores de virulência. Para isso, foi padronizada uma técnica de extração de proteínas totais de P. insidiosum, as quais foram quantificadas. A partir do protocolo de extração de proteínas foi obtido o perfil das proteínas expressas pelo oomiceto P. insidiosum por meio da análise por eletroforese bidimensional. Os géis analisados apresentaram 186 spots com massa molecular de 12 a 89 KDa, e ponto isoelétrico entre 4-7, destes 103 foram recortados e sequenciados. Um total de 36 proteínas foram identificadas e agrupadas de acordo com suas funções, seis delas foram classificadas como proteínas relacionadas à virulência - β 1,3 glucano sintetase, Hsp 70, enolase, peroxirredoxina 2, proteína G e proteassoma unidade β. Os resultados do presente trabalho contribuirão para o melhor entendimento dos mecanismos patogênicos de P. insidiosum, bem como para novos estudos no campo terapêutico e diagnóstico.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Universidade Estadual Paulista (Unesp)Bosco, Sandra de Moraes Gimenes [UNESP]Santos, Lucilene Delazari dos [UNESP]Universidade Estadual Paulista (Unesp)Chechi, Jéssica Luana [UNESP]2016-04-28T21:22:49Z2016-04-28T21:22:49Z2016-02-26info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfapplication/pdfhttp://hdl.handle.net/11449/13814500087030333004064080P33368404126695911porinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESP2023-11-01T06:13:02Zoai:repositorio.unesp.br:11449/138145Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-11-01T06:13:02Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Caracterização do Pythium insidiosum por abordagem proteômica
Characterization of Pythium insidiosum by proteomics approach
title Caracterização do Pythium insidiosum por abordagem proteômica
spellingShingle Caracterização do Pythium insidiosum por abordagem proteômica
Chechi, Jéssica Luana [UNESP]
Pythium insidiosum
Pythiosis
Proteomics
Two-dimensional electrophoresis
Pythium insidiosum
Pitiose
Proteômica
Eletroforese bidimensional
title_short Caracterização do Pythium insidiosum por abordagem proteômica
title_full Caracterização do Pythium insidiosum por abordagem proteômica
title_fullStr Caracterização do Pythium insidiosum por abordagem proteômica
title_full_unstemmed Caracterização do Pythium insidiosum por abordagem proteômica
title_sort Caracterização do Pythium insidiosum por abordagem proteômica
author Chechi, Jéssica Luana [UNESP]
author_facet Chechi, Jéssica Luana [UNESP]
author_role author
dc.contributor.none.fl_str_mv Bosco, Sandra de Moraes Gimenes [UNESP]
Santos, Lucilene Delazari dos [UNESP]
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Chechi, Jéssica Luana [UNESP]
dc.subject.por.fl_str_mv Pythium insidiosum
Pythiosis
Proteomics
Two-dimensional electrophoresis
Pythium insidiosum
Pitiose
Proteômica
Eletroforese bidimensional
topic Pythium insidiosum
Pythiosis
Proteomics
Two-dimensional electrophoresis
Pythium insidiosum
Pitiose
Proteômica
Eletroforese bidimensional
description Pythiosis, whose etiologic agent is the oomycete Pythium insidiosum, is a disease that affects several animal species, including human, being more prevalent in horses. The disease has difficult diagnosis and treatment. Studies on protein characterization of P. insidiosum are scarce. The objective of this study was to determine the protein profile of Pythium insidiosum by mass spectrometry and bioinformatics strategies aiming to identify virulence factors. To this end, an extraction was standardized technique of total proteins of P. insidiosum, which were quantitated. From the protein extraction protocol it was obtained the profile of proteins expressed by the oomycete P. insidiosum through analysis by two-dimensional electrophoresis. The gels had 186 spots analyzed with molecular weight 12-89 kDa and an isoelectric point of 4-7, 103 of these were cut and sequenced. A total of 36 proteins were identified and grouped according to their functions, six of them were classified as proteins related to virulence - β 1,3 glucan synthase, Hsp 70, enolase, peroxiredoxin 2, G protein and the proteasome β unit. The results of this work will contribute to better understanding of the pathogenic mechanisms of P. insidiosum as well as for further studies in the therapeutic field and diagnosis.
publishDate 2016
dc.date.none.fl_str_mv 2016-04-28T21:22:49Z
2016-04-28T21:22:49Z
2016-02-26
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://hdl.handle.net/11449/138145
000870303
33004064080P3
3368404126695911
url http://hdl.handle.net/11449/138145
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dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Universidade Estadual Paulista (Unesp)
publisher.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.source.none.fl_str_mv 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)
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