Caracterização do Pythium insidiosum por abordagem proteômica
Autor(a) principal: | |
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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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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 |
identifier_str_mv |
000870303 33004064080P3 3368404126695911 |
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) |
repository.mail.fl_str_mv |
|
_version_ |
1792961709279805440 |