Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina
Autor(a) principal: | |
---|---|
Data de Publicação: | 2008 |
Tipo de documento: | Tese |
Idioma: | por |
Título da fonte: | Repositório Institucional da UFG |
Texto Completo: | http://repositorio.bc.ufg.br/tede/handle/tede/4003 |
Resumo: | Paracoccidioides brasiliensis, an important human pathogen causative of paracoccidioidomycosis (PCM), a systemic mycosis with broad distribution in Latin America. Adhesion to and invasion of host cells are essential steps involved in the infection and dissemination of pathogens. Furthermore, pathogens use their surface molecules to bind to host extracellular matrix components to establish infection. An adhesin of P. brasiliensiswas isolated from two dimensional electrophoresis and characterized. Peptides obtained by partial sequencing of the isolated protein, which presenteda molecular mass of 29 kDa and pI 5.8, were subjected to sequence analysis of their amino acids, that revealed strong homology to triose phosphate isomerase (TPI) from several sources. The complete cDNA and gene encoding TPI of P. brasiliensis (PbTPI) were characterized and both contained an open reading frame predicted to encode a 249 amino acid protein that presented all the peptides characterized in the native PbTPI. The complete coding PbTPI cDNA was cloned and over expressed in Escherichia coli host. The purified recombinant TPI was used to produce polyclonal antibody in rabbit. By immunoelectron microscopy and Western blot analysis, TPI was detected in the cell wall and the cytoplasm of the yeast phase of P. brasiliensis. The expression of PbTPI was analyzed in transition from mycelia to yeast phase. The native PbTPI is preferentially expressed in the yeast parasitic phase of P. brasiliensis. The recombinant PbTPI was found to bind to laminin and fibronectin in ligand far-Western blot assays. TPI binds preferentially to laminin, as determined by peptide inhibition assays. Of special note, the treatment of P. brasiliensisyeast cells with anti-PbTPI polyclonal antibody and the incubation of pneumocytes and VERO cells with the recombinant protein promoted inhibition of adherence and internalization of P. brasiliensisto those in vitrocultured cells. These observations indicate that TPI could be contribute to the adhesion of the microorganism to host tissues and to the dissemination of infection. |
id |
UFG-2_5ab37b7bf9b535c9a4ff2b5d0ffb3775 |
---|---|
oai_identifier_str |
oai:repositorio.bc.ufg.br:tede/4003 |
network_acronym_str |
UFG-2 |
network_name_str |
Repositório Institucional da UFG |
repository_id_str |
|
spelling |
Soares, Célia Maria de Almeidahttp://lattes.cnpq.br/8539946335852637Ulhoa, Cirano JoséCampos, Ivan Torres NicolauIzaac, Silvia Maria SalemGiannini, Maria José Soares MendesSoares, Célia Maria de Almeidahttp://lattes.cnpq.br/1549739934623931Pereira, Luiz Augusto2015-01-29T18:42:52Z2008-09-04PEREIRA, Luiz Augusto. Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina. 2008. 79 f. Tese (Doutorado em Medicina Tropical e Saúde Publica) - Universidade Federal de Goiás, Goiânia, 2008.http://repositorio.bc.ufg.br/tede/handle/tede/4003ark:/38995/0013000002w5gParacoccidioides brasiliensis, an important human pathogen causative of paracoccidioidomycosis (PCM), a systemic mycosis with broad distribution in Latin America. Adhesion to and invasion of host cells are essential steps involved in the infection and dissemination of pathogens. Furthermore, pathogens use their surface molecules to bind to host extracellular matrix components to establish infection. An adhesin of P. brasiliensiswas isolated from two dimensional electrophoresis and characterized. Peptides obtained by partial sequencing of the isolated protein, which presenteda molecular mass of 29 kDa and pI 5.8, were subjected to sequence analysis of their amino acids, that revealed strong homology to triose phosphate isomerase (TPI) from several sources. The complete cDNA and gene encoding TPI of P. brasiliensis (PbTPI) were characterized and both contained an open reading frame predicted to encode a 249 amino acid protein that presented all the peptides characterized in the native PbTPI. The complete coding PbTPI cDNA was cloned and over expressed in Escherichia coli host. The purified recombinant TPI was used to produce polyclonal antibody in rabbit. By immunoelectron microscopy and Western blot analysis, TPI was detected in the cell wall and the cytoplasm of the yeast phase of P. brasiliensis. The expression of PbTPI was analyzed in transition from mycelia to yeast phase. The native PbTPI is preferentially expressed in the yeast parasitic phase of P. brasiliensis. The recombinant PbTPI was found to bind to laminin and fibronectin in ligand far-Western blot assays. TPI binds preferentially to laminin, as determined by peptide inhibition assays. Of special note, the treatment of P. brasiliensisyeast cells with anti-PbTPI polyclonal antibody and the incubation of pneumocytes and VERO cells with the recombinant protein promoted inhibition of adherence and internalization of P. brasiliensisto those in vitrocultured cells. These observations indicate that TPI could be contribute to the adhesion of the microorganism to host tissues and to the dissemination of infection.Paracoccidioides brasiliensis é um importante patógeno humano que causa a paracoccidioidomicose (PCM), uma micose sistêmica com ampla distribuição na América Latina. A adesão e a invasão de células são eventos essenciais envolvidos na infecção e disseminação do patógeno. Para isso, patógenos utilizam suas moléculas de superfície para se ligar a componentes da matriz extracelular e estabelecer a infecção. Uma proteína antigênica de P. brasiliensisfoi isolada a partir do gel de eletroforese bidimensional de proteínas totais do fungo e caracterizada. Peptídeos obtidos por sequenciamento parcial da proteína de 29 kDa e pI 5.8 mostraram homologia com triose fosfato isomerase (TPI) de diversos organismos. O cDNA e o gene completos que codificam para TPI de P. brasiliensis (PbTPI) foram caracterizados, e ambos contém uma ORF que codifica para uma proteína com 249 aminoácidos que apresenta todos os peptídeos caracterizados na PbTPI nativa. O cDNA completo que codifica para PbTPI foi expresso em Escherichia coli. A proteína recombinante TPI foi utilizada para produção de anticorpo policlonal em coelho. Através de imunomicroscopia de transmissão eletrônica e análises por Western blotting, foi detectada a presença da TPI, na parede celular de leveduras de P. brasiliensis e no citoplasma. A expressão da PbTPI foi analisada na transição das fases de micélio para levedura. A PbTPI nativa está preferencialmente expressa na fase parasitária de P. brasiliensis. A PbTPI recombinante foi capaz de se ligar a laminina e fibronectina em ensaios de Western blotting de afinidade. PbTPI se liga preferencialmente a laminina, como foi determinado por ensaio de inibição com peptídeos sintéticos. Uma observação importante, é que tanto o tratamento de P. brasiliensiscom anticorpo anti-PbTPI, quanto de pneumócitos e células VERO tratados com a TPI recombinante, promoveram considerável inibição da aderência e internalização de P. brasiliensisàs células cultivadas in vitro. Essas observações indicam que a TPI possivelmente contribui para a adesão do microrganismo aos tecidos do hospedeiro e para a disseminação da infecção.Submitted by Erika Demachki (erikademachki@gmail.com) on 2015-01-29T18:42:14Z No. of bitstreams: 2 Tese - Luiz Augusto Pereira - 2008.pdf: 11628724 bytes, checksum: 97ca17282a858a05078e31d8a06bfefe (MD5) license_rdf: 23148 bytes, checksum: 9da0b6dfac957114c6a7714714b86306 (MD5)Approved for entry into archive by Erika Demachki (erikademachki@gmail.com) on 2015-01-29T18:42:52Z (GMT) No. of bitstreams: 2 Tese - Luiz Augusto Pereira - 2008.pdf: 11628724 bytes, checksum: 97ca17282a858a05078e31d8a06bfefe (MD5) license_rdf: 23148 bytes, checksum: 9da0b6dfac957114c6a7714714b86306 (MD5)Made available in DSpace on 2015-01-29T18:42:52Z (GMT). No. of bitstreams: 2 Tese - Luiz Augusto Pereira - 2008.pdf: 11628724 bytes, checksum: 97ca17282a858a05078e31d8a06bfefe (MD5) license_rdf: 23148 bytes, checksum: 9da0b6dfac957114c6a7714714b86306 (MD5) Previous issue date: 2008-09-04Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESapplication/pdfhttp://repositorio.bc.ufg.br/tede/retrieve/15589/Tese%20-%20Luiz%20Augusto%20Pereira%20-%202008.pdf.jpgporUniversidade Federal de GoiásPrograma de Pós-graduação em Medicina Tropical e Saúde Publica (IPTSP)UFGBrasilInstituto de Patologia Tropical e Saúde Pública - IPTSP (RG)http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessParacoccidioides brasiliensisTriose fosfato isomeraseAdesinaTriose phosphate isomeraseAdhesinCIENCIAS BIOLOGICAS::MICROBIOLOGIACaracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesinaFunctional characterization of the Paracoccidioides brasiliensis triosephosphate isomerase protein for potential adhesion functioninfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/doctoralThesis6085308344741430434600600600600-7769011444564556288-38545834699762208122075167498588264571reponame:Repositório Institucional da UFGinstname:Universidade Federal de Goiás (UFG)instacron:UFGLICENSElicense.txtlicense.txttext/plain; charset=utf-82165http://repositorio.bc.ufg.br/tede/bitstreams/44368e8d-ae46-4bd1-8350-72bf8aebc6fc/downloadbd3efa91386c1718a7f26a329fdcb468MD51CC-LICENSElicense_urllicense_urltext/plain; charset=utf-849http://repositorio.bc.ufg.br/tede/bitstreams/c6e94373-2793-46ed-8fa5-84cde53cd292/download4afdbb8c545fd630ea7db775da747b2fMD52license_textlicense_texttext/html; charset=utf-822901http://repositorio.bc.ufg.br/tede/bitstreams/049f8598-9f0b-48f1-a33e-bbad3b3519d3/download29b9d5e95be03707f9d4a2e110421c11MD53license_rdflicense_rdfapplication/rdf+xml; charset=utf-823148http://repositorio.bc.ufg.br/tede/bitstreams/1b312bcc-6567-4ac6-8b13-699c4cf2b8ac/download9da0b6dfac957114c6a7714714b86306MD54TEXTTese - Luiz Augusto Pereira - 2008.pdf.txtTese - Luiz Augusto Pereira - 2008.pdf.txtExtracted Texttext/plain109130http://repositorio.bc.ufg.br/tede/bitstreams/0adbfcac-6054-427b-af3d-63eabe006a45/download4a6ac652febfc14642083c0786377057MD56THUMBNAILTese - Luiz Augusto Pereira - 2008.pdf.jpgTese - Luiz Augusto Pereira - 2008.pdf.jpgGenerated Thumbnailimage/jpeg2852http://repositorio.bc.ufg.br/tede/bitstreams/764954a9-b718-4ccc-aba8-07981c5f5746/downloadca5c5e05b3abc13d3e001d71411db18bMD57ORIGINALTese - Luiz Augusto Pereira - 2008.pdfTese - Luiz Augusto Pereira - 2008.pdfapplication/pdf11628724http://repositorio.bc.ufg.br/tede/bitstreams/b9c99ebe-3450-45d0-84eb-a02b17bc2402/download97ca17282a858a05078e31d8a06bfefeMD55tede/40032015-01-30 03:05:11.072http://creativecommons.org/licenses/by-nc-nd/4.0/Acesso Abertoopen.accessoai:repositorio.bc.ufg.br:tede/4003http://repositorio.bc.ufg.br/tedeRepositório InstitucionalPUBhttp://repositorio.bc.ufg.br/oai/requesttasesdissertacoes.bc@ufg.bropendoar:2015-01-30T05:05:11Repositório Institucional da UFG - Universidade Federal de Goiás (UFG)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 |
dc.title.eng.fl_str_mv |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
dc.title.alternative.eng.fl_str_mv |
Functional characterization of the Paracoccidioides brasiliensis triosephosphate isomerase protein for potential adhesion function |
title |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
spellingShingle |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina Pereira, Luiz Augusto Paracoccidioides brasiliensis Triose fosfato isomerase Adesina Triose phosphate isomerase Adhesin CIENCIAS BIOLOGICAS::MICROBIOLOGIA |
title_short |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
title_full |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
title_fullStr |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
title_full_unstemmed |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
title_sort |
Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina |
author |
Pereira, Luiz Augusto |
author_facet |
Pereira, Luiz Augusto |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Soares, Célia Maria de Almeida |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/8539946335852637 |
dc.contributor.referee1.fl_str_mv |
Ulhoa, Cirano José |
dc.contributor.referee2.fl_str_mv |
Campos, Ivan Torres Nicolau |
dc.contributor.referee3.fl_str_mv |
Izaac, Silvia Maria Salem |
dc.contributor.referee4.fl_str_mv |
Giannini, Maria José Soares Mendes |
dc.contributor.referee5.fl_str_mv |
Soares, Célia Maria de Almeida |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/1549739934623931 |
dc.contributor.author.fl_str_mv |
Pereira, Luiz Augusto |
contributor_str_mv |
Soares, Célia Maria de Almeida Ulhoa, Cirano José Campos, Ivan Torres Nicolau Izaac, Silvia Maria Salem Giannini, Maria José Soares Mendes Soares, Célia Maria de Almeida |
dc.subject.por.fl_str_mv |
Paracoccidioides brasiliensis Triose fosfato isomerase Adesina |
topic |
Paracoccidioides brasiliensis Triose fosfato isomerase Adesina Triose phosphate isomerase Adhesin CIENCIAS BIOLOGICAS::MICROBIOLOGIA |
dc.subject.eng.fl_str_mv |
Triose phosphate isomerase Adhesin |
dc.subject.cnpq.fl_str_mv |
CIENCIAS BIOLOGICAS::MICROBIOLOGIA |
description |
Paracoccidioides brasiliensis, an important human pathogen causative of paracoccidioidomycosis (PCM), a systemic mycosis with broad distribution in Latin America. Adhesion to and invasion of host cells are essential steps involved in the infection and dissemination of pathogens. Furthermore, pathogens use their surface molecules to bind to host extracellular matrix components to establish infection. An adhesin of P. brasiliensiswas isolated from two dimensional electrophoresis and characterized. Peptides obtained by partial sequencing of the isolated protein, which presenteda molecular mass of 29 kDa and pI 5.8, were subjected to sequence analysis of their amino acids, that revealed strong homology to triose phosphate isomerase (TPI) from several sources. The complete cDNA and gene encoding TPI of P. brasiliensis (PbTPI) were characterized and both contained an open reading frame predicted to encode a 249 amino acid protein that presented all the peptides characterized in the native PbTPI. The complete coding PbTPI cDNA was cloned and over expressed in Escherichia coli host. The purified recombinant TPI was used to produce polyclonal antibody in rabbit. By immunoelectron microscopy and Western blot analysis, TPI was detected in the cell wall and the cytoplasm of the yeast phase of P. brasiliensis. The expression of PbTPI was analyzed in transition from mycelia to yeast phase. The native PbTPI is preferentially expressed in the yeast parasitic phase of P. brasiliensis. The recombinant PbTPI was found to bind to laminin and fibronectin in ligand far-Western blot assays. TPI binds preferentially to laminin, as determined by peptide inhibition assays. Of special note, the treatment of P. brasiliensisyeast cells with anti-PbTPI polyclonal antibody and the incubation of pneumocytes and VERO cells with the recombinant protein promoted inhibition of adherence and internalization of P. brasiliensisto those in vitrocultured cells. These observations indicate that TPI could be contribute to the adhesion of the microorganism to host tissues and to the dissemination of infection. |
publishDate |
2008 |
dc.date.issued.fl_str_mv |
2008-09-04 |
dc.date.accessioned.fl_str_mv |
2015-01-29T18:42:52Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/doctoralThesis |
format |
doctoralThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
PEREIRA, Luiz Augusto. Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina. 2008. 79 f. Tese (Doutorado em Medicina Tropical e Saúde Publica) - Universidade Federal de Goiás, Goiânia, 2008. |
dc.identifier.uri.fl_str_mv |
http://repositorio.bc.ufg.br/tede/handle/tede/4003 |
dc.identifier.dark.fl_str_mv |
ark:/38995/0013000002w5g |
identifier_str_mv |
PEREIRA, Luiz Augusto. Caracterização funcional da proteína Triose fosfato isomerase de Paracoccidioides brasiliensis como potencial adesina. 2008. 79 f. Tese (Doutorado em Medicina Tropical e Saúde Publica) - Universidade Federal de Goiás, Goiânia, 2008. ark:/38995/0013000002w5g |
url |
http://repositorio.bc.ufg.br/tede/handle/tede/4003 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.program.fl_str_mv |
6085308344741430434 |
dc.relation.confidence.fl_str_mv |
600 600 600 600 |
dc.relation.department.fl_str_mv |
-7769011444564556288 |
dc.relation.cnpq.fl_str_mv |
-3854583469976220812 |
dc.relation.sponsorship.fl_str_mv |
2075167498588264571 |
dc.rights.driver.fl_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Federal de Goiás |
dc.publisher.program.fl_str_mv |
Programa de Pós-graduação em Medicina Tropical e Saúde Publica (IPTSP) |
dc.publisher.initials.fl_str_mv |
UFG |
dc.publisher.country.fl_str_mv |
Brasil |
dc.publisher.department.fl_str_mv |
Instituto de Patologia Tropical e Saúde Pública - IPTSP (RG) |
publisher.none.fl_str_mv |
Universidade Federal de Goiás |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UFG instname:Universidade Federal de Goiás (UFG) instacron:UFG |
instname_str |
Universidade Federal de Goiás (UFG) |
instacron_str |
UFG |
institution |
UFG |
reponame_str |
Repositório Institucional da UFG |
collection |
Repositório Institucional da UFG |
bitstream.url.fl_str_mv |
http://repositorio.bc.ufg.br/tede/bitstreams/44368e8d-ae46-4bd1-8350-72bf8aebc6fc/download http://repositorio.bc.ufg.br/tede/bitstreams/c6e94373-2793-46ed-8fa5-84cde53cd292/download http://repositorio.bc.ufg.br/tede/bitstreams/049f8598-9f0b-48f1-a33e-bbad3b3519d3/download http://repositorio.bc.ufg.br/tede/bitstreams/1b312bcc-6567-4ac6-8b13-699c4cf2b8ac/download http://repositorio.bc.ufg.br/tede/bitstreams/0adbfcac-6054-427b-af3d-63eabe006a45/download http://repositorio.bc.ufg.br/tede/bitstreams/764954a9-b718-4ccc-aba8-07981c5f5746/download http://repositorio.bc.ufg.br/tede/bitstreams/b9c99ebe-3450-45d0-84eb-a02b17bc2402/download |
bitstream.checksum.fl_str_mv |
bd3efa91386c1718a7f26a329fdcb468 4afdbb8c545fd630ea7db775da747b2f 29b9d5e95be03707f9d4a2e110421c11 9da0b6dfac957114c6a7714714b86306 4a6ac652febfc14642083c0786377057 ca5c5e05b3abc13d3e001d71411db18b 97ca17282a858a05078e31d8a06bfefe |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 MD5 MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositório Institucional da UFG - Universidade Federal de Goiás (UFG) |
repository.mail.fl_str_mv |
tasesdissertacoes.bc@ufg.br |
_version_ |
1811721359716253696 |