Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://dx.doi.org/10.3109/13693786.2011.590825 http://repositorio.unifesp.br/handle/11600/34420 |
Resumo: | Paracoccidioidomycosis (PCM), caused by the pathogenic fungus Paracoccidioides brasiliensis, is a systemic mycosis with severe acute and chronic forms. the pathology of PCM is not completely understood, and the role of proteases in the infection is not clearly defined. in this report, we describe a metallopeptidase activity in P. brasiliensis total and cytosolic protein extracts similar to that of mammalian thimet oligopeptidase (TOP). the analogous enzyme was suggested by analysis of P. brasiliensis genome data-bank and by hydrolytic activity of the FRET peptide Abz-GFSPFRQ-EDDnp which was completely inhibited by o-phenanthrolin and significantly inhibited by the TOP inhibitor, JA-2. This activity was also partially inhibited by IgG purified from patients with PCM, but not from normal individuals. As shown by high-performance liquid chromatography (HPLC), the hydrolysis of bradykinin had the same pattern as that of mammalian TOP, and anti-mammalian TOP antibodies significantly inhibited fungal cytosolic peptidase activity. Moreover, anti-mammalian TOP antibodies recognized a component of 80 kDa on fungal cytosol. A P. brasiliensis virulent isolate showed higher gene expression and TOP-like peptidase activity than a non-virulent strain. the release of enzyme following fungal lysis would be consistent with host antibody production and may have a role in the pathogenesis, inflammation and further development of the mycosis. |
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Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strainParacoccidioides brasiliensismetallopeptidasethimet oligopeptidasebradykininFRET peptidesParacoccidioidomycosis (PCM), caused by the pathogenic fungus Paracoccidioides brasiliensis, is a systemic mycosis with severe acute and chronic forms. the pathology of PCM is not completely understood, and the role of proteases in the infection is not clearly defined. in this report, we describe a metallopeptidase activity in P. brasiliensis total and cytosolic protein extracts similar to that of mammalian thimet oligopeptidase (TOP). the analogous enzyme was suggested by analysis of P. brasiliensis genome data-bank and by hydrolytic activity of the FRET peptide Abz-GFSPFRQ-EDDnp which was completely inhibited by o-phenanthrolin and significantly inhibited by the TOP inhibitor, JA-2. This activity was also partially inhibited by IgG purified from patients with PCM, but not from normal individuals. As shown by high-performance liquid chromatography (HPLC), the hydrolysis of bradykinin had the same pattern as that of mammalian TOP, and anti-mammalian TOP antibodies significantly inhibited fungal cytosolic peptidase activity. Moreover, anti-mammalian TOP antibodies recognized a component of 80 kDa on fungal cytosol. A P. brasiliensis virulent isolate showed higher gene expression and TOP-like peptidase activity than a non-virulent strain. the release of enzyme following fungal lysis would be consistent with host antibody production and may have a role in the pathogenesis, inflammation and further development of the mycosis.Universidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Microbiol Imunol & Parasitol, Unidade Oncol Expt UNONEX, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Biofis, BR-04023062 São Paulo, BrazilUniv São Paulo USP, Dept Farmacol, São Paulo, BrazilUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Microbiol Imunol & Parasitol, Unidade Oncol Expt UNONEX, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Biofis, BR-04023062 São Paulo, BrazilWeb of ScienceFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Informa HealthcareUniversidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Gravi, Ellen Tihe [UNIFESP]Paschoalin, Thaysa [UNIFESP]Dias, Bianca Rachid [UNIFESP]Moreira, Dayson F.Belizario, Jose Ernesto [UNIFESP]Oliveira, Vitor [UNIFESP]Carmona, Adriana Karaoglanovic [UNIFESP]Juliano, Maria Aparecida [UNIFESP]Travassos, Luiz Rodolpho [UNIFESP]Rodrigues, Elaine Guadelupe [UNIFESP]2016-01-24T14:17:40Z2016-01-24T14:17:40Z2012-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion81-90http://dx.doi.org/10.3109/13693786.2011.590825Medical Mycology. London: Informa Healthcare, v. 50, n. 1, p. 81-90, 2012.10.3109/13693786.2011.5908251369-3786http://repositorio.unifesp.br/handle/11600/34420WOS:000298103400011engMedical Mycologyinfo:eu-repo/semantics/openAccesshttp://informahealthcare.com/userimages/ContentEditor/1255620309227/Copyright_And_Permissions.pdfreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2021-09-29T11:24:45Zoai:repositorio.unifesp.br/:11600/34420Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652021-09-29T11:24:45Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
title |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
spellingShingle |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain Gravi, Ellen Tihe [UNIFESP] Paracoccidioides brasiliensis metallopeptidase thimet oligopeptidase bradykinin FRET peptides |
title_short |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
title_full |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
title_fullStr |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
title_full_unstemmed |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
title_sort |
Identification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strain |
author |
Gravi, Ellen Tihe [UNIFESP] |
author_facet |
Gravi, Ellen Tihe [UNIFESP] Paschoalin, Thaysa [UNIFESP] Dias, Bianca Rachid [UNIFESP] Moreira, Dayson F. Belizario, Jose Ernesto [UNIFESP] Oliveira, Vitor [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Travassos, Luiz Rodolpho [UNIFESP] Rodrigues, Elaine Guadelupe [UNIFESP] |
author_role |
author |
author2 |
Paschoalin, Thaysa [UNIFESP] Dias, Bianca Rachid [UNIFESP] Moreira, Dayson F. Belizario, Jose Ernesto [UNIFESP] Oliveira, Vitor [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Travassos, Luiz Rodolpho [UNIFESP] Rodrigues, Elaine Guadelupe [UNIFESP] |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de São Paulo (UNIFESP) Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Gravi, Ellen Tihe [UNIFESP] Paschoalin, Thaysa [UNIFESP] Dias, Bianca Rachid [UNIFESP] Moreira, Dayson F. Belizario, Jose Ernesto [UNIFESP] Oliveira, Vitor [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Travassos, Luiz Rodolpho [UNIFESP] Rodrigues, Elaine Guadelupe [UNIFESP] |
dc.subject.por.fl_str_mv |
Paracoccidioides brasiliensis metallopeptidase thimet oligopeptidase bradykinin FRET peptides |
topic |
Paracoccidioides brasiliensis metallopeptidase thimet oligopeptidase bradykinin FRET peptides |
description |
Paracoccidioidomycosis (PCM), caused by the pathogenic fungus Paracoccidioides brasiliensis, is a systemic mycosis with severe acute and chronic forms. the pathology of PCM is not completely understood, and the role of proteases in the infection is not clearly defined. in this report, we describe a metallopeptidase activity in P. brasiliensis total and cytosolic protein extracts similar to that of mammalian thimet oligopeptidase (TOP). the analogous enzyme was suggested by analysis of P. brasiliensis genome data-bank and by hydrolytic activity of the FRET peptide Abz-GFSPFRQ-EDDnp which was completely inhibited by o-phenanthrolin and significantly inhibited by the TOP inhibitor, JA-2. This activity was also partially inhibited by IgG purified from patients with PCM, but not from normal individuals. As shown by high-performance liquid chromatography (HPLC), the hydrolysis of bradykinin had the same pattern as that of mammalian TOP, and anti-mammalian TOP antibodies significantly inhibited fungal cytosolic peptidase activity. Moreover, anti-mammalian TOP antibodies recognized a component of 80 kDa on fungal cytosol. A P. brasiliensis virulent isolate showed higher gene expression and TOP-like peptidase activity than a non-virulent strain. the release of enzyme following fungal lysis would be consistent with host antibody production and may have a role in the pathogenesis, inflammation and further development of the mycosis. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-01-01 2016-01-24T14:17:40Z 2016-01-24T14:17:40Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.3109/13693786.2011.590825 Medical Mycology. London: Informa Healthcare, v. 50, n. 1, p. 81-90, 2012. 10.3109/13693786.2011.590825 1369-3786 http://repositorio.unifesp.br/handle/11600/34420 WOS:000298103400011 |
url |
http://dx.doi.org/10.3109/13693786.2011.590825 http://repositorio.unifesp.br/handle/11600/34420 |
identifier_str_mv |
Medical Mycology. London: Informa Healthcare, v. 50, n. 1, p. 81-90, 2012. 10.3109/13693786.2011.590825 1369-3786 WOS:000298103400011 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Medical Mycology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess http://informahealthcare.com/userimages/ContentEditor/1255620309227/Copyright_And_Permissions.pdf |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://informahealthcare.com/userimages/ContentEditor/1255620309227/Copyright_And_Permissions.pdf |
dc.format.none.fl_str_mv |
81-90 |
dc.publisher.none.fl_str_mv |
Informa Healthcare |
publisher.none.fl_str_mv |
Informa Healthcare |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
biblioteca.csp@unifesp.br |
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1814268310291742720 |