Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/34420
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dc.contributor.authorGravi, Ellen Tihe [UNIFESP]
dc.contributor.authorPaschoalin, Thaysa [UNIFESP]
dc.contributor.authorDias, Bianca Rachid [UNIFESP]
dc.contributor.authorMoreira, Dayson F.
dc.contributor.authorBelizario, Jose Ernesto [UNIFESP]
dc.contributor.authorOliveira, Vitor [UNIFESP]
dc.contributor.authorCarmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorTravassos, Luiz Rodolpho [UNIFESP]
dc.contributor.authorRodrigues, Elaine Guadelupe [UNIFESP]
dc.date.accessioned2016-01-24T14:17:40Z-
dc.date.available2016-01-24T14:17:40Z-
dc.date.issued2012-01-01
dc.identifierhttp://dx.doi.org/10.3109/13693786.2011.590825
dc.identifier.citationMedical Mycology. London: Informa Healthcare, v. 50, n. 1, p. 81-90, 2012.
dc.identifier.issn1369-3786
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/34420-
dc.description.abstractParacoccidioidomycosis (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.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent81-90
dc.language.isoeng
dc.publisherInforma Healthcare
dc.relation.ispartofMedical Mycology
dc.rightsAcesso aberto
dc.subjectParacoccidioides brasiliensisen
dc.subjectmetallopeptidaseen
dc.subjectthimet oligopeptidaseen
dc.subjectbradykininen
dc.subjectFRET peptidesen
dc.titleIdentification of a metallopeptidase with TOP-like activity in Paracoccidioides brasiliensis, with increased expression in a virulent strainen
dc.typeArtigo
dc.rights.licensehttp://informahealthcare.com/userimages/ContentEditor/1255620309227/Copyright_And_Permissions.pdf
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Microbiol Imunol & Parasitol, Unidade Oncol Expt UNONEX, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Biofis, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniv São Paulo USP, Dept Farmacol, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Microbiol Imunol & Parasitol, Unidade Oncol Expt UNONEX, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo Escola Paulista Med UNIFESP EP, Dept Biofis, BR-04023062 São Paulo, Brazil
dc.identifier.doi10.3109/13693786.2011.590825
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000298103400011
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Artigo

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