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dc.contributor.authorDonofrio, Fabiana Cristina-
dc.contributor.authorAlvarez Calil, Ana Carolina-
dc.contributor.authorMiranda, Elaine Toscano-
dc.contributor.authorAlmeida, Ana Marisa Fusco-
dc.contributor.authorBenard, Gil-
dc.contributor.authorSoares, Christiane Pienna-
dc.contributor.authorVeloso, Sarah Nogueira-
dc.contributor.authorde Almeida Soares, Celia Maria-
dc.contributor.authorMendes-Giannini, Maria José Soares-
dc.identifier.citationJournal of Medical Microbiology. Reading: Soc General Microbiology, v. 58, n. 6, p. 706-713, 2009.-
dc.description.abstractParacoccidioides brasiliensis yeast cells can enter mammalian cells and may manipulate the host cell environment to favour their own growth and survival. Moreover, fibronectin and several other host extracellular matrix proteins are recognized by various components of the yeast cell extracts. The present study was designed to isolate and characterize a fibronectin-binding protein from P. brasiliensis. We also compared P. brasiliensis strain 18, tested before (Pb18a) and after (Pb18b) animal passage, in relation to its adhesion and invasion processes. Extracts from both samples, when cultured on blood agar solid medium, showed higher levels of protein expression than when the same samples were cultured on Fava-Netto solid medium, as demonstrated by two-dimensional electrophoresis and SDS-PAGE. Also, both Pb18a and Pb18b exhibited stronger adhesion to A549 epithelial cells when cultured on blood agar medium than when cultured on Fava-Netto medium. Ligand affinity binding assays revealed a protein of 54 kDa and pl 5.6 in P. brasiliensis cell-free extracts with the properties of a fibronectin-binding adhesin, which was characterized by tryptic digestion and mass spectroscopy as a homologue of enolase from P. brasiliensis. Antibody raised against this 54 kDa protein abolished 80 % of P. brasiliensis adhesion to A549 epithelial cells. Our results demonstrate that P. brasiliensis produces a fibronectin-binding adhesin, irrespective of the culture medium, and that this activity can be inhibited by a specific antibody and is involved in the adhesion of the fungus to pulmonary epithelial cells.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.publisherSoc General Microbiology-
dc.sourceWeb of Science-
dc.titleEnolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding proteinen
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Federal de Goiás (UFG)-
dc.description.affiliationUniv Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, São Paulo, Brazil-
dc.description.affiliationUniv São Paulo, Fac Med, Lab Dermatol & Imunodeficiencias, São Paulo, Brazil-
dc.description.affiliationUniversidade Federal de Goiás (UFG), Inst Ciencias Biol, Mol Biol Lab, Goiania, Go, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, São Paulo, Brazil-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Medical Microbiology-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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