Isolation and partial characterization of a 30 kDa adhesin from Paracoccidioides brasiliensis

dc.contributor.authorAndreotti, P. F.
dc.contributor.authorda Silva, JLM
dc.contributor.authorBailao, A. M. B.
dc.contributor.authorSoares, C. M. A.
dc.contributor.authorBenard, G.
dc.contributor.authorSoares, Christiane Pienna [UNESP]
dc.contributor.authorMendes-Giannini, Maria José Soares [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de Goiás (UFG)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T13:24:36Z
dc.date.available2014-05-20T13:24:36Z
dc.date.issued2005-05-01
dc.description.abstractThe virulence of Paracoccidioides brasiliensis can be attenuated or lost after long periods of repeated subculturing and reestablished after animal inoculation. Only one adhesin (gp43) has been described until now, among the various identified components of P. brasiliensis, and gp43 shows adhesion to laminin. Thus, the present study was designed to isolate and characterize factors putatively related to the capacity of this fungus to adhere to the host by comparing P brasiliensis samples, taken before and after animal inoculation. The two samples differed in their pattern of adhesion and invasion. The sample recently isolated from animals (Pb18b) demonstrated a greater capacity to adhere and to invade the Vero cells than the one subcultured in vitro (Pb18a). Extract from Ph18b also showed higher levels of protein expression than that from Pb18a, when two-dimensional electrophoresis gels were compared. A protein species of 30 kDa, pI 4.9, was more evident in the Pb18b extract and had properties of adhesin. Laminin, but none of the other extracellular matrix (ECM) components, such as fibronectin, collagen I and IV, bound specifically to the P. brasiliensis 30 kDa protein. The roles of 30 kDa and gp43 in cellular interactions were investigated and the adhesion of P. brasiliensis yeast cells was intensively inhibited by pre-treatment of epithelial cells with 30 kDa protein and gp43. Thus, this study presents evidence that adhesion capacity could be related to virulence, and that a 30 kDa adhesin accumulated differentially in samples with different levels of pathogenicity. This protein and its adhesion characteristics are being published for the first time and may be related to the virulence of P brasiliensis. (c) 2005 Elsevier SAS. All rights reserved.en
dc.description.affiliationUNESP, Fac Ciências Farmaceut, Dept Anal Clin, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUniv Fed Goias, Inst Ciências Biol, BR-74001970 Goiania, Go, Brazil
dc.description.affiliationUniv São Paulo, Fac Med, Lab Alergia & Imunol Clin & Expt & Clin Doencas I, BR-09500900 São Paulo, SP, Brazil
dc.description.affiliationUnespUNESP, Fac Ciências Farmaceut, Dept Anal Clin, BR-14801902 Araraquara, SP, Brazil
dc.format.extent875-881
dc.identifierhttp://dx.doi.org/10.1016/j.micinf.2005.02.005
dc.identifier.citationMicrobes and Infection. Amsterdam: Elsevier B.V., v. 7, n. 5-6, p. 875-881, 2005.
dc.identifier.doi10.1016/j.micinf.2005.02.005
dc.identifier.issn1286-4579
dc.identifier.lattes1768025290373669
dc.identifier.orcid0000-0002-8059-0826
dc.identifier.orcid0000-0003-1740-7360
dc.identifier.urihttp://hdl.handle.net/11449/7678
dc.identifier.wosWOS:000230224400009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMicrobes and Infection
dc.relation.ispartofjcr2.924
dc.relation.ispartofsjr1,205
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectParacoccidioides brasiliensispt
dc.subjectadhesinpt
dc.subject30 kDa proteinpt
dc.subjectlamininpt
dc.titleIsolation and partial characterization of a 30 kDa adhesin from Paracoccidioides brasiliensisen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes1768025290373669[6]
unesp.author.orcid0000-0001-7754-4047[3]
unesp.author.orcid0000-0002-8059-0826[7]
unesp.author.orcid0000-0003-1740-7360[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt

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