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dc.contributor.authorMendes-Giannini, Maria José Soares-
dc.contributor.authorAndreotti, Patricia Ferrari-
dc.contributor.authorVincenzi, Luciana Raquel-
dc.contributor.authorMonteiro da Silva, Juliana Leal-
dc.contributor.authorLenzi, Henrique Leonel-
dc.contributor.authorBenard, Gil-
dc.contributor.authorZancope-Oliveira, Roseli-
dc.contributor.authorLeonel de Matos Guedes, Herbert-
dc.contributor.authorSoares, Christiane Pienna-
dc.date.accessioned2014-05-20T13:24:28Z-
dc.date.accessioned2016-10-25T16:45:11Z-
dc.date.available2014-05-20T13:24:28Z-
dc.date.available2016-10-25T16:45:11Z-
dc.date.issued2006-05-01-
dc.identifierhttp://dx.doi.org/10.1016/j.micinf.2006.01.012-
dc.identifier.citationMicrobes and Infection. Amsterdam: Elsevier B.V., v. 8, n. 6, p. 1550-1559, 2006.-
dc.identifier.issn1286-4579-
dc.identifier.urihttp://hdl.handle.net/11449/7599-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/7599-
dc.description.abstractAdhesion to extracellular matrix (ECM) proteins plays a crucial role in invasive fungal diseases. ECM proteins bind to the surface of Paracoccidioides brasiliensis yeast cells in distinct qualitative patterns. Extracts from Pb18 strain, before (18a) and after animal inoculation (18b), exhibited differential adhesion to ECM components. Pb18b extract had a higher capacity for binding to ECM components than Pb18a. Laminin was the most adherent component for both samples, followed by type I collagen, fibronectin, and type IV collagen for Pb18b. A remarkable difference was seen in the interaction of the two extracts with fibronectin and their fragments. Pb18b extract interacted significantly with the 120-kDa fragment. Ligand affinity binding assays showed that type I collagen recognized two components (47 and 80 kDa) and gp43 bound both fibronectin and laminin. The peptide 1 (NLGRDAKRHL) from gp43, with several positively charged amino acids, contributed most to the adhesion of P. brasiliensis to Vero cells. Synthetic peptides derived from peptide YIGRS of laminin or from RGD of both laminin and fibronectin showed the greatest inhibition of adhesion of gp43 to Vero cells. In conclusion, this work provided new molecular details on the interaction between P. brasiliensis and ECNI components. (c) 2006 Elsevier SAS. All rights reserved.en
dc.format.extent1550-1559-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectParacoccidioides brasiliensispt
dc.subjectextracellular matrixpt
dc.subjectadhesinspt
dc.subjectgp43pt
dc.titleBinding of extracellular matrix proteins to Paracoccidioides brasiliensisen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionInst Oswaldo Cruz-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionFiocruz MS-
dc.description.affiliationUNESP, Fac Ciências Bioquim & Farmaceut, Dept Anal Clin, BR-14802901 Araraquara São Paulo, Brazil-
dc.description.affiliationInst Oswaldo Cruz, FIOCRUZ, Dept Patol, BR-20001 Rio de Janeiro, Brazil-
dc.description.affiliationUSP, Fac Med, Lab Alergia & Imunol Clin & Expt, BR-09500900 São Paulo, Brazil-
dc.description.affiliationUSP, Fac Med, Clin Doencas Infeecciosas & Parasitarias, BR-09500900 São Paulo, Brazil-
dc.description.affiliationFiocruz MS, Fundação Oswaldo Cruz, Inst Pesquisa Clin Evandro Chagas, IPEC,Lab Micol, BR-21045900 Rio de Janeiro, Brazil-
dc.description.affiliationUnespUNESP, Fac Ciências Bioquim & Farmaceut, Dept Anal Clin, BR-14802901 Araraquara São Paulo, Brazil-
dc.identifier.doi10.1016/j.micinf.2006.01.012-
dc.identifier.wosWOS:000239253100015-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofMicrobes and Infection-
dc.identifier.orcid0000-0002-8059-0826-
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