Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells

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dc.creatorNogueira, Sarah Veloso
dc.creatorFonseca, Fernanda Lopes
dc.creatorRodrigues, Marcio Lourenço
dc.creatorMundodi, Vasanth
dc.creatorAbi-chacra, Érika de Araújo
dc.creatorWinters, Michael S.
dc.creatorAlderete, John F.
dc.creatorSoares, Célia Maria de Almeida
dc.date.accessioned2018-07-11T14:04:11Z
dc.date.available2018-07-11T14:04:11Z
dc.date.issued2010-09
dc.description.abstractParacoccidioidomycosis (PCM), caused by the dimorphic fungus Paracoccidioides brasiliensis, is a dissemi- nated, systemic disorder that involves the lungs and other organs. The ability of the pathogen to interact with host components, including extracellular matrix (ECM) proteins, is essential to further colonization, invasion, and growth. Previously, enolase (EC 4.2.1.11) was characterized as a fibronectin binding protein in P. brasiliensis. Interaction of surface-bound enolase with plasminogen has been incriminated in tissue invasion for pathogenesis in several pathogens. In this paper, enolase was expressed in Escherichia coli as a recombinant glutathione S-transferase (GST) fusion protein (recombinant P. brasiliensis enolase [rPbEno]). The P. brasil- iensis native enolase (PbEno) was detected at the fungus surface and cytoplasm by immunofluorescence with an anti-rPbEno antibody. Immobilized purified rPbEno bound plasminogen in a specific, concentration- dependent fashion. Both native enolase and rPbEno activated conversion of plasminogen to plasmin through tissue plasminogen activator. The association between PbEno and plasminogen was lysine dependent. In competition experiments, purified rPbEno, in its soluble form, inhibited plasminogen binding to fixed P. brasiliensis, suggesting that this interaction required surface-localized PbEno. Plasminogen-coated P. brasil- iensis yeast cells were capable of degrading purified fibronectin, providing in vitro evidence for the generation of active plasmin on the fungus surface. Exposure of epithelial cells and phagocytes to enolase was associated with an increased expression of surface sites of adhesion. In fact, the association of P. brasiliensis with epithelial cells and phagocytes was increased in the presence of rPbEno. The expression of PbEno was upregulated in yeast cells derived from mouse-infected tissues. These data indicate that surface-associated PbEno may contribute to the pathogenesis of P. brasiliensis.pt_BR
dc.identifier.citationNOGUEIRA, Sarah Veloso; FONSECA, Fernanda L.; RODRIGUES, Marcio L.; MUNDODI, Vasanth; ABI-CHACRA, Erika A.; WINTERS, Michael S.; ALDERETE, John F.; SOARES, Célia Maria de Almeida. Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells. Infection and Immunity, Washington, v. 78, n. 9, p. 4040-4050, Sept. 2010.pt_BR
dc.identifier.doi10.1128/IAI.00221-10
dc.identifier.issn0019-9567
dc.identifier.issne- 1098-5522
dc.identifier.urihttp://repositorio.bc.ufg.br/handle/ri/15381
dc.language.isoengpt_BR
dc.publisher.countryEstados unidospt_BR
dc.publisher.departmentInstituto de Ciências Biológicas - ICB (RG)pt_BR
dc.rightsAcesso Abertopt_BR
dc.titleParacoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cellspt_BR
dc.typeArtigopt_BR

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