{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T09:15:08Z","timestamp":1789895708273,"version":"4.0.1"},"reference-count":53,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Paracoccidioidomycosis (PCM), caused by the dimorphic fungus\n            <jats:italic>Paracoccidioides brasiliensis<\/jats:italic>\n            , is a disseminated, 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\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            . 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\n            <jats:italic>Escherichia coli<\/jats:italic>\n            as a recombinant glutathione\n            <jats:italic>S<\/jats:italic>\n            -transferase (GST) fusion protein (recombinant\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            enolase [r\n            <jats:italic>Pb<\/jats:italic>\n            Eno]). The\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            native enolase (\n            <jats:italic>Pb<\/jats:italic>\n            Eno) was detected at the fungus surface and cytoplasm by immunofluorescence with an anti-r\n            <jats:italic>Pb<\/jats:italic>\n            Eno antibody. Immobilized purified r\n            <jats:italic>Pb<\/jats:italic>\n            Eno bound plasminogen in a specific, concentration-dependent fashion. Both native enolase and r\n            <jats:italic>Pb<\/jats:italic>\n            Eno activated conversion of plasminogen to plasmin through tissue plasminogen activator. The association between\n            <jats:italic>Pb<\/jats:italic>\n            Eno and plasminogen was lysine dependent. In competition experiments, purified r\n            <jats:italic>Pb<\/jats:italic>\n            Eno, in its soluble form, inhibited plasminogen binding to fixed\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            , suggesting that this interaction required surface-localized\n            <jats:italic>Pb<\/jats:italic>\n            Eno. Plasminogen-coated\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            yeast cells were capable of degrading purified fibronectin, providing\n            <jats:italic>in vitro<\/jats:italic>\n            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\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            with epithelial cells and phagocytes was increased in the presence of r\n            <jats:italic>Pb<\/jats:italic>\n            Eno. The expression of\n            <jats:italic>Pb<\/jats:italic>\n            Eno was upregulated in yeast cells derived from mouse-infected tissues. These data indicate that surface-associated\n            <jats:italic>Pb<\/jats:italic>\n            Eno may contribute to the pathogenesis of\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/iai.00221-10","type":"journal-article","created":{"date-parts":[[2010,7,7]],"date-time":"2010-07-07T02:22:06Z","timestamp":1278469326000},"page":"4040-4050","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":91,"title":["<i>Paracoccidioides brasiliensis<\/i>\n            Enolase Is a Surface Protein That Binds Plasminogen and Mediates Interaction of Yeast Forms with Host Cells"],"prefix":"10.1128","volume":"78","author":[{"given":"Sarah Veloso","family":"Nogueira","sequence":"first","affiliation":[{"name":"Laborato\u0301rio de Biologia Molecular, Instituto de Cie\u0302ncias Biolo\u0301gicas, Universidade Federal de Goia\u0301s, 74001-970 Goia\u0302nia, Goia\u0301s, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernanda L.","family":"Fonseca","sequence":"additional","affiliation":[{"name":"Laboratorio de Estudos Integrados em Bioquimica Microbiana, Instituto de Microbiologia Professor Paulo de Goes, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-590, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcio L.","family":"Rodrigues","sequence":"additional","affiliation":[{"name":"Laboratorio de Estudos Integrados em Bioquimica Microbiana, Instituto de Microbiologia Professor Paulo de Goes, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-590, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vasanth","family":"Mundodi","sequence":"additional","affiliation":[{"name":"School of Molecular Biosciences, Washington State University, Pullman, Washington 99163"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erika A.","family":"Abi-Chacra","sequence":"additional","affiliation":[{"name":"Laboratorio de Estudos Integrados em Bioquimica Microbiana, Instituto de Microbiologia Professor Paulo de Goes, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-590, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael S.","family":"Winters","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John F.","family":"Alderete","sequence":"additional","affiliation":[{"name":"School of Molecular Biosciences, Washington State University, Pullman, Washington 99163"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ce\u0301lia Maria de Almeida","family":"Soares","sequence":"additional","affiliation":[{"name":"Laborato\u0301rio de Biologia Molecular, Instituto de Cie\u0302ncias Biolo\u0301gicas, Universidade Federal de Goia\u0301s, 74001-970 Goia\u0302nia, Goia\u0301s, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2008.03.017"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/infdis\/173.3.684"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micinf.2005.07.027"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.74.1.382-389.2006"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.5.2.379-390.2006"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2001.02448.x"},{"key":"e_1_3_2_8_2","first-page":"15.8.1-15.8.28","year":"2006","unstructured":"Bookout, A. 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