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HSP90 is a molecular chaperone that helps in the folding and stabilization of selected polypeptides. HSP90 family members have been shown to present important roles in fungi, especially in the pathogenic species, as an immunodominant antigen and also as a potential antifungal therapeutic target.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>In this work, we decided to further study the <jats:italic>Pbhsp90<\/jats:italic> gene, its expression and role in cell viability because it plays important roles in fungal physiology and pathogenesis. Thus, we have sequenced a <jats:italic>Pbhsp90<\/jats:italic> cDNA and shown that this gene is present on the genome as a single copy. We have also confirmed its preferential expression in the yeast phase and its overexpression during dimorphic transition and oxidative stress. Treatment of the yeast with the specific HSP90 inhibitors geldanamycin and radicicol inhibited growth at 2 and 10 \u03bcM, respectively.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion<\/jats:title>\n            <jats:p>The data confirm that the <jats:italic>Pbhsp90<\/jats:italic> gene encodes a morphologically regulated and stress-responsive protein whose function is essential to cell viability of this pathogen. This work also enforces the potential of HSP90 as a target for antifungal therapies, since the use of HSP90 inhibitors is lethal to the <jats:italic>P. brasiliensis<\/jats:italic> yeast cells in a dose-responsive manner.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2180-8-158","type":"journal-article","created":{"date-parts":[[2008,9,30]],"date-time":"2008-09-30T18:15:43Z","timestamp":1222798543000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":33,"title":["The stress responsive and morphologically regulated hsp90 gene from Paracoccidioides brasiliensis is essential to cell viability"],"prefix":"10.1186","volume":"8","author":[{"given":"Andr\u00e9 M","family":"Nicola","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ros\u00e2ngela V","family":"Andrade","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandra S","family":"Dantas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patr\u00edcia A","family":"Andrade","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabr\u00edcio BM","family":"Arraes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Larissa","family":"Fernandes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ildinete","family":"Silva-Pereira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria Sueli S","family":"Felipe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2008,9,22]]},"reference":[{"issue":"7","key":"591_CR1","doi-asserted-by":"publisher","first-page":"1098","DOI":"10.1002\/1521-3773(20020402)41:7<1098::AID-ANIE1098>3.0.CO;2-9","volume":"41","author":"S Walter","year":"2002","unstructured":"Walter S, Buchner J: Molecular chaperones \u2013 cellular machines for protein folding. 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