ÿþ<HTML><HEAD><TITLE>XI International Meeting on Paracoccidioidomycosis</TITLE><link rel=STYLESHEET type=text/css href=css.css></HEAD><BODY aLink=#ff0000 bgColor=#FFFFFF leftMargin=0 link=#000000 text=#000000 topMargin=0 vLink=#000000 marginheight=0 marginwidth=0><table align=center width=700 cellpadding=0 cellspacing=0><tr><td align=left bgcolor=#cccccc valign=top width=550><font face=arial size=2><strong><font face=Verdana, Arial, Helvetica, sans-serif size=3><font size=1>XI International Meeting on Paracoccidioidomycosis</font></font></strong><font face=Verdana size=1><b><br></b></font><font face=Verdana, Arial,Helvetica, sans-serif size=1><strong> </strong></font></font></td><td align=right bgcolor=#cccccc valign=top width=150><font face=arial size=2><strong><font face=Verdana, Arial, Helvetica, sans-serif size=1><font size=1>Resume:110-1</font></em></font></strong></font></td></tr><tr><td colspan=2><br><br><table align=center width=700><tr><td><b>Poster (Painel)</b><br><table width="100%"><tr><td width="60">110-1</td><td><b>Hsp-90 cooperate with calcineurin to promote mycelium to yeast transition in Paracoccidioides brasiliensis</b></td></tr><tr><td valign=top>Authors:</td><td><u>Tatiana Guimarães de Freitas Matos </u> (UNIVAP - Universidade do Vale do Paraíba) ; Cláudia Barbosa Ladeira de Campos (UNIVAP - Universidade do Vale do Paraíba) </td></tr></table><p align=justify><b><font size=2>Abstract</font></b><p align=justify class=tres><font size=2>Paracoccidioidemycosis is a prevalent systemic mycosis in Latin America. It is caused by the etiological agent <i>Paracoccidioides brasiliensis</i>, which forms a group called dimorphic fungi, together with five other phylogenetically related fungi. They are so called because they suffer a change in morphology inside host´s body. In the environment, they live as hyphal molds (mycelium) and convert to a pathogenic yeast form in the host´s lungs. The <i>P. brasiliensis</i> morphological transition (M-Y phase transition) can be induced <i>in vitro</i> by switching the incubation temperature from 25°C to 37°C. The morphological switch can be, therefore, considered as a kind of heat-shock response. In this way, we postulated that Hsp-90, a heat-shock protein, could be involved in <i>P. brasilisensis</i> M-Y phase transition. In order to test our hypothesis we treated <i>P. brasiliensis</i> with Geldanamycin (GdA), an Hsp-90 inhibitor, during M-Y phase transition as well as the yeast and mycelial phases. We noticed that treatment with GdA caused a dose-dependent inhibition of <i>P. brasilisensis</i> yeast proliferation, but this inhibition is not observed in the mycelial phase. We also observed that Hsp-90 inhibition by GdA blocks M-Y transition in a dose-dependent manner. It has been shown that calcineurin is a client protein of Hsp-90 in many different biological systems. In this way, we combined GdA and ciclosporin A (CsA), a calcineurin inhibitor, to treat <i>P. brasiliensis</i> during M-Y phase transition in order to test whether these proteins could be interacting in <i>P. brasiliensis</i> model system. We show that at low concentrations, these drugs separately have a small effect over M-Y phase transition, but presented a much greater effect when combined and completely block transition. So, in this work, we conclude that HSP-90 plays an important role in <i>P. brasiliensis</i> M-Y phase transition, helping in the fungus adaptation when submitted to a heat stress, probably not only in the culture but also inside host´s body. We also conclude that Hsp-90 activity is dependent on calcineurin activity, and we suggest that these proteins may be linked in a pathway that governs M-Y phase transition. Supported by Fapesp, CNPq and Capes. </font></p><br><b>Keyword: </b>&nbsp;Dimorphism, Hsp-90, Calcineurin, mycelium, yeast</td></tr></table></tr></td></table></body></html>