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<p class="MsoTitle" style="margin:0cm;margin-bottom:.0001pt"><span style="font-size:18.0pt;font-family:"Verdana","sans-serif";color:black;font-weight:normal"><o:p> </o:p></span></p>
<p class="MsoTitle" style="margin:0cm;margin-bottom:.0001pt"><span style="font-size:18.0pt;font-family:"Verdana","sans-serif";color:black;font-weight:normal">VABILO NA PREGLOV KOLOKVIJ / INVITATION TO THE PREGL COLLOQUIUM<o:p></o:p></span></p>
<p class="MsoNormal"><b><span style="font-size:12.0pt;font-family:"Verdana","sans-serif""><o:p> </o:p></span></b></p>
<p class="MsoNormal" align="center" style="text-align:center"><b><span lang="EN-GB" style="font-size:20.0pt;font-family:"Verdana","sans-serif";color:#17365D">Prof. Van der Goot Grunberg Françoise Gisou
<o:p></o:p></span></b></p>
<p class="MsoNormal" align="center" style="text-align:center"><b><span style="font-size:20.0pt;font-family:"Verdana","sans-serif""><o:p> </o:p></span></b></p>
<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><span lang="EN-US" style="font-size:12.0pt;line-height:150%;font-family:"Arial","sans-serif";color:black;mso-fareast-language:SL">Global Health Institute, Ecole Polytechnique Fédérale
de Lausanne (EPFL), Station 15, CH-1015 Lausanne, Switzerland: <a href="mailto:gisou.vandergoot@epfl.ch">
gisou.vandergoot@epfl.ch</a><o:p></o:p></span></p>
<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><span lang="IT" style="font-size:8.0pt;line-height:150%;font-family:"Verdana","sans-serif";mso-fareast-language:SL"><o:p> </o:p></span></p>
<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><b><span style="font-size:16.0pt;line-height:150%;font-family:"Verdana","sans-serif"">Èetrtek / Thursday, 04. 04. 2013, ob / at 13:00<o:p></o:p></span></b></p>
<h6 style="mso-margin-top-alt:0cm;margin-right:0cm;margin-bottom:6.0pt;margin-left:0cm;line-height:150%">
<span lang="EN-US" style="font-size:12.0pt;line-height:150%;font-family:"Arial","sans-serif";color:black;mso-fareast-language:SL">Velika predavalnica Kemijskega in¹tituta / Lecture Hall at the National Institute of Chemistry; Hajdrihova 19, Ljubljana
<o:p></o:p></span></h6>
<p class="MsoNormal" align="center" style="text-align:center"><b><span lang="EN-GB" style="font-size:18.0pt;font-family:"Verdana","sans-serif";color:#993366">Swirling your way into the plasma membrane: the pore-forming toxin Aerolysin<o:p></o:p></span></b></p>
<p class="MsoNormal" align="center" style="text-align:center"><b><span lang="EN-GB" style="font-size:18.0pt;font-family:"Verdana","sans-serif";color:#993366"><o:p> </o:p></span></b></p>
<p class="Default" style="text-align:justify;line-height:150%"><span lang="EN-US" style="font-size:11.0pt;line-height:150%">Pore-forming toxins are the largest class of bacterial toxins. Pore-forming proteins are however found in all kingdoms of life from bacteria
to plants and mammals. The seminar will be divided into two parts. Since pore formation is a very ancient form of attack cells have developed means to respond to their permeabilizing effects. Recent findings related to cellular responses will be reported.
The second, and major, part will be focused on the structure of. Aerolysin, which is the founding member of a super-family of ß-pore forming toxins for which the pore structure is unknown. The mechanisms leading to biosynthetic folding into the soluble state
will be discussed. We have also combined X-ray crystallography, cryo-electron microscopy (EM), molecular dynamics and computational modeling to determine the structures of aerolysin mutants in their heptameric forms, trapped at various stages of the pore formation
process. A dynamic docking approach based on swarm intelligence was applied whereby the intrinsic flexibility of aerolysin extracted from new X-ray structures was utilized to fully exploit the cryo-EM spatial restraints. Using this integrated strategy, we
obtained a radically new arrangement of the prepore conformation and a near-atomistic structure of the aerolysin pore, which is fully consistent with all biochemical data available so far. Upon transition from the prepore to pore, the aerolysin heptamer shows
a unique concerted swirling movement, accompanied by a vertical collapse of the complex, ultimately leading to the insertion of a transmembrane ß-barrel.
<o:p></o:p></span></p>
<p class="MsoNormal"><span lang="FR" style="font-size:11.0pt;font-family:"Arial","sans-serif""><o:p> </o:p></span></p>
<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><b><span lang="FR" style="font-size:14.0pt;line-height:150%;font-family:"Verdana","sans-serif"">Vljudno vabljeni! / Kindly invited!<o:p></o:p></span></b></p>
<p class="MsoFooter" align="center" style="text-align:center"><span lang="IT" style="font-size:11.0pt;font-family:"Verdana","sans-serif""><o:p> </o:p></span></p>
<p class="MsoFooter" align="center" style="text-align:center"><span lang="IT" style="font-size:11.0pt;font-family:"Verdana","sans-serif"">info: prof. dr. Gregor Anderluh;
<a href="mailto:gregor.anderluh@ki.si">gregor.anderluh@ki.si</a> <o:p></o:p></span></p>
<p class="MsoNormal" align="center" style="text-align:center;line-height:150%"><b><span lang="FR" style="font-size:14.0pt;line-height:150%;font-family:"Verdana","sans-serif""><o:p> </o:p></span></b></p>
<p class="MsoNormal"><span lang="FR" style="font-size:11.0pt;font-family:"Calibri","sans-serif""><o:p> </o:p></span></p>
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