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EBV Conference 2008 Guangzhou - Baylor College of Medicine

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78 (RegID: 1226)<br />

Raphele Germi<br />

Institution: University Joseph Fourier/CHU de Grenoble<br />

e-mail: rgermi@chu-grenoble.fr<br />

THREE DIMENSIONAL STRUCTURE OF THE EPSTEIN-BARR VIRUS CAPSID<br />

RAPHAELE GERMI, PATRICE MORAND, SYLVIE LARRAT, JOSETTE GUIMET, Geneviève GUY,<br />

ROB RUIGROK, GUY SCHOEHN<br />

Posterabstract:<br />

The knowledge <strong>of</strong> <strong>EBV</strong> morphology is widely based on its homology with the others herpesviruses. The<br />

common properties <strong>of</strong> HSV-1, CMV and HHV8 icosahedral capsid structure is a triangulation number <strong>of</strong><br />

T=16, 150 hexamers and 12 pentamers <strong>of</strong> the major capsid protein (VP5) and 320 triplex complexes<br />

located on each <strong>of</strong> the local three-fold axis. The triplex complex is an heterotrimers alpha beta 2 (VP19C<br />

and VP23). Here we report the 3D structure <strong>of</strong> the <strong>EBV</strong> capsid, reconstructed from electron<br />

cryomicroscopy (cryoEM) images and show its structural similarities and differences with HHV8. Viruses<br />

were produced in cells culture, concentrated and purified onto CsCl density gradient, localize by<br />

negative-stain and cryo-EM was performed by using a LaB6 FEI CM200 microscope equipped with a<br />

Gatan 626 cryoholder operated at 200 kV and 20,000x nominal magnification. The 500 best particles,<br />

selected manually from 19 Kodak SO163 films digitised at a 7 祄 sampling step on a Z/I Imaging<br />

PhotoScan, were used to calculate the 20 ?resolution. The 3D structure <strong>of</strong> the virus exhibit the T=16<br />

triangulation number which characterize the herpesviridae family. The structure is very similar to the one<br />

<strong>of</strong> HHV8, in size (1250 ?in diameter) but also in the different capsomer organization. The hexons, pentons<br />

and the triplex capsomers are very similar in shape. There is anyway a big difference between all the<br />

known structure <strong>of</strong> herpesviruses and our structure. Around the 5-fold axis <strong>of</strong> the <strong>EBV</strong> capsid, at the<br />

expected position <strong>of</strong> the triplex protein, there is only a small density present. This is the first time that this<br />

kind <strong>of</strong> phenomena is visible in the herpesviridae family.<br />

<strong>EBV</strong> <strong>Conference</strong> <strong>2008</strong> <strong>Guangzhou</strong><br />

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