Protein macro-assembly and Prion diseases

The main field of investigation of the Protein macro-assembly and Prion diseases research group aims at understanding the relationship between protein structural information transfer and prion replication and neurotoxicity.

To achieve this goal, our team covers a broad spectrum of scientific expertise, from biophysics and biochemistry to prion biology per se: cell culture and transgenic mouse models (collaboration with J-L. Vilotte's team, INRA - GABI Unit).

The results published by the team address major topics in the prion field:

• Prion diversity and evolution under selective pressure (Beringue et al., Science 2012, PloS Pathogens 2006, J Neuroscience 2007, PLoS one 2008, Emerging Infectious Diseases 2008)

• Identification of the minimal structural perturbation initiating prion replication (Xu et al., JBC 2011, FASEB J 2011, Prigent et al., Prion 2011)

• Oligomerization pathways of PrP and other misfolded proteins (Chakroun et al., FASEB J 2010, Eghiaian et al., PNAS 2007)

• Demonstration of a strain-dependent relationship between infectivity and the size of misfolded PrP assemblies, using fractionation methods (Tixador et al., PLoS Pathogens 2010)

• Deciphering molecular events leading to neuronal death with CNS primary cultures permissive to prion replication (Cronier et al., PNAS 2004, J Virol 2007 and FASEB J 2012)

• Study of normal/abnormal PrP and more recently Shadoo biochemistry (Dron, Moudjou et al., JBC 2010, Moudjou et al., Neurochem int 2007, unpublished)