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2011 Call for projects in the field of viral safety for biological products
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Selected projects 2009

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Elucidation of the misfolding process…Insights into a preamyloid state by selectively trapping prion proteins in oligomeric forms

PI:J.Torrent - Unité mixte Inserm U710-UM2-EPHE, Montpellier - France

Other Investigators: Véronique Perrier - U710-UM2-EPHE, Montpellier - France
Human Rezaei - INRA, Jouy-en-Josas - France

We can represent, in a very simplified way, the process governing the pathology of prion diseases as a molecular transformation of a soluble cellular protein (PrPC) into a misfolded form (PrPSc), which finally assembles into large complex deposits.
To understand and eventually control this as yet unknown process, we aim to develop an original approach: study the mechanisms involved in the early steps of PrP self-assembly by selectively trapping PrPs in small particles composed of two, three or four PrP molecules. Since PrP assembly proceeds very rapidly, these small transient and extremely unstable particles are very difficult to study. To circumvent this problem, we will use a recently identified family of chemical compounds that remarkably trigger the formation of stable small particles of PrPSc.
These chemical compounds should therefore provide key tools for understanding the molecular events governing the formation of the large complex deposits. Since low molecular weight species are believed to be neurotoxic in various amyloid diseases and responsible for prion infectivity, this project should help in the development of therapeutic strategies impeding prion toxicity and infectivity.


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