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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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Probing the chemistry and conformational change underlying autocatalytic self-propagation of misfolded prion protein

M. Beekes - P24,Transmissible Spongiform Encephalopathies, Robert Koch-Institut, Berlin - Germany

Prions, the causative agents of fatal neurodegenerative diseases in animals and humans such as scrapie, bovine spongiform encephalopathy (BSE, “mad cow disease”), Creutzfeldt-Jakob disease (CJD) or its variant form vCJD consist essentially of a misfolded and aberrantly aggregated isoform of a cellular protein called PrP (prion protein).

Prions differ fundamentally from bacteria, viruses, fungi or parasites in that they are thought to replicate without the need of genetic material (i.e. nucleic acid) by a mechanism called “seeded polymerization” which in principle resembles phenomena known from crystallization. However, the formation, replication and exact chemical composition of prions are still far from being completely understood.

In this reaearch project a recently developed method called “protein misfolding cyclic amplification” (PMCA) that allows to study prions and their replication in vitro (i.e. in the test tube) will be used to further probe the role of molecules other than PrP (e.g. nucleic acids) and the mechanisms involved in the propagation of misfolded prion proteins. This shall also provide a better understanding of the molecular basis of the “strain phenomenon”, i. e. the existence of distinct prion strains that differ in their phenotypic characteristics although they are derived from the same cellular prion protein. Changes in the spatial structure associated with the propagation of misfolded prion proteins by PMCA will be monitored using biophysical spectroscopical methods in order to define as precisely as possible the impact of chemical misfolding factors on the molecular conversion of PrP.

The further elucidation of the molecular entities and mechanisms involved in the infectious misfolding of prion proteins will contribute to an efficient management and control of biohazards emanating from prions.

 
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