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Prion Protein Oligomerization

[ Vol. 5 , Issue. 6 ]


H. Rezaei   Pages 572 - 578 ( 7 )


The PrP propensity to adopt different structures is tightly linked to transmissible spongiform encephalopathies (TSE) which include Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scjeinker (GSS) and Kuru syndrome. In most cases, TSE is associated with the accumulation in the brain of an abnormally folded protease-resistant protein, PrPSc or PrPres, which is derived from a cellular host-encoded protease-sensitive conformer, designated PrPC. The prion propagation in the brain is postulated to occur via a conformational change of PrPC into the amyloidogenic form PrPSc, characterized by a high β sheet content. The characterization of PrPSC oligomers as well as their biological activity is currently an area of active research. Indeed, PrPSc structural diversity was proposed several years ago as a hypothesis to explain the origin of “prion strain” diversity. As prion pathologies belong to protein miss-assembly diseases, investigation of PrP conformational dynamics and, more precisely, oligomerization pathways exploration will help to acheave a better understanding of the pathological events at the molecular level.


transmissible spongiform encephalopathies, kinetic intermediate, oligomerization, soluble oligomers, protein misassembly, amyloid, catalyse, nucleus, seed


Virologie et Immunologie Moleculaires, Institut National de la Recherche Agronomique, F-78352 Jouy-en-Josas, France.

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