Free access
Review
Issue
Vet. Res.
Volume 39, Number 4, July-August 2008
Prion diseases in animals
Number of page(s) 17
DOI http://dx.doi.org/10.1051/vetres:2008025
Published online 05 June 2008
How to cite this article Vet. Res. (2008) 39:48
How to cite this article: Vet. Res. (2008) 39:48
DOI: 10.1051/vetres:2008025

Review

Misfolding of the prion protein: linking biophysical and biological approaches

Sylvie Noinville, Jean-François Chich and Human Rezaei

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

Received 23 November 2007; accepted 03 June 2008; published online 05 June 2008

Abstract - Prion diseases are a group of neurodegenerative diseases that can arise spontaneously, be inherited, or acquired by infection in mammals. The propensity of the prion protein to adopt different structures is a clue to its pathological and perhaps biological role too. While the normal monomeric PrP is well characterized, the misfolded conformations responsible for neurodegeneration remain elusive despite progress in this field. Both structural dynamics and physico-chemical approaches are thus fundamental for a better knowledge of the molecular basis of this pathology. Indeed, multiple misfolding pathways combined with extensive posttranslational modifications of PrP and probable interaction(s) with cofactors call for a combination of approaches. In this review, we outline the current physico-chemical knowledge explaining the conformational diversities of PrP in relation with postulated or putative cellular partners such as proteic or non-proteic ligands.


Key words: structure / membrane / oligomer / kinetics

Corresponding author: human.rezaei@jouy.inra.fr

© INRA, EDP Sciences 2008