Template-induced protein misfolding underlying prion diseases

International audienceProteins with prion properties are closely associated to a class of fatal neurodegenerative illnesses in mammals and to the emergence and propagation of phenotypic traits in yeast. The structural transition from the correctly folded, native form of a prion protein to a persistent misfolded form that ultimately may cause cell death or the transmission of phenotypic traits are not yet fully understood. The structural and functional properties of mammalian and yeast prions in their soluble and oligomeric forms are presented as are the mechanistic models accounting for this structure-based mode of inheritance. This review highlights a number of unquestioned issues and unanswered questions that may allow a better understanding of the role of prion proteins in vivo and their propagation mechanism(s)