Synthetic prions with novel strain-specified properties

• DOI: 10.1371/journal.ppat.1005354
• Publication Date: 2015-12-31T18:37:29Z
• Authors: Fabio Moda; Thanh-Nhat T. Le; Suzana Aulić; Edoardo Bistaffa; Ilaria Campagnani; Tommaso Virgilio; Antonio Indaco; Luisa Palamara; Olivier Andréoletti; Fabrizio Tagliavini; Giuseppe Legname
• Keywords: Amyloid (mycology); Amyloid disease

Prions are infectious proteins that possess multiple self-propagating structures. The information for strains and structural specific barriers appears to be contained exclusively in the folding of pathological isoform, PrPSc. Many recent studies determined de novo prion could generated vitro from conversion recombinant (rec) protein (PrP) into amyloidal Our aim was elucidate conformational diversity recPrP amyloids their biological activities, as well gain novel insights characterizing molecular events involved mammalian propagation. To this end we materials different methodology required only purified rec full-length mouse (Mo) PrP common chemicals. Neither infected brain extracts nor amplified PrPSc were used. Following two protocols recMoPrP converted amyloid fibrils without any seeding factor. Mouse hypothalamic GT1 neuroblastoma N2a cell lines with these preparations fast screening characterize materials. Remarkably, a large number able induce change endogenous PrPC harbor several distinctive proteinase-resistant forms. One such preparation characterized vivo habouring synthetic strain specified neuropathological biochemical properties.