title: Aggregation and amyloid fibril formation of the prion protein is accelerated in the presence of glycogen.
abstract: Prion diseases like Creutzfeldt-Jakob disease in humans or scrapie in sheep and goats are infectious neurodegenerative diseases. Their infectious agent, called prion, is composed mainly of aggregated and misfolded prion protein and non-proteinaceous components. An example of such a common non-proteinaceous secondary component of natural prions is the polysaccharide scaffold. We studied the influence of such a polysaccharide on the conformational transition of PrP applying an in vitro conversion system. Here we report that glycogen supports and accelerates PrP amorphous aggregation similar to seeded aggregation and leads to co-aggregates. Furthermore, PrP fibril formation was highly accelerated in the presence of glycogen.
authors.affiliation: Institut für Physikalische Biologie, Heinrich-Heine-Universität, Düsseldorf, Germany.
authors.forename: Giannantonio
authors.initials: G
authors.lastname: Panza
authors.forename: Jan
authors.initials: J
authors.lastname: Stöhr
authors.forename: Eva
authors.initials: E
authors.lastname: Birkmann
authors.forename: Detlev
authors.initials: D
authors.lastname: Riesner
authors.forename: Dieter
authors.initials: D
authors.lastname: Willbold
authors.forename: Otto
authors.initials: O
authors.lastname: Baba
authors.forename: Tatsuo
authors.initials: T
authors.lastname: Terashima
authors.forename: Christian
authors.initials: C
authors.lastname: Dumpitak
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D002942:Circular Dichroism; D006224:Cricetinae; D006003:Glycogen / Q000494:pharmacology*; D008647:Mesocricetus; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D000682:Amyloid; D011328:Prions; D011994:Recombinant Proteins; D006003:Glycogen