2007
DOI: 10.1073/pnas.0702662104
|View full text |Cite|
|
Sign up to set email alerts
|

Formation of native prions from minimal components in vitro

Abstract: The conformational change of a host protein, PrP C , into a disease-associated isoform, PrP Sc , appears to play a critical role in the pathogenesis of prion diseases such as Creutzfeldt–Jakob disease and scrapie. However, the fundamental mechanism by which infectious prions are produced in neurons remains unknown. To investigate the mechanism of prion formation biochemically, we conducted a series of experiments using the protein misfolding cyclic amplification … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

33
640
0
1

Year Published

2008
2008
2017
2017

Publication Types

Select...
5
2
2

Relationship

0
9

Authors

Journals

citations
Cited by 585 publications
(674 citation statements)
references
References 55 publications
33
640
0
1
Order By: Relevance
“…3.3.2) lends support for a relatively finite rather than a continuous portfolio of favored conformations [120]. Recently it has been shown that infectious prions could be spontaneously generated using PMCA from healthy brains unseeded with prions [66]. It would be of interest to see to which extent the spectrum of artificially created PrP Sc conformations will overlap that of the natural one.…”
Section: The Conformational Selection Hypothesismentioning
confidence: 99%
“…3.3.2) lends support for a relatively finite rather than a continuous portfolio of favored conformations [120]. Recently it has been shown that infectious prions could be spontaneously generated using PMCA from healthy brains unseeded with prions [66]. It would be of interest to see to which extent the spectrum of artificially created PrP Sc conformations will overlap that of the natural one.…”
Section: The Conformational Selection Hypothesismentioning
confidence: 99%
“…Thus, 269 it has been suggested that an as yet unidentified polyanion may be a component of 270 the infectious prion particle (13). The search for a more complete understanding of 271 the causative agent(s) of PrP--C to PrP--Sc conversion has continued (13). 272 273…”
Section: Transmissible Spongiform Encephalopathymentioning
confidence: 99%
“…Teflon 267 beads increase the amplification rate in prion PMCA reactions (PCMAb) for 268 unknown reasons, as does addition of the amphipathic glycoside saponin (15). Thus, 269 it has been suggested that an as yet unidentified polyanion may be a component of 270 the infectious prion particle (13). The search for a more complete understanding of 271 the causative agent(s) of PrP--C to PrP--Sc conversion has continued (13).…”
Section: Transmissible Spongiform Encephalopathymentioning
confidence: 99%
“…This hypothesis suggests that abnormally--261 folded PrP--Sc protein itself is the transmissible and infectious agent causing TSE 262 disease. However, exposure to PrP--Sc alone results in only limited conversion of 263 normal PrP--C. Further and of equal interest, it has been demonstrated that PrP--Sc 264 can actually be formed without provision of pre--existing PrP--Sc, using a protein 265 misfolding cyclic amplification (PMCA) technique relying on PrP--C, lipid molecules, 266 and a synthetic polyanion such as use of poly(A) RNA substrate (13,15). Teflon 267 beads increase the amplification rate in prion PMCA reactions (PCMAb) for 268 unknown reasons, as does addition of the amphipathic glycoside saponin (15).…”
Section: Transmissible Spongiform Encephalopathymentioning
confidence: 99%