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Protein Misfolding Cyclic Amplification of Prions
Published on: November 7, 2012
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Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification
Mohammed Moudjou1, Jérôme Chapuis1, Mériem Mekrouti1
1VIM, INRA, Université Paris-Saclay, 78350, Jouy-en-Josas, France.
Scientific Reports
|July 8, 2016
Summary
Prion strains are not determined by the glycosylation of prion proteins. The structural backbone of misfolded prion protein assemblies, not attached glycans, encodes strain properties and perpetuation.
Area of Science:
- Neuroscience
- Biochemistry
- Molecular Biology
Background:
- Prions are misfolded prion protein assemblies (PrPSc) that replicate by converting cellular prion protein (PrPC).
- Distinct prion strains exhibit unique biochemical properties, including glycotype, and biological traits.
- The mechanism of prion strain information storage and self-perpetuation remains unclear.
Purpose of the Study:
- To investigate the role of cellular prion protein (PrPC) glycosylation in prion formation and strain perpetuation.
- To determine if PrPC or PrPSc glycoform stoichiometry influences prion strain properties.
Main Methods:
- Developed an efficient protein misfolding cyclic amplification (PMCA) method using cells expressing specific PrPC species.
- Applied PMCA to cells expressing PrPC glycosylation mutants.
Main Results:
- Neither PrPC nor PrPSc glycoform stoichiometry was essential for PrPSc formation.
- Glycosylation status did not influence the perpetuation of prion strain properties.
Conclusions:
- Prion strain properties, including PrPSc glycotype, are encoded within the structural backbone of PrPSc assemblies.
- Attached glycans do not play a critical role in enciphering prion strain information or perpetuation.
