Prion protein conversion in vitro

  title={Prion protein conversion in vitro},
  author={Surachai Supattapone},
  journal={Journal of Molecular Medicine},
  • S. Supattapone
  • Published 10 March 2004
  • Biology
  • Journal of Molecular Medicine
The infectious agents of prion diseases are composed primarily of an infectious protein designated PrPSc. In cells infected with prions, a host glycoprotein termed PrPC undergoes induced conformational change to PrPSc, but the molecular mechanism underlying this structural transition occurs remains unknown. The prion-seeded conversion of PrPC to protease-resistant PrPSc-like molecules (PrPres) has been studied both in crude and purified in vitro systems in order to investigate the mechanism of… 

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Prion Protein Complexed to N2a Cellular RNAs through Its N-terminal Domain Forms Aggregates and Is Toxic to Murine Neuroblastoma Cells*S⃞

Results indicate that there is selectivity in the species generated by interaction with different molecules of RNA, and the catalytic effect of RNA on the PrPC→PrPSc conversion depends on the RNA sequence, and small RNA molecules may exert a protective effect.

Prions: protein only or something more? Overview of potential prion cofactors.

Recent findings such as the cellular factors that might be involved in the conformational conversion of prion proteins and the potential mechanisms by which they could operate are discussed.

The reconstitution of mammalian prion infectivity de novo

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Aspects of prion protein dynamics in cell culture models

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RNA molecules stimulate prion protein conversion

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Cell-free formation of protease-resistant prion protein

The conversion of PrPc to protease-resistant forms similar to PrPSc in a cell-free system composed of substantially purified constituents is reported, providing direct evidence that PrP sc derives from specific PrP c–PrPSc interactions.

Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding

The method could be applied to diagnose the presence of currently undetectable prion infectious agent in tissues and biological fluids, and may provide a unique opportunity to determine whether PrPSc replication results in the generation of infectivity in vitro.

In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups.

Using an in vitro PrP(Sc) amplification technique adapted from protein misfolding cyclic amplification (PMCA), the first evidence that a reactive chemical group plays an essential role in the conformational change from Pr(C) to PrP (Sc) is provided.

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Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms.

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Non-genetic propagation of strain-specific properties of scrapie prion protein

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Purification and properties of the cellular and scrapie hamster prion proteins.

Development of a purification protocol for PrPC should facilitate comparisons of the two PrP isoforms and lead to an understanding of how PrPSc is synthesized either from PrPC or a precursor.

Strain-specific prion-protein conformation determined by metal ions

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