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

Carlo Fasano1, Vincenza Campana, Chiara Zurzolo

  • 1Unité de Trafic Membranaire et Pathogénése, Institut Pasteur, 75724 Paris Cedex 15, France.

Journal of Molecular Neuroscience : MN
|November 7, 2006
PubMed

Insights

Transmissible spongiform encephalopathies (TSEs) are caused by prions, which are misfolded proteins. This review explores cellular factors crucial for prion protein conversion, a process previously difficult to replicate in vitro.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases in humans and animals.
  • These diseases are caused by infectious agents known as prions, which are misfolded forms of the cellular prion protein (PrP(C)).
  • The conversion of PrP(C) to the infectious PrP(Sc) form is central to prion disease pathogenesis.

Purpose of the Study:

  • To review recent findings on cellular factors involved in prion protein conformational conversion.
  • To explore potential mechanisms by which these cellular factors facilitate prion replication.
  • To address the challenges in replicating prion conversion in vitro and the role of host factors.

Main Methods:

  • This review synthesizes findings from various experimental studies.
  • It discusses proposed models for prion protein conversion.
  • It highlights the importance of cellular co-factors in prion pathogenesis.

Main Results:

  • Recent research suggests that cellular factors are necessary for efficient prion protein conversion.
  • These factors may act as catalysts or chaperones in the misfolding process.
  • Understanding these factors is key to deciphering prion replication mechanisms.

Conclusions:

  • Cellular factors play a critical role in the conformational conversion of prion proteins.
  • Further research into these factors is essential for developing therapeutic strategies against TSEs.
  • The in vitro replication of prion conversion likely requires the presence of specific host-derived co-factors.

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