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Evolving views in prion glycosylation: functional and pathological implications.

M Ermonval1, S Mouillet-Richard, P Codogno

  • 1Laboratoire de Differenciation Cellulaire et Prions, UPR1983 CNRS, 7, rue Guy-Moquet, 94800 Villejuif, France. ermonval@vjf.cnrs.fr

Biochimie
|May 27, 2003
PubMed
Summary

Prion diseases are transmissible neurodegenerative disorders involving abnormal prion protein (PrPSc). This review explores how cellular prion protein (PrPC) glycosylation impacts its function, disease, and strain diversity.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Prion diseases are fatal neurodegenerative conditions characterized by transmissible, misfolded prion proteins (PrPSc).
  • The normal cellular prion protein (PrPC) is a cell-surface glycoprotein involved in various cellular functions.
  • Key aspects of PrPC function, prion replication, and neurodegeneration remain incompletely understood.

Purpose of the Study:

  • To review the implications of PrPC glycosylation.
  • To elucidate the role of glycosylation in PrPC function and conversion to PrPSc.
  • To explore how glycosylation influences prion strain diversity and neuronal targeting.

Main Methods:

  • This review synthesizes existing research on PrPC structure and function.

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  • It analyzes studies investigating the biochemical properties of PrPC isoforms.
  • The review integrates findings on prion pathogenesis and strain characteristics.

    • Main Results:

    • PrPC exists in various isoforms based on processing, topology, and glycosylation.
    • Glycosylation patterns of PrPC influence its cellular fate and conversion to PrPSc.
    • PrPC glycosylation is implicated in the emergence of distinct prion strains and their selective neurotoxicity.

    Conclusions:

    • PrPC glycosylation is a critical factor in understanding prion disease mechanisms.
    • Targeting PrPC glycosylation may offer therapeutic strategies for prion disorders.
    • Further research into PrPC glycosylation is essential for unraveling prion pathogenesis.