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Glycosylation differences between the normal and pathogenic prion protein isoforms.

P M Rudd1, T Endo, C Colominas

  • 1Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|November 11, 1999
PubMed
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Prion protein (PrP) glycoforms are structurally similar in normal (PrP(C)) and pathogenic (PrP(Sc)) states, but their proportions differ. Altered N-acetylglucosaminyltransferase III (GnTIII) activity impacts prion disease pathogenesis.

Area of Science:

  • Glycobiology
  • Neuroscience
  • Molecular Biology

Background:

  • Prion protein (PrP) exists as various glycosylated forms (glycoforms).
  • Cellular events and disease states can alter protein glycosylation patterns.
  • Oligosaccharide processing enzymes are sensitive to cellular conditions.

Purpose of the Study:

  • To investigate the N-linked oligosaccharide structures of normal (PrP(C)) and pathogenic (PrP(Sc)) prion proteins.
  • To determine if specific glycoforms are preferentially converted to the pathogenic form.
  • To explore the role of glycosylation machinery alterations in prion disease.

Main Methods:

  • Analysis of N-linked oligosaccharides from Syrian hamster PrP(C) and PrP(Sc) using mass spectrometry.
  • Quantification of individual glycan structures and their relative proportions.

Related Experiment Videos

  • Inference of enzyme activity changes based on glycan profile alterations.

    • Main Results:

    • PrP(C) and PrP(Sc) share a common set of at least 52 N-linked oligosaccharides.
    • The relative proportions of these glycans differ between PrP(C) and PrP(Sc).
    • PrP(Sc) shows reduced bisecting GlcNAc residues and increased tri-/tetra-antennary sugars compared to PrP(C).

    Conclusions:

    • Prion conversion is not limited to specific glycoforms.
    • A decrease in N-acetylglucosaminyltransferase III (GnTIII) activity occurs during PrP(Sc) formation.
    • Perturbation of glycosylation machinery, specifically reduced GnTIII activity, is linked to prion disease pathogenesis and replication.