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Updated: Aug 11, 2026
10:17
Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
Published on: April 28, 2010
Prion glycoprotein: structure, dynamics, and roles for the sugars
P M Rudd1, M R Wormald, D R Wing
1Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. pmr@glycob.ox.ac.uk
Biochemistry
|April 13, 2001
Summary
Prion protein
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- The prion protein (PrP) features N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor.
- PrP's N-linked sugars shield its surface, protecting it from proteases and non-specific interactions.
- These sugars may facilitate protein folding through the calnexin pathway in the endoplasmic reticulum.
Purpose of the Study:
- To investigate the role of glycosylation and the GPI anchor in prion protein structure, function, and disease.
- To analyze the glycan composition of prion protein and its implications for strain type and disease transmission.
- To explore the potential role of the GPI anchor in prion protein cell-to-cell translocation.
Main Methods:
- Glycan analysis of prion protein.
- Immunoprecipitation using calnexin.
- Comparison of glycan profiles between PrP(C) and PrP(Sc) in Syrian hamsters.
Main Results:
- Prion protein contains at least 52 different brain-derived sugars with site-specific processing.
- PrP(Sc) exhibits a higher proportion of tri- and tetra-antennary sugars compared to PrP(C), potentially due to decreased GnTIII activity.
- The GPI anchor, modified with sialic acid, may confer mobility in the lipid bilayer.
Conclusions:
- Prion protein glycosylation significantly influences its structural stability and interactions.
- Glycan composition variations may be linked to prion strain diversity and disease pathogenesis.
- The GPI anchor's mobility function could be crucial for prion propagation between cells.
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