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Related Experiment Videos

Selective neuronal targeting in prion disease

S J DeArmond1, H Sánchez, F Yehiely

  • 1Department of Pathology, University of California, San Francisco 94143, USA.

Neuron
|January 14, 1998
PubMed
Summary
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Altering prion protein (PrP(C)) glycosylation in mice impacts scrapie prion (PrP(Sc)) accumulation patterns. Changes to oligosaccharides affect PrP(C) trafficking and susceptibility to prion infection, influencing disease progression.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Scrapie prion protein (PrP(Sc)) accumulation patterns vary with prion strain.
  • The role of Asn-linked oligosaccharides on the cellular prion protein (PrP(C)) in this process is not fully understood.

Purpose of the Study:

  • To investigate how Asn-linked oligosaccharides of PrP(C) influence PrP(Sc) deposition patterns in transgenic mice.
  • To determine the impact of altering PrP(C) glycosylation on prion infection and disease progression.

Main Methods:

  • Generation of transgenic mice with deletions in PrP(C) oligosaccharide attachment sites.
  • Analysis of PrP(Sc) deposition patterns in the brain.
  • Assessment of PrP(C) trafficking and susceptibility to prion infection.

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Main Results:

  • Deletion of the first oligosaccharide attachment site altered PrP(C) trafficking and conferred resistance to two prion strains.
  • Deletion of the second attachment site did not affect PrP(C) trafficking but allowed infection with one strain, profoundly altering PrP(Sc) deposition patterns.
  • Glycosylation appears to influence PrP(C) conformation and its affinity for specific PrP(Sc) conformers.

Conclusions:

  • Asn-linked oligosaccharides on PrP(C) play a critical role in determining PrP(Sc) accumulation patterns.
  • Glycosylation can modify PrP(C) conformation, affecting prion strain propagation and deposition.
  • These findings suggest glycosylation as a potential target for modulating prion diseases.