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Amyloid core formed of full-length recombinant mouse prion protein involves sequence 127-143 but not sequence 107-126

Biswanath Chatterjee1, Chung-Yu Lee, Chen Lin

  • 1Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.

Plos One
|July 12, 2013
PubMed

Insights

Prion protein conversion into disease-associated PrP(Sc) involves structural changes and amyloid formation. Research identified the 127-143 peptide segment as crucial for amyloid core formation in mouse prion protein (mPrP).

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Prion diseases stem from the misfolding of cellular prion protein (PrP(C)) into pathogenic PrP(Sc) isoforms.
  • This structural conversion involves a shift from alpha-helical to beta-sheet content, leading to amyloid aggregate formation.
  • In vitro studies suggest various proteins and peptides can form amyloid under specific conditions.

Purpose of the Study:

  • To pinpoint the specific peptide segment within recombinant mouse prion protein (mPrP(23-230)) responsible for forming the amyloid core.
  • To investigate the role of different prion peptide segments in seeding the amyloidogenesis of full-length recombinant prion protein.

Main Methods:

  • Seed-induced amyloid formation assays were performed using recombinant mouse prion protein (mPrP(23-230)).
  • Seeds were generated from short prion peptides: mPrP(107-143), mPrP(107-126), and mPrP(127-143).
  • The ability of these peptide seeds to induce amyloidogenesis in mPrP(23-230) was assessed.

Main Results:

  • Amyloid fibrils formed from mPrP(107-143) and mPrP(127-143) successfully seeded amyloidogenesis of mPrP(23-230).
  • Amyloid fibrils generated from mPrP(107-126) did not seed mPrP(23-230) amyloid formation.
  • These findings indicate that the 127-143 sequence segment is integral to the amyloid core of mPrP(23-230).

Conclusions:

  • The prion protein segment spanning residues 127-143 is essential for the formation of the amyloid core during the fibrillization of mPrP(23-230).
  • This research clarifies the structural basis of prion amyloid formation, contributing to understanding prion disease pathogenesis.

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