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Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity.

Koren Nishina1, Samantha Jenks, Surachai Supattapone

  • 1Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.

The Journal of Biological Chemistry
|July 21, 2004
PubMed
Summary

Misfolded prion protein (PrPSc) conformations are structurally interconvertible. Only protease-resistant PrPSc, influenced by ionic strength and metal ions like copper and zinc, can induce new prion formation.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Infectious prions are composed of misfolded prion protein (PrPSc), derived from normal cellular prion protein (PrPC).
  • The conformational plasticity and conversion activity of PrPSc remain incompletely understood.

Purpose of the Study:

  • To investigate the influence of ionic strength, copper, and zinc on PrPSc conformation, protease resistance, and conversion activity.
  • To determine if PrPSc molecules exist in unique conformations or can undergo further changes.

Main Methods:

  • Examined protease resistance and conversion-inducing activity of PrPSc in scrapie-infected hamster brains.
  • Assessed the effects of varying ionic strength and the addition of copper and zinc ions.
  • Studied purified truncated PrP-(27-30) molecules to identify metal ion binding regions.

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Main Results:

  • PrPSc exhibited increased protease sensitivity at low ionic strength, which was reversed by copper or zinc ions.
  • These metal ions influenced PrPSc conformation independently of the N-terminal octapeptide repeat region.
  • Protease-sensitive and resistant PrPSc conformations were reversibly interconverted.
  • Only high-ionic-strength-induced, protease-resistant PrPSc initiated new protease-resistant PrP (PrPres) formation in vitro.

Conclusions:

  • PrPSc molecules are structurally dynamic and interconvertible.
  • A specific subset of PrPSc conformations, stabilized by environmental factors, is responsible for prion propagation.