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Cofactor molecules induce structural transformation during infectious prion formation.

Michael B Miller1, Daphne W Wang, Fei Wang

  • 1Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.

Structure (London, England : 1993)
|October 15, 2013
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Cofactor molecules induce major structural changes during prion formation. This dynamic process, studied using deuterium exchange mass spectrometry, results in biologically active prions from recombinant PrP.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Misfolded proteins spread in neurodegenerative diseases.
  • Mammalian prions are uniquely infectious in vitro.
  • Prion formation involves complex protein conformational changes.

Purpose of the Study:

  • To investigate stepwise protein conformational changes during prion formation.
  • To understand the role of cofactors (POPG and RNA) in prion genesis.
  • To elucidate the structural pathway from recombinant PrP to infectious PrP(Sc).

Main Methods:

  • Generation of infectious prions de novo from purified recombinant PrP.
  • Utilizing deuterium exchange mass spectrometry (DXMS) to monitor conformational changes.
  • Employing specific conversion cofactors: palmitoyl-oleoyl-phosphatidylglycerol (POPG) and RNA.

Main Results:

  • POPG induced significant structural alterations in PrP, affecting α helices and β strands.
  • RNA addition led to increased exposure of the PrP N terminus.
  • Conversion to infectious PrP(Sc) showed decreased solvent exposure but retained cofactor-induced features.

Conclusions:

  • Cofactor molecules initiate major structural rearrangements in PrP.
  • Prion formation is a dynamic sequence of conformational changes.
  • These cofactor-driven changes are critical for generating biologically active prions.