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Modeling PrPSc Generation Through Deformed Templating.

Giovanni Spagnolli1,2, Marta Rigoli1, Giovanni Novi Inverardi1

  • 1Department of Cellular, Computational and Integrative Biology, Centre for Integrative Biology, University of Trento, Trento, Italy.

Frontiers in Bioengineering and Biotechnology
|October 30, 2020
PubMed
Summary
This summary is machine-generated.

Deformed templating explains how misfolded prion proteins (PrP) can convert to infectious forms (PrPSc). This study models this process, revealing intermediate structures and mechanisms of prion replication.

Keywords:
4RβSPIRIBSPrP amyloidPrPScPrPSc structuredeformed templatingmolecular dynamics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Deformed templating describes the conversion of non-infectious PrP amyloid into infectious PrPSc conformers.
  • This process involves a mismatch between template and substrate under varying conditions.
  • Intermediate conformers emerge during deformed templating, bridging initial and final states.

Purpose of the Study:

  • To develop a molecular model of deformed templating using recent structural data.
  • To investigate the atomistic details of intermediate conformer formation.
  • To elucidate the structural basis of prion replication mechanisms.

Main Methods:

  • Utilized cryo-electron microscopy (cryo-EM) structural data.
  • Employed a proposed atomistic model of PrPSc.
  • Applied molecular modeling and Molecular Dynamics (MD) simulations.

Main Results:

  • Generated a complete molecular model of deformed templating.
  • Created an atomistic model of a glycosylated intermediate conformer.
  • Showed that glycosylated PrP can stack in-register.
  • Identified shared structural motifs between 4-rung β-solenoid (4RβS) and PIRIBS PrP architectures.

Conclusions:

  • The study provides a detailed molecular mechanism for deformed templating.
  • Reveals the structural basis for intermediate conformer formation during prion conversion.
  • Offers insights into the fundamental mechanisms governing prion replication and structural transitions.