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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Structural consequences of sequence variation in mammalian prion β2α2 loop segments.

Calina Glynn1, Evelyn Hernandez1, Marcus Gallagher-Jones1

  • 1Department of Chemistry and Biochemistry, STROBE NSF Science and Technology Center, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA, United States.

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Mammalian prion protein (PrP) β2α2 loop sequence variations influence its structure and amyloid packing. Residue 174 is key, affecting fibril morphology and stability.

Keywords:
cryoEMmicroEDprionstructuretransmission

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • The β2α2 loop of mammalian prion protein (PrP) is crucial for its structure.
  • Sequence variations in this loop can affect protein folding and aggregation.

Purpose of the Study:

  • To investigate how sequence variations in the PrP β2α2 loop impact its structure and amyloid packing.
  • To understand the biochemical and biophysical consequences of natural and artificial loop variants.

Main Methods:

  • Microcrystal electron diffraction (MicroED) was used to determine atomic resolution structures of β2α2 loop segments.
  • Biochemical and biophysical analyses were performed on various PrP loop sequences.
  • Negative stain electron microscopy evaluated fibril morphology of recombinant PrP segments.

Main Results:

  • Two dominant amyloid packing polymorphisms, 'clasped' and 'interdigitated,' were identified.
  • The identity of residue 174 significantly influences the adopted packing.
  • Single residue substitutions in the β2α2 loop impacted fibril morphology.

Conclusions:

  • Prion protein β2α2 loop sequence variations dictate distinct amyloid packing structures.
  • Residue 174 and overall loop sequence are critical for prion assembly stability and morphology.
  • These findings highlight sequence-specific polymorphisms in prion diseases.