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Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria

Bruno Macedo1,2,3, Ricardo Sant'Anna4, Susanna Navarro5,6

  • 1Faculdade de Farmácia, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Av. Carlos Chagas Filho 373, Bloco B, Subsolo, Sala 17, Rio de Janeiro, RJ, 21941-902, Brazil. brunoo_macedo@hotmail.com.

Microbial Cell Factories
|November 6, 2015
PubMed
Abstract

Insights

Mammalian prions, infectious proteins causing disease, can be studied using bacterial amyloid models. This research shows recombinant prion proteins form diverse amyloid structures in bacteria, aiding disease mechanism understanding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Amyloid structures are linked to various pathological states.
  • Mammalian prions are unique infectious agents causing neurodegenerative diseases through protein misfolding.
  • Studying intracellular amyloid aggregation, especially prion-like structures, is challenging.

Purpose of the Study:

  • To demonstrate that recombinant prion proteins can form amyloid structures within bacteria.
  • To investigate the structural diversity and properties of these bacterial amyloid aggregates.
  • To establish bacteria as a model system for studying prion protein amyloidogenesis.

Main Methods:

  • Expression and purification of recombinant murine prion protein (PrP) and its C-terminal domain in bacteria.
  • Analysis of inclusion bodies formed by PrP proteins.
  • Characterization of amyloid properties including fibril morphology, dye binding, stability, proteinase K resistance, and neurotoxicity.

Main Results:

  • Recombinant murine PrP and its C-terminal domain form amyloid conformations inside bacteria.
  • These bacterial amyloid inclusions exhibit significant conformational diversity.
  • Differences were observed in fibril morphology, amyloid dye binding, stability, proteinase K resistance, and neurotoxicity.

Conclusions:

  • Bacterial cell factories can serve as a valuable system for modeling prion protein amyloid formation.
  • This approach offers insights into structural features that influence the pathogenic impact of prion proteins.
  • Further understanding of prion-like amyloidogenesis can be achieved using microbial models.

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