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A bacteria-based genetic assay detects prion formation.

Eleanor Fleming1, Andy H Yuan1, Danielle M Heller1

  • 1Department of Microbiology, Blavatnik Institue, Harvard Medical School, Boston, MA 02115.

Proceedings of the National Academy of Sciences of the United States of America
|February 21, 2019
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel genetic assay to detect bacterial prions. This tool identified prion-forming potential in Campylobacter hominis SSB protein, enabling propagation studies.

Keywords:
Escherichia coliSSBSup35prionsprotein-based heredity

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Prions are infectious protein aggregates causing neurodegenerative diseases in mammals.
  • Evidence suggests prions may exist in bacteria, but detection assays are lacking.
  • Evaluating bacterial prion candidates requires robust genetic tools.

Purpose of the Study:

  • To develop a bacteria-based genetic assay for prion detection.
  • To investigate the prion-forming potential of Campylobacter hominis SSB protein.
  • To understand the propagation mechanisms of bacterial prions.

Main Methods:

  • Developed a genetic assay using a model yeast prion protein to distinguish prion and nonprion forms in bacteria.
  • Applied the assay to assess the prion-forming capabilities of Campylobacter hominis SSB.
  • Studied the generational propagation of the prion form and the role of ClpB disaggregase.

Main Results:

  • Successfully established a bacterial genetic assay for prion detection.
  • Identified a prion-forming domain within Campylobacter hominis SSB.
  • Demonstrated stable propagation of the bacterial prion form over 100 generations, dependent on ClpB.

Conclusions:

  • The developed assay effectively distinguishes bacterial prion conformations.
  • Campylobacter hominis SSB protein exhibits prion-forming characteristics.
  • Bacterial prions can be propagated and are influenced by cellular machinery like ClpB.
  • This tool can advance the study of prion-like phenomena across life domains.