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A viral expression factor behaves as a prion.

Hao Nan1, Hongying Chen1, Mick F Tuite2

  • 1State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, 712100, Yangling, Shaanxi, China.

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|January 22, 2019
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Baculovirus LEF-10 protein acts as a prion, functionally replacing yeast prion domains and inhibiting viral gene expression. This discovery expands prion research to non-cellular life forms, suggesting prions are widespread in nature.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Prions are self-propagating protein conformers found in various species but not previously in viruses.
  • The Sup35 protein from yeast serves as a model for studying prion formation and function.

Purpose of the Study:

  • To investigate whether baculovirus-encoded proteins exhibit prion-like behavior.
  • To determine the functional implications of a viral protein acting as a prion.

Main Methods:

  • Functional replacement assays using the yeast Sup35 protein's prion domain (PrD).
  • In vitro and in vivo studies of baculovirus LEF-10 protein aggregation.
  • Analysis of viral gene expression in infected cells.

Main Results:

  • Baculovirus LEF-10 protein and its candidate prion-forming domain (cPrD) functionally replaced the yeast Sup35 PrD, inducing a [PSI+]-like phenotype.
  • High multiplicity of infection triggered LEF-10 aggregation in infected cells.
  • LEF-10 aggregation led to the inhibition of viral late gene expression.

Conclusions:

  • The baculovirus LEF-10 protein demonstrates prion-forming capabilities, extending the known range of prion proteins to non-cellular life.
  • Viral prions can influence viral gene expression, suggesting a novel regulatory mechanism.
  • Prion-forming proteins are likely a widespread phenomenon across diverse life forms.