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The yeast Sup35NM domain propagates as a prion in mammalian cells

Carmen Krammer1, Dmitry Kryndushkin, Michael H Suhre

  • 1Institute of Virology, Technische Universität München, Trogerstrasse 30, 81675 Munich, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|December 31, 2008
PubMed

Insights

Researchers transmitted yeast prions to mammalian cells, demonstrating cross-kingdom prion propagation. This study reveals that mammalian cells can support prion-like inheritance of yeast prion domains.

Area of Science:

  • Molecular Biology
  • Prion Biology
  • Cell Biology

Background:

  • Prions are infectious protein aggregates implicated in neurodegenerative diseases.
  • Understanding prion replication mechanisms is crucial for both mammalian and fungal systems.
  • Yeast prions offer a tractable model for studying prion propagation.

Purpose of the Study:

  • To investigate the aggregation propensity and propagation of a yeast prion domain in a mammalian cell culture.
  • To determine if yeast prions can be artificially transmitted across phylogenetic kingdoms.
  • To explore the potential for prion-like inheritance in mammalian cytosolic environments.

Main Methods:

  • Stable expression of HA epitope-tagged yeast Sup35p prion domain (NM-HA) in murine neuroblastoma cells.
  • Induction of NM-HA aggregation using fibrils of bacterially produced Sup35NM.
  • Phenotypic and biochemical characterization of induced aggregates.
  • Assessment of aggregate inheritance by daughter cells and infectivity to recipient cells (mammalian and yeast).

Main Results:

  • Cytosolically expressed NM-HA remained soluble in neuroblastoma cells without induction.
  • Addition of bacterial Sup35NM fibrils efficiently induced distinct NM-HA aggregates.
  • These induced aggregates were inherited by daughter cells and were infectious to recipient mammalian cells.
  • Cross-kingdom transmission of yeast prion infectivity to mammalian cells was achieved.

Conclusions:

  • The yeast Sup35NM prion domain can propagate as a prion in mammalian neuroblastoma cells.
  • Mammalian cellular mechanisms are capable of supporting prion-like inheritance.
  • This study demonstrates the artificial transmission of a yeast prion across a phylogenetic kingdom, highlighting conserved mechanisms of protein aggregation and propagation.

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