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Rapid cell-surface prion protein conversion revealed using a novel cell system.

R Goold1, S Rabbanian, L Sutton

  • 1Department of Neurodegenerative Disease, Institute of Neurology, University College London, Queen Square, London WC1N 3BG, UK.

Nature Communications
|April 21, 2011
PubMed
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Prion diseases are rapidly initiated within 1 minute of exposure. This study reveals the plasma membrane as the primary site for prion conversion, using a novel epitope-tagged prion protein system.

Area of Science:

  • Neurodegenerative diseases
  • Prion biology
  • Cellular microbiology

Background:

  • Prion diseases are fatal neurodegenerative conditions.
  • The infectious agent is a misfolded prion protein (PrPSc).
  • Early prion infection events remain poorly understood due to the difficulty in distinguishing PrPSc from normal cellular prion protein (PrPC).

Purpose of the Study:

  • To develop a novel cell system for studying early prion infection events.
  • To investigate the kinetics and cellular location of prion conversion.
  • To characterize the earliest molecular events in prion pathogenesis.

Main Methods:

  • Development of a neuroblastoma cell line with prion protein (PrP) knockdown (KD).
  • Expression of epitope-tagged PrPC in PrP-KD cells to support prion replication.

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  • Utilizing epitope-tagged PrPSc to track initial prion infection and misfolding events.

    • Main Results:

    • Prion replication and production of epitope-tagged PrPSc were achieved in the engineered cell system.
    • Cellular prion infection was observed to be extremely rapid, occurring within 1 minute of prion exposure.
    • The plasma membrane was identified as the primary site for prion conversion.

    Conclusions:

    • The developed cell system enables the study of early prion infection dynamics.
    • Prion conversion is a rapid process initiated at the cell surface.
    • These findings provide critical insights into the initial molecular mechanisms of prion diseases.