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

R. Goold, S. Rabbanian, L. Sutton, R. Andre, P. Arora, J. Moonga, A.R. Clarke, G. Schiavo, P. Jat, J. Collinge and S.J. Tabrizi ()
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R. Goold: Institute of Neurology, University College London, Queen Square
S. Rabbanian: Institute of Neurology, University College London, Queen Square
L. Sutton: Institute of Neurology, University College London, Queen Square
R. Andre: Institute of Neurology, University College London, Queen Square
P. Arora: MRC Prion Unit, Institute of Neurology, University College London, Queen Square
J. Moonga: Institute of Neurology, University College London, Queen Square
A.R. Clarke: MRC Prion Unit, Institute of Neurology, University College London, Queen Square
G. Schiavo: Molecular NeuroPathobiology Group, Cancer Research UK London Research Institute
P. Jat: Institute of Neurology, University College London, Queen Square
J. Collinge: Institute of Neurology, University College London, Queen Square
S.J. Tabrizi: Institute of Neurology, University College London, Queen Square

Nature Communications, 2011, vol. 2, issue 1, 1-11

Abstract: Abstract Prion diseases are fatal neurodegenerative disorders with unique transmissible properties. The infectious and pathological agent is thought to be a misfolded conformer of the prion protein. Little is known about the initial events in prion infection because the infecting prion source has been immunologically indistinguishable from normal cellular prion protein (PrPC). Here we develop a unique cell system in which epitope-tagged PrPC is expressed in a PrP knockdown (KD) neuroblastoma cell line. The tagged PrPC, when expressed in our PrP-KD cells, supports prion replication with the production of bona fide epitope-tagged infectious misfolded PrP (PrPSc). Using this epitope-tagged PrPSc, we study the earliest events in cellular prion infection and PrP misfolding. We show that prion infection of cells is extremely rapid occurring within 1 min of prion exposure, and we demonstrate that the plasma membrane is the primary site of prion conversion.

Date: 2011
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DOI: 10.1038/ncomms1282

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