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British Medical Bulletin 66:43-60 (2003)
© 2003 The British Council

PrP knock-out and PrP transgenic mice in prion research

C Weissmann and E Flechsig

MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, London, UK
Institut für Virologie und Immunbiologie, Würzburg, Germany

Spongiform encephalopathies such as scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle or Creutzfeldt-Jacob disease (CJD) and Gerstmann-Sträussler-Scheinker syndrome (GSS) in humans is caused by a transmissible agent designated prion. The ‘protein only’ hypothesis proposes that the prion consists partly or entirely of a conformational isoform of the normal host protein PrPC, designated PrP*1 and that the abnormal conformer, when introduced into the organism, causes the conversion of PrPC into a likeness of itself. PrP* may be congruent with PrPSc, a protease-resistant, aggregated conformer of PrP that accumulates mainly in brain of almost all prion-infected organisms.

PrPC consists of a flexible N-terminal half, comprising Cu2+-binding octapeptide repeats, and a globular domain consisting of three {alpha}-helices, one short antiparallel ß-sheet and a single disulphide bond2. It is anchored at the outer cell-surface by a glycosyl phosphatidylinositol (GPI) tail and is present in almost all tissues, however, mainly in brain3.

Compelling linkage between the prion and PrP was established by biochemical and genetic data4–8 and led to the prediction that animals devoid of PrP should be resistant to experimental scrapie and fail to propagate infectivity. This prediction was indeed borne out, adding substantial support to the ‘protein only’ hypothesis. In addition, the availability of PrP knock-out mice provided an approach to carry out reverse genetics9 on PrP, both in regard to prion disease and to its physiological role.


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