The emergence of a <i>Drosophila</i> model to measure ovine prion infectivity.
2013
Bujdoso, R. | Thackray, A. M.
Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative conditions of humans and various vertebrate species. Scrapie, a naturally occurring prion disease of sheep, is considered to be the prototypic TSE. The transmissible agent responsible for these conditions is a novel infectious particle referred to as a prion that is composed principally, if not solely, of PrPSc an abnormal isomer of the normal host protein PrPC. Prions are a significant risk to public health through their potential for zoonotic transmission, as evidenced by the bovine spongiform encephalopathy epizootic in UK cattle and subsequent emergence of variant Creutzfeldt-Jakob disease in humans. Consequently, much attention has focused on the molecular basis of prion propagation and the measurement of prion infectivity in different tissues and fluids from prion-infected individuals. The goal of such studies is to understand the biology of infectious prions and ensure the safety of animal products destined for human consumption. In this review we discuss aspects of ovine prion infectivity and molecular aspects of ovine PrP in relation to classical and atypical sheep scrapie. In addition, we describe the development of an invertebrate model of transmissible ovine prion disease suitable for the measurement of prion infectivity. In doing so, we highlight the importance of the study of sheep scrapie, not only for the relevance of this condition in the natural host, but also for prion disease research in general.
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