Scrapie is a naturally occurring transmissible spongiform encephalopathy in sheep and goat. It has been known for ~250 years and is characterised by the accumulation of an abnormal isoform of a host-encoded prion protein that leads to progressive neurodegeneration and death. Scrapie is recognised in two forms, classical and atypical scrapie. The susceptibility to both types of scrapie is influenced by polymorphisms of the prion protein gene (PRNP). Sheep susceptibility or resistance to classical scrapie is strongly regulated by the polymorphisms at codons 136, 154 and 171 of the PRNP. The genetic role in atypical scrapie in sheep has been defined by polymorphisms at codons 141, 154 and 171, which are associated with different degrees of risk in the occurrence of the ovine disease. Progress has been achieved in the prevention of scrapie in sheep due to efficient genetic breeding programmes based on eradication and control of the disease. In Europe, the success of these programmes has been verified by applying eradication and genetic selection plans. In general terms, the ovine selection plans aim to eliminate and reduce the susceptible allele and to enrich the resistant allele ARR. During outbreaks all susceptible animals are slaughtered, only ARR/ARR resistant rams and sheep and semi-resistant females are preserved. In the occurrence of scrapie positive goats a complete cull of the flock (stamping out) is performed with great economic loss and severe risk of extinction for the endangered breeds. The ability to select scrapie-resistant animals allows to define new breeding strategies aimed to boost genetic progress while reducing costs during scrapie outbreaks. Allelic variants of PRNP can be protective for caprine scrapie, and the knowledge of their distribution in goats has become very important. Over the past few years, the integration of genetic information on goat populations could be used to make selection decisions, commonly referred to as genetic selection. The objective of this review was to summarise the main findings of polymorphisms of the caprine prion protein (PrP) gene and to discuss the possible application of goat breeding schemes integrating genetic selection, with their relative advantages and limitations.

It has recently been discovered that lichens contain a serine protease capable of degrading the pathogenic prion protein, the etiological agent of prion diseases such as sheep scrapie and cervid chronic wasting disease. Limited methods are available to degrade or inactivate prion disease agents, especially in the environment, and lichens or their serine protease could prove important for management of these diseases. Scant information is available regarding the presence or absence of the protease responsible for degrading prion protein (PrP) in lichen species and, in this study, we tested the hypothesis that PrP degradation activity in lichens is phylogenetically-based by testing 44 species of Cladonia lichens, a genus for which a significant portion of the phylogeny is well established. We categorized PrP degradation activity among the 44 species (high, moderate, low or none) and found that activity in Cladonia species did not correspond with phylogenetic position of the species. Degradation of PrP did correspond, however, with three classical taxonomic characters within the genus: species with brown apothecia, no usnic acid, and the presence of a cortex. Of the 44 species studied, 18 (41%) had either high or moderate PrP degradation activity, suggesting the protease may be frequent in this genus of lichens.

The risk of classical scrapie in sheep is associated with polymorphisms in the prion protein (PrP) gene. In recent years, large-scale selective breeding programmes for sheep at lower risk of disease have been undertaken across the European Union. We analysed large-scale datasets on scrapie and sheep demography to investigate additional effects of sheep breed on scrapie risk. There was evidence for variation between certain breeds in the scrapie risk of some PrP genotypes, which could be caused by innate breed differences or distinct scrapie strains circulating within them. While the PrP genotypes of cases are generally consistent across breeds, some exceptions provide evidence that scrapie strain may influence affected PrP genotypes to a greater extent than innate breed differences. There was a significant association between the breed-level incidence of scrapie and the frequency of susceptible PrP genotypes in breeds. Our results lend support to selective breeding programmes which aim to reduce the frequency of high-risk PrP genotypes with measures not varying by sheep breed.

Extensive surveillance for classical scrapie has been carried out in Great Britain since 1993, the results of which can be used for monitoring the effect of control measures introduced since 2001. A back-calculation approach was used to estimate the prevalence of sheep infected with classical scrapie, which integrates data on reported clinical cases (1993–2007) and the results of fallen stock and abattoir surveys (2002–2007). The prevalence of classical scrapie in GB was fairly constant until 2003, although the estimates depended on assumptions made about the performance of diagnostic tests used in the surveys. If infected animals could be detected in the final quarter of the incubation period, the estimated prevalence was 0·6–0·7%, while if they could be detected in the final half of the incubation period, it was 0·3–0·4%. Between 2003 and 2007 the prevalence declined by around 40%, and the magnitude of the reduction was independent of assumptions made about the diagnostic tests.

Transmissible spongiform encephalopathies (TSEs) are a family of neurodegenerative diseases characterized by their long incubation periods, progressive neurological changes, and spongiform appearance in the brain. There is much evidence to show that TSEs are caused by an isoform of the normal cellular surface prion protein PrPC. The normal function of PrPC is still unknown, but it exhibits properties of a cupro-protein, capable of binding up to six copper ions. There are two differing views on copper's role in prion diseases. While one view looks at the PrPC copper-binding as the trigger for conversion to PrPSc, the opposing viewpoint sees a lack of PrPC copper-binding resulting in the conformational change into the disease causing isoform. Manganese and zinc have been shown to interact with PrPC as well and have been found in abnormal levels in prion diseases. This review addresses the interaction between select trace elements and the PrPC.

The objective of this study was to analyse the associations between ovine prion protein (PrP) genotypes and reproduction traits in three German meat sheep breeds. Reproduction traits were age at first early lambing, age at first late lambing, first lambing interval, second lambing interval and total number of lambs born. The data set included 595 genotyped German Texel sheep among 5225 recorded sheep, 351 genotyped German Black-Headed Mutton among 10 177 sheep and 282 genotyped Suffolk sheep among 2849 sheep. Linear animal models were employed for the analysis of the PrP-genotype effect. The PrP-genotype effect was analysed by comparing the most frequent PrP genotypes ARR/ARR, ARR/ARQ, and ARQ/ARQ. In a more general analysis three PrP genotype classes of animals with two, one or no copy of the ARR allele were compared.

In most cases, no significant associations were found between the PrP genotypes and the reproduction traits investigated. Only for the traits age at first early lambing in German Texel and second lambing interval in German Black-Headed Mutton and Suffolk could a significant association with the PrP genotype be observed.