Humanized Transgenic Mice Are Resistant to Chronic Wasting Disease Prions From Norwegian Reindeer and Moose.

Chronic wasting disease (CWD) is the transmissible spongiform encephalopathy or prion disease affecting cervids. In 2016, the first cases of CWD were reported in Europe in Norwegian wild reindeer and moose. The origin and zoonotic potential of these new prion isolates remain unknown.

In vitro amplification of ovine prions from scrapie-infected sheep from Great Britain reveals distinct patterns of propagation.

Background: Protein misfolding cyclic amplification (PMCA) is a method that facilitates the detection of prions from many sources of transmissible spongiform encephalopathy (TSE). Sheep scrapie represents a unique diversity of prion disease agents in a range of susceptible PRNP genotypes. In this study PMCA was assessed on a range of Great Britain (GB) sheep scrapie isolates to determine the applicability to veterinary diagnosis of ovine TSE.

Temperature influences the interaction of ruminant PrP (TSE) with soil.

Ovine scrapie and cervid chronic wasting disease can be transmitted in the absence of animal-to-animal contact, and environmental reservoirs of infectivity have been implicated in their spread and persistence. Investigating environmental factors that influence the interaction of disease-associated PrP with soils is imperative to understanding what is likely to be the complex role of soil in disease transmission. Here, we describe the effects of soil temperature on the binding/desorption and persistence of both ovine scrapie- and bovine BSE-PrP (TSE) .

Differentiating ovine BSE from CH1641 scrapie by serial protein misfolding cyclic amplification.

Whilst ovine BSE displays distinct pathological characteristics to ovine CH1641-like scrapie upon passage in rodents, they have very similar molecular phenotypes. As such, the in vitro differentiation of these strains in routine surveillance programmes presents a significant diagnostic challenge. In this study, using serial protein-misfolding cyclic amplification (sPMCA), ovine BSE was readily amplified in vitro in brain substrates from sheep with V₁₃₆R₁₅₄Q₁₇₁/V₁₃₆R₁₅₄Q₁₇₁ or AHQ/AHQ PRNP genotypes.

Prions are secreted into the oral cavity in sheep with preclinical scrapie.

A major concern in prion disease transmission is the spread of the disease agent by means of secretions and excretions. We analyzed buccal swab samples obtained from preclinical scrapie-infected sheep by concentrating the collected prions on silicon dioxide, followed by amplification by serial protein misfolding cyclic amplification. Data clearly demonstrate that prions are present in buccal swab samples from sheep with a VRQ/VRQ PRNP genotype during preclinical scrapie infection.

In vitro amplification of prions from milk in the detection of subclinical infections.

Prions can be amplified by serial protein misfolding cyclic amplification (sPMCA) from the milk of a high proportion of apparently healthy, scrapie exposed sheep with PRNP genotypes not previously associated with high disease penetrance. These data strongly suggest the widespread presence of subclinical scrapie infections within scrapie-exposed flocks containing sheep with a range of susceptible PRNP genotypes. These data also lead to the hypothesis that similar subclinical disease states may be common for other animal and human prion diseases.

Retrospective study of Campylobacter infection in a zoological collection.

Little is known about the epidemiology of Campylobacter spp. in wild animal populations. However, zoological collections can provide valuable insights.