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The amyloid properties of RAD51 imply that aberrant protein-based assemblies could potentially affect DNA lesions, thus providing a possible link between protein-based and DNA-based transmission machineries. The authors highlight the biological functions of amyloids formed by proteins containing -barrel domains and discuss probable pathways of amyloid formation by such proteins. The review critically assesses existing diagnostic techniques and explains how the principles and procedures derived from studying transmissible amyloids could be applied to clinical and pre-clinical detection of amyloids involved in other diseases, such as renal amyloids. While some of cases of amyloid-associated diseases are heritable (that is, derived from DNA mutations), the majority of cases are sporadic, and prion-like transmissibility of protein assemblies has been observed at a cellular level and, in some experimental models, even at the organismal level [[14], [16]]. [Extracted from the article]

Bovine spongiform encephalopathy (BSE) is a prion disease that is always fatal in cattle and is considered an important risk factor for human health. Genetic polymorphisms that alter prion proteins may be associated with susceptibility or resistance to infectious spongiform encephalopathy. Therefore, we investigated the distribution of the 23 bp indel variant in the prion protein (PRNP) gene in Jersey cattle in Turkey. A total of 95 unrelated Jersey cattle (79 of reproductive age and 16 of non-reproductive age) from a private farm in Izmir were included in the study. Genomic DNA was obtained from the milk of reproductive-age cattle and the saliva of non-reproductive-age cattle. A 23-bp indel polymorphism in the PRNP gene promoter region was genotyped by polymerase chain reaction (PCR) analysis. The three genotypes of the PRNP 23-bp indel variant were classified as follows: I/I (223 bp), I/D (both 223 and 200 bp fragments), and D/D (200 bp). The frequencies of the I/I, I/D, and D/D genotypes of the PRNP 23-bp indel variant in cattle were 22 (23.16%), 48 (50.53%), and 25 (26.32%). We then examined genotype and allele distribution according to service period. No significant difference was detected in terms of PRNP gene 23 bp-indel variant genotype and allele distribution in the groups created according to the service period (p>0.05). Although the PRNP gene 23 bp-indel variant genotype and allele distribution in jersey-type cattle in Turkey did not differ according to service period, our results may benefit the understanding of the genetic characteristics of the PRNP gene in cattle breeds. [ABSTRACT FROM AUTHOR]

Yoon also added, " I For now i [emphasis added] the ROK and the US are proceeding with discussion regarding the ROK side sharing information, participating together, joint planning, and joint execution [with the US] - regarding concerns on US nuclear assets."[31] The statement suggested that while South Korea accepted US extended deterrence at present, other nuclear options were still on the table for the future. In meetings with their US counterparts, South Korean policymakers have repeatedly raised the same question: can South Korea trust the United States? Strengthening the US-South Korea Alliance The year 2023 marks the 70 SP th sp anniversary of the US-South Korea alliance. [Extracted from the article]

The purpose of this research is to demonstrate the utilization of animal wastes and by‐products in the production of low‐energy and low‐CO2 clinkers and cements in order to preserve natural resources, such as limestone, while reducing CO2 emissions released from the cement manufacturing process and reducing potential health risk to the world population (such as bovine spongiform encephalopathy or other health issues...). Pure calcium sulfoaluminate clinker was produced with calcium hydroxide, aluminum hydroxide, and calcium sulfate hemihydrate; followed by additional clinkers produced from substituting calcium hydroxide with bone ash (from 0 to 100% of the calcium hydroxide replaced). The final clinkers contained various amounts of ye'elimite, calcium aluminate phases, as well as tricalcium phosphate, depending on the firing temperature. Finally, some preliminary results on the hydration process and compressive strength are provided for the production of these binders. [ABSTRACT FROM AUTHOR]

Agustina Bazterrica's I Tender is the Flesh i portrays a world in which farming humans for their meat has become the norm. As humans intrude on the natural environments of nonhuman animals, progressively consume more animals, and live in close proximity with animals, so too do animals more commonly become vectors of disease.[8] Second, the viral outbreak in the narrative is often understood in Malthusian terms; that is, many suggest it is the result of overpopulation. This passage not only questions the distinctions between humans and primates, as Marcos cannot determine whether the bones are from a human or nonhuman animal, but it also removes barriers between human and animal as Marcos walks into the enclosure. [Extracted from the article]

The novel emergence of variant Creutzfeldt-Jakob disease (vCJD) in the United Kingdom in 1995/96 as a result of the transmission of bovine spongiform encephalopathy (BSE) agents from cattle to humans triggered a previously unprecedented crisis in Europe at the interface of animal health and human public health. This prompted Germany to reconsider, among other things, the practice of reprocessing medical devices with regard to the unconventional BSE/ vCJD pathogens, so-called prions (from “proteinaceous infectious particles”). In 2002, a vCJD task force set up with this objective presented recommendations for minimizing/reducing the risk of vCJD transmission through surgical instruments and other medical devices. According to these recommendations, routine reprocessing should combine at least two procedures that are also (at least partially) suitable for decontamination/inactivation of these pathogens if there is no identifiable risk of contamination with prions. In practice, this includes in particular careful cleaning (decontamination), preferably with alkaline detergents, and subsequent sterilization with moist heat (“steam sterilization”) at 134°C with a holding time of 5 minutes. The validation of the processes is of great importance. From today’s point of view, the central recommendations of the vCJD Task Force for medical device reprocessing have proven to be sustainable with good practicability. The effectiveness of the recommended measures against prions has been confirmed on a broad basis in numerous studies. In line with the paradigmatically high demands that prions place on hygiene in the reprocessing of medical devices, this effectiveness in practice extends simultaneously to conventional pathogens such as bacteria, viruses or fungi. In perspective, this also applies at least in part to potential new challenges, such as those that have been discussed for some time with regard to self-replicating protein particles of Alzheimer’s or Parkinson’s disease and other protein aggregation diseases. [ABSTRACT FROM AUTHOR]

Prion diseases are a novel class of infectious disease based in the misfolding of the cellular prion protein (PrPC) into a pathological, self-propagating isoform (PrPSc). These fatal, untreatable neurodegenerative disorders affect a variety of species causing scrapie in sheep and goats, bovine spongiform encephalopathy (BSE) in cattle, chronic wasting disease (CWD) in cervids, and Creutzfeldt-Jacob disease (CJD) in humans. Of the animal prion diseases, CWD is currently regarded as the most significant threat due its ongoing geographical spread, environmental persistence, uptake into plants, unpredictable evolution, and emerging evidence of zoonotic potential. The extensive efforts to manage CWD have been largely ineffective, highlighting the need for new disease management tools, including vaccines. Development of an effective CWD vaccine is challenged by the unique biology of these diseases, including the necessity, and associated dangers, of overcoming immune tolerance, as well the logistical challenges of vaccinating wild animals. Despite these obstacles, there has been encouraging progress towards the identification of safe, protective antigens as well as effective strategies of formulation and delivery that would enable oral delivery to wild cervids. In this review we highlight recent strategies for antigen selection and optimization, as well as considerations of various platforms for oral delivery, that will enable researchers to accelerate the rate at which candidate CWD vaccines are developed and evaluated. [ABSTRACT FROM AUTHOR]

Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative disease that belongs to a group of diseases known as transmissible spongiform encephalopathies (TSEs). It is believed that the infectious agent responsible for prion diseases is abnormally folded prion protein (PrPSc), which derives from a normal cellular protein (PrPC), which is a cell surface glycoprotein predominantly expressed in neurons. There are three different types of BSE, the classical BSE (C-type) strain and two atypical strains (H-type and L-type). BSE is primarily a disease of cattle; however, sheep and goats also can be infected with BSE strains and develop a disease clinically and pathogenically indistinguishable from scrapie. Therefore, TSE cases in cattle and small ruminants require discriminatory testing to determine whether the TSE is BSE or scrapie and to discriminate classical BSE from the atypical H- or L-type strains. Many methods have been developed for the detection of BSE and have been reported in numerous studies. Detection of BSE is mainly based on the identification of characteristic lesions or detection of the PrPSc in the brain, often by use of their partial proteinase K resistance properties. The objective of this paper was to summarize the currently available methods, highlight their diagnostic performance, and emphasize the advantages and drawbacks of the application of individual tests. [ABSTRACT FROM AUTHOR]

Since prion diseases share many molecular features with other neurodegenerative disorders that involve prion-like mechanisms, outcomes from prion research have the potential to cross-fertilize progress in such diseases. Prion diseases are fatal and infectious neurodegenerative disorders and prototypic conformational diseases. Whereas in prion diseases, a bona fide infectious agent (prion) propagates and spreads within and between individuals, prion-like mechanisms are limited to seeded conversion and spread of disease-causing protein aggregates from cell to cell within a host. Real-time quaking-induced conversion (RT-QuIC) is an ultrasensitive in vitro prion amplification method that uses recombinant prion protein (substrate) for real-time detection of prion seeds (template). [Extracted from the article]

Prion diseases are fatal infectious neurodegenerative disorders and prototypic conformational diseases, caused by the conformational conversion of the normal cellular prion protein (PrPC) into the pathological PrPSc isoform. Examples are scrapie in sheep and goat, bovine spongiform encephalopathy (BSE) in cattle, chronic wasting disease (CWD) in cervids, and Creutzfeldt–Jacob disease (CJD) in humans. There are no therapies available, and animal prion diseases like BSE and CWD can negatively affect the economy, ecology, animal health, and possibly human health. BSE is a confirmed threat to human health, and mounting evidence supports the zoonotic potential of CWD. CWD is continuously expanding in North America in numbers and distribution and was recently identified in Scandinavian countries. CWD is the only prion disease occurring both in wild and farmed animals, which, together with extensive shedding of infectivity into the environment, impedes containment strategies. There is currently a strong push to develop vaccines against CWD, including ones that can be used in wildlife. The immune system does not develop a bona fide immune response against prion infection, as PrPC and PrPSc share an identical protein primary structure, and prions seem not to represent a trigger for immune responses. This asks for alternative vaccine strategies, which focus on PrPC-directed self-antibodies or exposure of disease-specific structures and epitopes. Several groups have established a proof-of-concept that such vaccine candidates can induce some levels of protective immunity in cervid and rodent models without inducing unwanted side effects. This review will highlight the most recent developments and discuss progress and challenges remaining. [ABSTRACT FROM AUTHOR]

Chronic wasting disease (CWD) strains present a novel challenge to defining and mitigating this contagious prion disease of deer, elk, moose, and reindeer. Similar to strains of other prion diseases (bovine spongiform encephalopathy, sheep scrapie), CWD strains can affect biochemical and neuropathological properties of the infectious agent, and importantly interspecies transmission. To date, ten CWD strains have been characterized. The expanding range of CWD in North America and its presence in South Korea as well as Scandinavian countries will potentially result in millions of cervids infected with CWD; thus, novel strains will continue to emerge. In this review, we will summarize the characteristics of known CWD strains and describe the impact of prion protein gene polymorphisms on the generation of strains. We will also discuss the evidence that individual cervids can harbor more than one CWD strain, complicating strain analysis, and affecting selection and adaptation of strains in new hosts. [ABSTRACT FROM AUTHOR]

An interview with Jeffrey Whitsett, neonatologist and pulmonary biologist at the Cincinnati Children's Hospital in Ohio, is presented. Whitsett talks about his decision to go to medical school and to pursue pulmonary biology and neonatology. He discusses continuous positive airway pressure (CPAP), calcium signaling and placentral biology, and his role in the early days of surfactant replacement therapy.

Prion diseases are transmissible neurodegenerative disorders that affect humans and ruminant species consumed by humans. Ruminant prion diseases include bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep and goats and chronic wasting disease (CWD) in cervids. In 1996, prions causing BSE were identified as the cause of a new prion disease in humans; variant Creutzfeldt-Jakob disease (vCJD). This sparked a food safety crisis and unprecedented protective measures to reduce human exposure to livestock prions. CWD continues to spread in North America, and now affects free-ranging and/or farmed cervids in 30 US states and four Canadian provinces. The recent discovery in Europe of previously unrecognized CWD strains has further heightened concerns about CWD as a food pathogen. The escalating CWD prevalence in enzootic areas and its appearance in a new species (reindeer) and new geographical locations, increase human exposure and the risk of CWD strain adaptation to humans. No cases of human prion disease caused by CWD have been recorded, and most experimental data suggest that the zoonotic risk of CWD is very low. However, the understanding of these diseases is still incomplete (e.g., origin, transmission properties and ecology), suggesting that precautionary measures should be implemented to minimize human exposure. [ABSTRACT FROM AUTHOR]

Following the bovine spongiform encephalopathy (BSE) in 2001, processed animal proteins (PAPs) reintroduction is envisaged in non-ruminant feed thanks to their high protein content, easy availability and cost-effective characteristics. PAPs must be submitted to rendering practices, providing sterilization of products, under standardized conditions of temperature and pressure, according to Regulation (EC) No 142/2011. However, the chemical risk associated to these raw materials has been never evaluated. The aim of this study was to develop and validate a reliable liquid chromatography tandem mass spectrometry (LC–MS/MS) method for the determination and quantification of tetracycline residues in PAPs at µg kg−1 level. The LC–MS/MS method performances were evaluated in terms of specificity, linearity (25–500 µg kg−1), limit of quantitation (LOQ) (25 µg kg−1), accuracy and precision (CV% < 25%), uncertainty, recovery (80–120%) and ruggedness. All the evaluated parameters fulfilled the analytical performance criteria, and the validated LC–MS/MS method fits for purpose as confirmatory method on the occurrence of residues (µg kg−1) of tetracyclines in PAPs. PAPs are a powerful product which could be used both as raw materials in feed and in organic fertilizer production in a circular economy context. Therefore, the lack of regulation and control over antibiotic occurrence should be implemented to avoid a misuse and an increment of antibiotic resistance pressure over the environment and to ensure safety of the feed and food chain. [ABSTRACT FROM AUTHOR]

Bovine spongiform encephalopathy (BSE) belongs to the group of transmissible spongiform encephalopathies and is associated with the accumulation of a pathological isoform of the host-encoded glycoprotein, designated prion protein (PrPSc). Classical BSE (C-type) and two atypical BSE forms (L- and H-type) are known, and can be discriminated by biochemical characteristics. The goal of our study was to identify type-specific PrPSc profiles by using Immunohistochemistry. In our study, brain samples from 21 cattle, intracerebrally inoculated with C-, H-, and L-type BSE, were used. In addition, the corresponding samples from three orally C-type BSE infected animals were also included. From all animals, a lesion and PrPSc-profiles of six brain regions were determined. The lesion profile and the neuroanatomical distribution of PrPSc was highly consistent between the groups, but the immunohistochemical analysis revealed a distinct PrPSc profile for the different BSE-types, which included both the topographic and cellular pattern of PrPSc. This qualitative and quantitative analysis of PrPSc affected structures sheds new light into the pathogenesis of the different BSE types. Furthermore, immunohistochemical characterization is supported as an additional diagnostic tool in BSE surveillance programs, especially when only formalin-fixed tissue samples are available. [ABSTRACT FROM AUTHOR]

Bovine Spongiform Encephalopathy (BSE) has a place with the uncommon cluster of continuously progressive neurological infections identified as Transmissible Spongiform Encephalopathies (TSEs). TSE sicknesses are described by long incubation periods ranging from a while for transmissible mink encephalopathy, to several years for BSE. TSE consistence testaments are a sort of CEP (Certificate of Suitability). During the 1980s, when the principal TSE pandemic happened, researchers started centering a greater amount of their time and work to figure out these circumstances. By 1996, a connection between the human type of mad cow illness, Creutzfeldt-Jakob infection, and BSE from ingestion of meat was found. With the connection between BSE and Creutzfeldt-Jakob being found, researchers affirmed that level transmission of TSEs from animals to people can happen. This is of extraordinary concern while working with specific animal-derived reagents in the lab since there is right now no fix or treatment for TSEs. Research recommends that TSEs are brought about by a strange variant of a protein called a prion (prion is short for proteinaceous irresistible molecule). Prion isoforms of the Prion Protein (PrP), are conjectured as the reason for transmissible spongiform encephalopathies, including scrapie, Chronic Wasting Disease (CWD), bovine spongiform encephalopathy and Creutzfeldt-Jakob Infection (CJD). Numerous materials utilized in labs are engineered or gotten from creature tissues that don't represent a gamble of getting a prion illness so not all items will be TSE ensured. [ABSTRACT FROM AUTHOR]

Background: Bovine spongiform encephalopathy (BSE) is a prion disease that is always fatal in cattle and is considered an important risk factor for human health. Genetic polymorphisms that alter prion proteins may be associated with susceptibility or resistance to infectious spongiform encephalopathy. Therefore, we investigated the distribution of the 23 bp indel variant in the prion protein (PRNP) gene in Jersey cattle in Turkey. Methods: A total of 95 unrelated Jersey cattle (79 of reproductive age and 16 of non-reproductive age) from a private farm in Izmir were included in the study. Genomic DNA was obtained from the milk of reproductive-age cattle and the saliva of non-reproductive-age cattle. A 23-bp indel polymorphism in the PRNP gene promoter region was genotyped by polymerase chain reaction (PCR) analysis. Results: The three genotypes of the PRNP 23-bp indel variant were classified as follows: I/I (465 bp), I/D (306 bp) and D/D (both 465 and 306 bp fragments). The frequencies of the I/I, I/D, and D/D genotypes of the PRNP 23-bp indel variant in cattle were 22 (23.16%), 48 (50.53%), and 25 (26.32%). We then examined genotype and allele distribution according to service period. No significant difference was detected in terms of PRNP gene 23 bp-indel variant genotype and allele distribution in the groups created according to the service period (p>0.05). Conclusion: Although the PRNP gene 23 bp-indel variant genotype and allele distribution in jersey-type cattle in Turkey did not differ according to service period, our results may benefit the understanding of the genetic characteristics of the PRNP gene in cattle breeds.

This article discusses a quality improvement study conducted at Royal Victoria Hospital and Belfast City Hospital in Belfast, Northern Ireland. The study aimed to assess the effectiveness of a short learning module on Creutzfeldt-Jakob disease (CJD) and variant Creutzfeldt-Jakob disease (vCJD) for endoscopy nurses. Pre- and post-module surveys were used to measure the self-reported improvement in nurse understanding of the diseases. The results showed a significant increase in knowledge confidence among the nurses after completing the module. The study concludes that the education module was effective in informing nurses about CJD and the reasons for implementing policies for at-risk patients. [Extracted from the article]

To reduce the transmission risk of bovine spongiform encephalopathy prions (PrPBSE), specified risk materials (SRM) that can harbour PrPBSE are prevented from entering the feed and food chains. As composting is one approach to disposing of SRM, we investigated the inactivation of PrPBSE in lab-scale composters over 28 days and in bin composters over 106–120 days. Lab-scale composting was conducted using 45 kg of feedlot manure with and without chicken feathers. Based on protein misfolding cyclic amplification (PMCA), after 28 days of composting, PrPBSE seeding activity was reduced by 3–4 log10 with feathers and 3 log10 without. Bin composters were constructed using ~ 2200 kg feedlot manure and repeated in 2017 and 2018. PMCA results showed that seeding activity of PrPBSE was reduced by 1–2 log10 in the centre, but only by 1 log10 in the bottom of bin composters. Subsequent assessment by transgenic (Tgbov XV) mouse bioassay confirmed a similar reduction in PrPBSE infectivity. Enrichment for proteolytic microorganisms through the addition of feathers to compost could enhance PrPBSE degradation. In addition to temperature, other factors including varying concentrations of PrPBSE and the nature of proteolytic microbial populations may be responsible for differential degradation of PrPBSE during composting. [ABSTRACT FROM AUTHOR]

This research was organized in order to reveal people's organic plant and animal production, product, information, and consumption habits. In this study, a survey was applied to 399 people. In the study, while 95.0% of the participants knew about organic agriculture, 5.0% reported that they had no information. Do you think the food consumed is safe? The most frequently answered question was sometimes (33.8%), and the rate of those who answered no was 15.3%. They stated that the most important food risk was chemicals (60.4%), GMOs, mad cow disease, and radiation applications, and the least amount (16.0%) was microorganisms. Considering the rate of those who read the labels on the food, 55.1% answered sometimes; 4.5% stated that they have never read. When asked whether organic food is more reliable, 77.9% replied yes. It was determined that 80.2% of the participants consumed organic products. When consumers were asked what their reasons were for not buying organic products, 55.9% said they did not trust that it was organic, 12.8% did not believe that it would bring any additional benefit, and 9.8% said it had a high price. Participants stated that they had heard of the concept of organic feed (84.2%) before, and that the conditions of the shelter affected the quality of animal products (97.5%). It has been observed that the participants are willing to pay more for organic, reliable, and healthy products (78.7%), and they pay attention to being a well-known brand (82.0%) when buying organic animal products. [ABSTRACT FROM AUTHOR]

In 2008, the South Korean government decided to resume importing beef from the United States, which had been stopped since 2003. The government's attempt to reassure citizens with scientific claims met severe resistance, resulting in a whirlwind of political and technoscientific controversies over risks of bovine spongiform encephalopathy (BSE). This article examines memories of protests in 2008 with two objectives; first, to discuss how sub-politics evolves when matters of concern become matters of fact and second, to better understand the aftermath of Korean BSE controversies. Thirty-eight semi-structured interviews with proponents and opponents of the BSE protests were conducted in 2019 and analyzed. Focusing on the complicated discursive struggles over science, society, and their relations, we demonstrated that, along with what people widely accept as the "facts" about US beef, a modern imaginary of science and politics as two separate spheres was reconstructed in Korea. [ABSTRACT FROM AUTHOR]

Establishing a system of Networks of organisations operating in the fields within EFSA's mission is among the tasks of EFSA, according to Regulation (EC) No 178/2002, in order to facilitate a scientific cooperation framework by the coordination of activities, the exchange of information, the development and implementation of joint projects, the exchange of expertise and best practices. The EFSA Scientific Network on bovine spongiform encephalopathies and other transmissible spongiform encephalopathies (BSE‐TSE) was established in 2006 and held its 17th annual meeting on 13‐14 October 2022, as a hybrid meeting. The meeting served as an opportunity to exchange scientific information on BSE‐TSE related issues among EU Member States, countries from the European Free Trade Association, EU candidate countries, EFSA, the European Commission (EC) and ad hoc participants [in the 2022 meeting, represented by the World Organisation for Animal Health (WOAH)]. The topics discussed included: update on the situation and surveillance of CWD in North America and Norway, the molecular characterization of emergent CWD strains in Europe, the impact of feed ban on L‐BSE, the history experimental models using non‐human primates assessing transmissibility, pathogenesis and resistance of prions, a online real‐time pulse survey on the network and TSE in Europe, recent and ongoing activities on TSE of EFSA, WOAH and EC, as well as the preliminary results of the 2021 EU TSE summary report. [ABSTRACT FROM AUTHOR]

Event-based surveillance (EBS) gathers information from a variety of data sources, including online news articles. Unlike the data from formal reporting, the EBS data are not structured, and their interpretation can overwhelm epidemic intelligence (EI) capacities in terms of available human resources. Therefore, diverse EBS systems that automatically process (all or part of) the acquired nonstructured data from online news articles have been developed. These EBS systems (e.g., GPHIN, HealthMap, MedISys, ProMED, PADI-web) can use annotated data to improve the surveillance systems. This paper describes a framework for the annotation of epidemiological information in animal disease-related news articles. We provide annotation guidelines that are generic and applicable to both animal and zoonotic infectious diseases, regardless of the pathogen involved or its mode of transmission (e.g., vector-borne, airborne, by contact). The framework relies on the successive annotation of all the sentences from a news article. The annotator evaluates the sentences in a specific epidemiological context, corresponding to the publication date of the news article. Measurement(s) Precision/Recall • Annotator aggreement Technology Type(s) Expert annotation • Kappa's coefficient • Natural Language Processing Sample Characteristic - Organism Animal • African swine fever virus • Avian influenza • Foot-and-mouth disease virus • Bluetongue virus • Bovine spongiform encephalopathy Sample Characteristic - Environment Animal infectious diseases [ABSTRACT FROM AUTHOR]

The role of the glycosylation status of PrPC in the conversion to its pathological counterpart and on cross-species transmission of prion strains has been widely discussed. Here, we assessed the effect on strain characteristics of bovine spongiform encephalopathy (BSE) isolates with different transmission histories upon propagation on a model expressing a non-glycosylated human PrPC. Bovine, ovine and porcine-passaged BSE, and variant Creutzfeldt-Jakob disease (vCJD) isolates were used as seeds/inocula in both in vitro and in vivo propagation assays using the non-glycosylated human PrPC-expressing mouse model (TgNN6h). After protein misfolding cyclic amplification (PMCA), all isolates maintained the biochemical characteristics of BSE. On bioassay, all PMCA-propagated BSE prions were readily transmitted to TgNN6h mice, in agreement with our previous in vitro results. TgNN6h mice reproduced the characteristic neuropathological and biochemical hallmarks of BSE, suggesting that the absence of glycans did not alter the pathobiological features of BSE prions. Moreover, back-passage of TgNN6h-adapted BSE prions to BoTg110 mice recovered the full BSE phenotype, confirming that the glycosylation of human PrPC is not essential for the preservation of the human transmission barrier for BSE prions or for the maintenance of BSE strain properties. Author summary: Bovine spongiform encephalopathy (BSE), publicly known as "mad cow disease", is a neurodegenerative disorder affecting cattle, caused by unconventional agents called prions. BSE can naturally transmit to human beings, producing the variant form of Creutzfeldt-Jakob disease (vCJD), which caused an unprecedented health and economic crisis in the UE. Prions are composed of PrPSc, a misfolded form of the cellular protein PrPC, which can be variably glycosylated by conjugation with sugar molecules at two positions of its sequence. Several studies reported the role of PrPC-attached sugars on important aspects of prion biology, such as the existence of different prion strains. Here, we demonstrate that it is possible to propagate BSE prions (from different animal and human sources) in a non-glycosylated human PrPC environment without loss of their strain properties. Different BSE isolates were successfully transmitted to a transgenic mouse model expressing non-glycosylated human PrPC, and these animals manifested neuropathological and biochemical signs compatible with BSE. To definitely prove the maintenance of the strain, non-glycosylated BSE prions were transmitted to their original host: transgenic mice expressing cattle PrPC. These animals recovered the full BSE phenotype, confirming that the glycosylation of human PrPC is not relevant for the propagation of this particular prion strain. [ABSTRACT FROM AUTHOR]

The globalisation of food and agricultural trade has brought issues of food safety and biosecurity to the centre of geopolitical research. This paper explores the relationship between food risks and sovereignty practices, a topic that has received relatively scant attention in the scholarship. Going beyond conventional conceptualisations of sovereignty as an external-legal notion that is delimited to the realm of 'high politics' in international relations, this paper points to how it is also expressed and negotiated in quotidian practices of food import and consumption, and how this has contributed to the politicisation of food safety. Focusing on the case of Taiwan, a de facto island state with contested sovereignty status, and comparing the food safety discourses that arose during the outbreaks of Mad Cow Disease and African Swine Fever, we argue that food risks provide opportunities for social and political actors to participate in the everyday construction of sovereignty. While the Taiwanese government's handling of the Mad Cow Disease shows it to be ultimately constrained by the geopolitical reality of fragile sovereignty, the outbreak of African Swine Fever enabled it to legitimise the securitisation of borders and bolster its legitimacy by staging collective defensive actions against perceived external risks. By drawing attention to how sovereignty is produced and performed through practice, this paper further advances recent discussions of sovereignty as a dynamic, social process. [ABSTRACT FROM AUTHOR]