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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 (PrP[sup.Sc] ). 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 PrP[sup.Sc] 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 PrP[sup.Sc] -profiles of six brain regions were determined. The lesion profile and the neuroanatomical distribution of PrP[sup.Sc] was highly consistent between the groups, but the immunohistochemical analysis revealed a distinct PrP[sup.Sc] profile for the different BSE-types, which included both the topographic and cellular pattern of PrP[sup.Sc] . This qualitative and quantitative analysis of PrP[sup.Sc] 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.

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.

What a waste I suspect most PN readers have long enough memories to remember the BSE crisis in the UK and even John Gummer the MP who was pictured feeding his 4 year-old daughter a hamburger at the height of the panic. [...]any endemic prion based disorder which may jump species to species (particularly in a post-COVID world) is alarming. How long before there is a spillover event from venison that could be costing us dear? https://www.theguardian.com/environment/2023/dec/22/zombie-deer-disease-yellowstone-scientists-fears-fatal-chronic-wasting-disease-cwd-jump-species-barrier-humans-aoe No sex please, we’re robots Whoever had ‘what can sex robots teach us about consent in the context of serious assault?’ as their most important unanswered research question were treated to an odyssey of artificial intelligence (AI) and morality. If you want to know, for example, why The Netherlands predicts a 7·5% decline in prevalence between 1990 to 2016, whereas Norway predicts a 87·1% increase over the same time period, treat yourself and read the whole paper.

Prions propagate as multiple strains in a wide variety of mammalian species. The detection of all such strains by a single ultrasensitive assay such as Real Time Quaking-induced Conversion (RT-QuIC) would facilitate prion disease diagnosis, surveillance and research. Previous studies have shown that bank voles, and transgenic mice expressing bank vole prion protein, are susceptible to most, if not all, types of prions. Here we show that bacterially expressed recombinant bank vole prion protein (residues 23-230) is an effective substrate for the sensitive RT-QuIC detection of all of the different prion types that we have tested so far--a total of 28 from humans, cattle, sheep, cervids and rodents, including several that have previously been undetectable by RT-QuIC or Protein Misfolding Cyclic Amplification. Furthermore, comparison of the relative abilities of different prions to seed positive RT-QuIC reactions with bank vole and not other recombinant prion proteins allowed discrimination of prion strains such as classical and atypical L-type bovine spongiform encephalopathy, classical and atypical Nor98 scrapie in sheep, and sporadic and variant Creutzfeldt-Jakob disease in humans. Comparison of protease-resistant RT-QuIC conversion products also aided strain discrimination and suggested the existence of several distinct classes of prion templates among the many strains tested.

Classical bovine spongiform encephalopathy (BSE) is the only zoonotic prion disease described to date. Although the zoonotic potential of atypical BSE prions have been partially studied, an extensive analysis is still needed. We conducted a systematic study by inoculating atypical BSE isolates from different countries in Europe into transgenic mice overexpressing human prion protein (PrP): TgMet , TgMet/Val , and TgVal . L-type BSE showed a higher zoonotic potential in TgMet mice than classical BSE, whereas Val -PrP variant was a strong molecular protector against L-type BSE prions, even in heterozygosis. H-type BSE could not be transmitted to any of the mice. We also adapted 1 H- and 1 L-type BSE isolate to sheep-PrP transgenic mice and inoculated them into human-PrP transgenic mice. Atypical BSE prions showed a modification in their zoonotic ability after adaptation to sheep-PrP producing agents able to infect TgMet and TgVal , bearing features that make them indistinguishable of sporadic Creutzfeldt-Jakob disease prions.

Transmissible spongiform encephalopathies (TSE), caused by abnormal prion protein (PrPSc), affect many species. The most classical scrapie isolates harbor mixtures of strains in different proportions. While the characterization of isolates has evolved from using wild-type mice to transgenic mice, no standardization is established yet. Here, we investigated the incubation period, lesion profile and PrPSc profile induced by well-defined sheep scrapie isolates, bovine spongiform encephalopathy (BSE) and ovine BSE after intracerebral inoculation into two lines of ovine PrP (both ARQ/ARQ) overexpressing transgenic mice (Tgshp IX and Tgshp XI). All isolates were transmitted to both mouse models with an attack rate of almost 100%, but genotype-dependent differences became obvious between the ARQ and VRQ isolates. Surprisingly, BSE induced a much longer incubation period in Tgshp XI compared to Tgshp IX. In contrast to the histopathological lesion profiles, the immunohistochemical PrPSc profiles revealed discriminating patterns in certain brain regions in both models with clear differentiation of both BSE isolates from scrapie. These data provide the basis for the use of Tgshp IX and XI mice in the characterization of TSE isolates. Furthermore, the results enable a deeper appreciation of TSE strain diversity using ovine PrP overexpressing transgenic mice as a biological prion strain typing approach.

Let A be a Banach algebra and let X be a Banach A-bimodule. We consider the Banach algebra ${A\\oplus _1 X}$ , where A is a commutative Banach algebra. We investigate the Bochner–Schoenberg–Eberlein (BSE) property and the BSE module property on $A\\oplus _1 X$ . We show that the module extension Banach algebra $A\\oplus _1 X$ is a BSE Banach algebra if and only if A is a BSE Banach algebra and $X=\\{0\\}$ . Furthermore, we consider $A\\oplus _1 X$ as a Banach $A\\oplus _1 X$ -module and characterise the BSE module property on $A\\oplus _1 X$ . We show that $A\\oplus _1 X$ is a BSE Banach $A\\oplus _1 X$ -module if and only if A and X are BSE Banach A-modules.

Let $\\mathcal A$ and $\\mathcal B$ be commutative and semisimple Banach algebras and let $\\theta \\in \\Delta (\\mathcal B)$ . In this paper, we prove that $\\mathcal A\\times _{\\theta }\\mathcal B$ is a type I-BSE algebra if and only if ${\\mathcal A}_e$ and $\\mathcal B$ are so. As a main application of this result, we prove that $\\mathcal A\\times _{\\theta }\\mathcal B$ is isomorphic with a $C^*$ -algebra if and only if ${\\mathcal A}_e$ and $\\mathcal B$ are isomorphic with $C^* $ -algebras. Moreover, we derive related results for the case where $\\mathcal A$ is unital.

Alexandra MacKenzie Imperial College School of Medicine, Imperial College London, London, UKCorrespondence: Alexandra MacKenzieImperial College School of Medicine, Imperial College London, South Kensington Campus, Sir Alexander Fleming Building, London, UKTel +44 7588040282Email alexandra.mackenzie16@imperial.ac.uk View the original paper by Mrs Urga and colleagues

Atypical/Nor98 scrapie (AS) is a prion disease of small ruminants. Currently there are no efficient measures to control this form of prion disease, and, importantly, the zoonotic potential and the risk that AS might represent for other farmed animal species remains largely unknown. In this study, we investigated the capacity of AS to propagate in bovine PrP transgenic mice. Unexpectedly, the transmission of AS isolates originating from 5 different European countries to bovine PrP mice resulted in the propagation of the classical BSE (c-BSE) agent. Detection of prion seeding activity in vitro by protein misfolding cyclic amplification (PMCA) demonstrated that low levels of the c-BSE agent were present in the original AS isolates. C-BSE prion seeding activity was also detected in brain tissue of ovine PrP mice inoculated with limiting dilutions (endpoint titration) of ovine AS isolates. These results are consistent with the emergence and replication of c-BSE prions during the in vivo propagation of AS isolates in the natural host. These data also indicate that c-BSE prions, a known zonotic agent in humans, can emerge as a dominant prion strain during passage of AS between different species. These findings provide an unprecedented insight into the evolution of mammalian prion strain properties triggered by intra- and interspecies passage. From a public health perspective, the presence of c-BSE in AS isolates suggest that cattle exposure to small ruminant tissues and products could lead to new occurrences of c-BSE.