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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.

Let (𝒜, ∥ · ∥𝒜) be a commutative and semisimple Banach algebra and (𝓑, ∥ · ∥𝓑) be an abstract Segal algebra with respect to 𝒜. In this paper, we first show that 𝒜 is Tauberian if and only if 𝓑 is Tauberian. Then we prove that A ^ ⊆ C BSE 0 ( Δ ( A ) ) if and only if B ^ ⊆ C BSE 0 ( Δ ( B ) ) . Afterwards, we conclude that whenever 𝒜 is a BED algebra, then 𝓑 is a BED algebra if and only if C BSE 0 ( Δ ( B ) ) ⊆ B ^ .

In this paper, X is a locally compact Hausdorff space and A is a Banach algebra. First, we study some basic features of C 0 ( X , A ) related to BSE concept, which are gotten from A . In particular, we prove that if C 0 ( X , A ) has the BSE property then A has so. We also establish the converse of this result, whenever X is discrete and A has the BSE-norm property. Furthermore, we prove the same result for the BSE property of type I. Finally, we prove that C 0 ( X , A ) has the BSE-norm property if and only if A has so.

In this paper, the electronic and adsorption properties of Ag 2 O metal oxides modified BP/BSe van der Waals heterostructures were investigated using density functional theory calculations. The adsorptions of CO, N 2 O, NO and NO 2 gas molecules on the Ag 2 O modified BP/BSe heterostructures were examined to evaluate their sensing abilities. The largest binding energy (− 1.72 eV) is observed for the binding of Ag 2 O to the center of BSe hexagon at the hollow sites. The Ag atoms are covalently bonded to the nearest Se atoms, as confirmed by the accumulation of charge density in the CDD diagrams between the Ag and Se atoms. We found that the NO 2 adsorption on the Ag 2 O-BP/BSe heterostructure exhibits the highest adsorption energy of − 2.64 eV, which can verify the strong chemisorption of NO 2 molecule on the heterostructure system. The changes in the band structures and work functions indicate the great effects of gas adsorption on the electronic properties of studied heterostructures. The N–O distance between the N atom of NO 2 molecule and the O atom of Ag 2 O is 1.35 Å. It can be concluded that Ag 2 O modification can greatly improve the adsorption capacity of BP/BSe heterostructures. Our theoretical results clearly highlight the potential application of novel Ag 2 O metal oxide modified BP/BSe heterostructures in sensing gas molecules.

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.

Given a weight function τ, we introduce a new class of Banach function algebras with respect to τ, denoted by C_0b(X, τ ). We provide a complete solution to the isomorphism problem in this class. We further characterize the BSE-extension and the Inoue-Doss ideal associated with it. As an application of our results, we show the equivalence of the four statements: (i) C_0b(X, τ) is of BSE, (ii) C_0b(X, τ) is of BED, (iii) C_0b(X, τ) is Tauberian and (iv) τ is bounded.

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(129), TgMet/Val(129), and TgVal(129). L-type BSE showed a higher zoonotic potential in TgMet(129) mice than classical BSE. whereas Val(1)(29)-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(129) and TgVal(129) 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.

Triticum monococcum ssp. aegilopoides (syn. T. boeoticum) is a wild diploid species that harbors the AbAb genome containing many disease resistance genes useful for wheat improvement. Genetic analysis conducted on an F2 population from a cross between T. boeoticum accessions PI 427741 and PI 427560, which are contrasting in powdery mildew responses, indicated that the resistance in PI 427741 was controlled by two dominant genes, PmNCA6 and another unknown gene. Bulked segregant exome capture sequencing (BSE-Seq) analysis of a segregating F3 family without PmNCA6 demonstrated a new powdery mildew resistance gene, Pm72, on the long arm of chromosome 6A. Through linkage analysis, Pm72 was mapped to a 1.28-cM genetic interval defined by markers XTb6AL04 and XTb6AL06. According to the reference genome of T. boeoticum accession TA299, the Pm72 locus corresponded to a 940-kb physical region (Chr6A: 635,963,867–636,888,696), containing 21 nucleotide-binding leucine-rich repeat receptor (NLR)-like disease resistance genes. Phenotyping showed that Pm72 confers effective resistance to powdery mildew at both the seedling and the adult-plant stages in the hexaploid wheat background. The co-segregating marker XTb6AL05 was useful for marker-assisted selection of Pm72. The identification of the new powdery mildew resistance gene Pm72 will contribute to its positional cloning and breeding application in wheat.