Identification of H-type BSE in Portugal

Orge, Leonor; Machado, Carla; Ramalho, Luísa; Carvalho, Renata; Silva, João; Almeida, Paula; Tavares, Paula; Ochoa, Cristina; Lima, Carla Caroline Valença de; Pinto, M. J.; Simas, J. Pedro

doi:10.1080/19336896.2014.997615

Cited by 6 publications

(5 citation statements)

References 33 publications

(54 reference statements)

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“…L-type BSE cases show immunolabelling in the cerebellum, in both the molecular and granular layers, similar to that described for atypical scrapie in sheep [ 130 , 132 , 134 ]. In H-type BSE the immunolabelling in the molecular and granular layers of the cerebellum is minimal and less uniformly distributed compared to L-type BSE, but there is a remarkable widespread glial labelling throughout the white matter of the spinal cord and the cerebellum [ 130 ].…”

Section: Neuropathologysupporting

confidence: 75%

“…Stellate type PrP Sc deposition is predominantly identified in the cerebral cortex, basal nuclei, thalamus, hypothalamus and hippocampus, and often in the cerebellar cortex, but it is not visible in the brainstem and spinal cord [ 121 ]. Intraglial-type PrP Sc deposition is highly consistent throughout the white matter tracts of the brainstem [ 132 , 133 , 134 ] ( Figure 6 ). Some animals present PrP Sc -positive plaques scattered throughout the cerebral white matter [ 121 ].…”

Section: Neuropathologymentioning

confidence: 99%

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Neuropathology of Animal Prion Diseases

et al. 2021

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Transmissible Spongiform Encephalopathies (TSEs) or prion diseases are a fatal group of infectious, inherited and spontaneous neurodegenerative diseases affecting human and animals. They are caused by the conversion of cellular prion protein (PrPC) into a misfolded pathological isoform (PrPSc or prion- proteinaceous infectious particle) that self-propagates by conformational conversion of PrPC. Yet by an unknown mechanism, PrPC can fold into different PrPSc conformers that may result in different prion strains that display specific disease phenotype (incubation time, clinical signs and lesion profile). Although the pathways for neurodegeneration as well as the involvement of brain inflammation in these diseases are not well understood, the spongiform changes, neuronal loss, gliosis and accumulation of PrPSc are the characteristic neuropathological lesions. Scrapie affecting small ruminants was the first identified TSE and has been considered the archetype of prion diseases, though atypical and new animal prion diseases continue to emerge highlighting the importance to investigate the lesion profile in naturally affected animals. In this report, we review the neuropathology and the neuroinflammation of animal prion diseases in natural hosts from scrapie, going through the zoonotic bovine spongiform encephalopathy (BSE), the chronic wasting disease (CWD) to the newly identified camel prion disease (CPD).

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Section: Neuropathologysupporting

confidence: 75%

Section: Neuropathologymentioning

confidence: 99%

Neuropathology of Animal Prion Diseases

et al. 2021

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“…[11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] Prions of atypical BSE are distinguished biochemically and pathologically from the C-BSE prion. The risk of transmission of atypical BSE prions to human beings is still under investigation.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of rapid post-mortem test kits for bovine spongiform encephalopathy (BSE) screening in Japan: Their analytical sensitivity to atypical BSE prions

Hagiwara

Iwamaru

Tabeta

et al. 2017

Prion

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ABSTRACT. A classical type of bovine spongiform encephalopathy (C-BSE), recognized in 1987, had a large impact on public health due to its zoonotic link to variant Creutzfeldt-Jakob disease by the human consumption of dietary products contaminated with the C-BSE prion. Thus, a number of countries implemented BSE surveillance using rapid post-mortem test kits that were approved for detection of the C-BSE prion in the cattle brain. However, as atypical BSE (L-and H-BSE) cases emerged in subsequent years, the efficacy of the kits for the detection of atypical BSE prions became a matter of concern. In response to this, laboratories in the European Union and Canada evaluated the kits used in their countries. Here, we carried out an evaluation study of NippiBL Ò , a kit currently used for BSE screening in Japan. By applying the kit to cattle brains of field cases of C-BSE and L-BSE, and an experimental case of H-BSE, we showed its comparable sensitivities to C, L-, and H-BSE prions, and satisfactory performance required by the European Food Safety Authority. In addition to NippiBL Ò , two kits (TeSeE Ò and FRELISA Ò ) formerly used in Japan were effective for detection of the L-BSE prion, although the two kits were unable to be tested for the H-BSE prion due to the discontinuation of domestic sales during this study. These results indicate that BSE screening Correspondence to: Ken'ichi Hagiwara;

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“…In contrast, very few cases of sporadic forms of BSE have been reported in comparison to classical BSE. Animals affected by sporadic BSE, also called atypical BSE, have been reported in several countries; however, their aetiology has not been fully explained so far (Guldimann et al, 2012;Orge et al, 2015).…”

Section: Abstract: Bovine Prion Protein Gene Codon 211 Mutationmentioning

confidence: 99%

Lack of germline mutation at codon 211 of the prion protein gene (PRNP) in Korean native cattle — Short communication

Kim

Jeong

2017

Acta Veterinaria Hungarica

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Bovine prion diseases are composed of two types of bovine spongiform encephalopathy (BSE), classical BSE and atypical BSE. Recent studies have identified one case of atypical BSE with an E211K mutation. E211K is homologous to the human E200K mutation, which is related to familial Creutzfeldt-Jakob disease (CJD), one of the familial forms of human prion diseases. To date, familial forms of prion diseases have not been reported in non-human animals. Because the familial forms of human prion diseases account for more than 10% of all human prion disease cases, the detection of the E211K mutation in healthy cattle is very important for verifying the role of this mutation as a familial form of BSE. To detect putative mutations related to familial BSE, specifically E211K in Korean native cattle (Hanwoo) and Korean dairy cattle (Holstein), we performed direct sequencing targeting codon 211 and the adjacent regions of the bovine prion protein (PRNP) gene in 384 Hanwoo and 152 Holstein cattle. We did not find the E211K mutation in any of the Korean cattle. Although we did not find the E211K mutation in Korean native cattle, E211K is a postulated mutation; therefore, further screening in other countries and larger samples is highly desirable.

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Identification of H-type BSE in Portugal

Cited by 6 publications

References 33 publications

Neuropathology of Animal Prion Diseases

Neuropathology of Animal Prion Diseases

Evaluation of rapid post-mortem test kits for bovine spongiform encephalopathy (BSE) screening in Japan: Their analytical sensitivity to atypical BSE prions

Lack of germline mutation at codon 211 of the prion protein gene (PRNP) in Korean native cattle — Short communication

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