Prion Diseases

Mastrianni, James A.

doi:10.1016/b978-0-12-410529-4.00021-8

Cited by 12 publications

(13 citation statements)

References 288 publications

(273 reference statements)

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“…On the other hand, FFI is caused by the D178N mutation, the disease progresses quickly, and the patient dies within a few months after the onset of symptoms sleep disorders with agitation, fractionated sleep, snoring, and daytime sleepiness (Ayuso Blanco et al, 2006;Montagna et al, 2003). The inheritable familial forms of all Prion diseases (fCJD, GSS, and FFI) are inherited as autosomaldominant disorders (Mastrianni, 2003). The polymorphism coding for methionine (M) or valine (V) at codon 129 of the Prion protein gene (PRNP M129V) plays a pivotal role in the susceptibility to CJD, influencing familial, transmitted, and sporadic forms of the disease (Alperovitch et al, 1999), homozygosity for methionine at position 129 (met/met at codon 129) predisposes susceptibility and earlier age of onset of disease (Kretzschmar & Illig, 2009;Mead et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Prions: the danger of biochemical weapons

Xavier¹

2014

Food Sci. Technol (Campinas)

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Section: Discussionmentioning

confidence: 99%

Prions: the danger of biochemical weapons

Xavier¹

2014

Food Sci. Technol (Campinas)

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“…Familial Creutzfeldt-Jakob disease (fCJD), GSS and FFI represent the main phenotypes of genetic prion disease (Mastrianni, 2003). About half of the genetic cases identified by surveillance have a family history of the disease, but an unknown proportion of cases may also result from de novo gene mutation (Mastrianni et al, 2003).…”

Section: Agent Strains In Humansmentioning

confidence: 99%

Scientific Opinion on a request for a review of a scientific publication concerning the zoonotic potential of ovine scrapie prions

2015

EFSA Journal

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The factors that modulate the transmissibility of Transmissible Spongiform Encephalopathies (TSE) and the approaches for the study of their zoonotic potential are reviewed. The paper 'Evidence for zoonotic potential of ovine scrapie prions' by Cassard et al. (2014) is scientifically appraised, focussing on the experimental design, the results and the conclusions. The paper provides evidence in a laboratory experiment that some Classical scrapie isolates can propagate in humanised transgenic mice and produce prions that on second passage are similar to those causing one form of sporadic Creutzfeldt-Jakob disease (sCJD). It is concluded that the results from the study raise the possibility that scrapie prions have the potential to be zoonotic, but do not provide evidence that transmission can or does take place under field conditions. The conclusions of the 2011 ECDC-EFSA 'Joint Scientific Opinion on any possible epidemiological or molecular association between TSEs in animals and humans' are reviewed in the light of the new scientific evidence available since its publication. This supports and strengthens the conclusions of that opinion with regard to the potential for some animal TSE to be zoonotic, but does not provide evidence of a causal link between Classical or Atypical scrapie and human TSE. Current evidence does not establish this link, and no consistent risk factors have been identified for sCJD. The possibility of scrapie-related public health risks from the consumption of ovine products cannot be assessed. Recommendations are formulated on further studies and data that are needed to investigate the zoonotic potential of animal TSE and to estimate the amount of infectivity from TSE-infected products sourced from small ruminants and entering the food chain in the European Union. © European Food Safety Authority, 2015Keywords: Atypical scrapie, Classical scrapie, Creutzfeldt-Jakob disease, transmissible spongiform encephalopathy, zoonosis Amendment: An amendment has been made to the following sentence on p. 31: 'In this regard the emergence of sCJD is not so surprising, and has been described after inoculation of tgHu mice with cattle BSE and human vCJD (Asante et al., 2002;Beringue et al., 2008b)'. This was carried out to clarify that one of the references reported emergence of sporadic CJD after experimental inoculation of humanised transgenic mice with vCJD, which was not correctly stated in the published opinion. An amendment has been made on p. 28, to add the word 'OR' between two search terms within the literature search string reported. Reproduction is authorised provided the source is acknowledged. Requestor: European CommissionThe EFSA Journal is a publication of the European Food Safety Authority, an agency of the European Union. SummaryFollowing a request from the European Commission (EC), the EFSA Panel on Biological Hazards (BIOHAZ Panel) was asked to deliver a scientific opinion on the review of a scientific publication concerning the zoonotic potential of ovine scrapie prions.T...

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“…The transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group priónicas, son un grupo de padecimientos que afectan tanto a animales como al ser humano, y se caracterizan por presentar un período de incubación de años y un amplio espectro de manifestaciones neurológicas, debido a la pérdida de neuronas del sistema nervioso central (SNC) por áreas, acompañada de una activación de astrocitos, sin infiltrado inflamatorio y generalmente con depósitos de placas amiloides (material proteínico con un alto contenido de tiras b-plegadas) (1,2) .Estas enfermedades incluyen al Kuru, la enfermedad de Creutzfeldt-Jakob (CJD), el síndrome de Gerstmann-Sträussler-Scheinker (GSS) y el Insomnio Familiar Fatal (IFF) en seres humanos, así como el Scrapie en ovejas y cabras, la encefalopatía esponjiforme bovina (EEB), y encefalopatías en visones, felinos, venados y alces (3)(4)(5) . Todas ellas se relacionan con la presencia de una forma anormal de la Proteína Priónica Celular (PrP C ), denominada como Proteína Priónica Scrapie (PrP Sc ), la cual se considera el agente causal de las EETs.…”

Section: Introductionunclassified

“…Ratones tratados con siRNA mostraron un incremento en la supervivencia después de ser of neurological disorders that affect animals and humans. They are characterized by long incubation periods (years) and wide range of neurological manifestations, mainly due to the loss of central nervous system (CNS) neurons, accompanied by activation of astrocytes, without inflammatory infiltration and generally with amyloid deposits (beta-sheet rich protein material) (1,2) . These diseases include Kuru, Creutzfeldt-Jacob disease (CJD), Gerstmann-Sträussler-Scheinker (GSS) and fatal familial insomnia (IFF) in humans, as well as scrapie in sheep and goats, bovine spongiform encephalopathy (BSE), and encelopathies in minks, felines, deer and elks (3)(4)(5) .…”

Section: Introductionmentioning

confidence: 99%

El silenciamiento de la proteína priónica celular (PrPC) mediante RNA de interferencia (siRNA) reduce la infección por HSV-1 y HSV-2 en células SK-SY5Y

Ortega-Soto¹,

Arellano-Anaya²,

Castañeda-Colín³

et al. 2018

Rev. Mex. Cienc. Pecu.

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RESUMENLas encefalopatías espongiformes transmisibles (EETs) son enfermedades neurodegenerativas fatales que afectan a humanos y ciertas especies animales. La hipótesis más aceptada indica que el agente infeccioso, denotado como prion y compuesto principalmente por la Proteína Priónica Scrapie (PrP Sc ), corresponde a una conformación anormal de una proteína codificada por el huésped denominada Proteína Priónica Celular (PrP C ), cuya función es aún desconocida; sin embargo, la expresión ubicua de PrP C así como su elevado grado de conservación entre especies, sugieren un papel importante para esta proteína. En este trabajo se detectó a la PrP C en diferentes tipos celulares incluyendo un cultivo primario de células de peces (Tilapia, Oreochromis spp.). Además, basándonos en la secuencia de la PrP C humana, se diseñó un RNA de interferencia (siRNA) con el fin de silenciar el gen PRNP en células neuronales SK-SY5Y. El siRNA diseñado inhibió la expresión de PrP C a lo largo de las 96 h post-transfección y las células silenciadas fueron menos susceptibles a la infección por HSV-1 y HSV-2, en comparación con células no transfectadas con el siRNA. PALABRAS CLAVE: Proteína Priónica, PrP C , siRNA, HSV-1, HSV-2. ABSTRACTThe transmissible spongiform encephalopathies (TSEs) are neurodegenerative and fatal diseases, affecting humans and some other animal species. The most accepted hypothesis suggests that the infectious agent, named "prion", is composed mainly by the prion protein scrapie (PrP Sc ) and it corresponds to an abnormal conformation of a host encoded protein, the cellular prion protein (PrP C ), which function is still unknown. However, the ubiquitous expression of PrP C and its highly conserved presence among different species suggests it has a very important role in cell functions. In this work, the PrP C in different cell types, including a primary fish cell culture (Oreochromis spp.), was detected. In addition, based on the human PrP C sequence, we designed a short interfering RNA (siRNA) to silence the PRNP gen in neuronal SK-SY5Y cells. The designed siRNA inhibited the PrP C expression along 96 hours posttransfection and the silenced cells were less susceptible to HSV-1 and HSV-2 infections, in comparison to non siRNA-transfected cells.

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Prion Diseases

Cited by 12 publications

References 288 publications

Prions: the danger of biochemical weapons

Prions: the danger of biochemical weapons

Scientific Opinion on a request for a review of a scientific publication concerning the zoonotic potential of ovine scrapie prions

El silenciamiento de la proteína priónica celular (PrPC) mediante RNA de interferencia (siRNA) reduce la infección por HSV-1 y HSV-2 en células SK-SY5Y

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