Identification of a second bovine amyloidotic spongiform encephalopathy: molecular similarities with sporadic Creutzfeldt-Jakob disease
Cristina Casalone,Gianluigi Zanusso,Pier Luigi Acutis,Sergio Ferrari,Lorenzo Capucci,Fabrizio Tagliavini,Salvatore Monaco,Maria Caramelli +7 more
TLDR
Evidence of a second cattle TSE is provided, pathologically characterized by the presence of PrP-immunopositive amyloid plaques, as opposed to the lack of amyloids deposition in typical BSE cases, and by a different pattern of regional distribution and topology of brain PrP(Sc) accumulation.Abstract:
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are mammalian neurodegenerative disorders characterized by a posttranslational conversion and brain accumulation of an insoluble, protease-resistant isoform (PrPSc) of the host-encoded cellular prion protein (PrPC). Human and animal TSE agents exist as different phenotypes that can be biochemically differentiated on the basis of the molecular mass of the protease-resistant PrPSc fragments and the degree of glycosylation. Epidemiological, molecular, and transmission studies strongly suggest that the single strain of agent responsible for bovine spongiform encephalopathy (BSE) has infected humans, causing variant Creutzfeldt-Jakob disease. The unprecedented biological properties of the BSE agent, which circumvents the so-called ”species barrier” between cattle and humans and adapts to different mammalian species, has raised considerable concern for human health. To date, it is unknown whether more than one strain might be responsible for cattle TSE or whether the BSE agent undergoes phenotypic variation after natural transmission. Here we provide evidence of a second cattle TSE. The disorder was pathologically characterized by the presence of PrP-immunopositive amyloid plaques, as opposed to the lack of amyloid deposition in typical BSE cases, and by a different pattern of regional distribution and topology of brain PrPSc accumulation. In addition, Western blot analysis showed a PrPSc type with predominance of the low molecular mass glycoform and a protease-resistant fragment of lower molecular mass than BSE-PrPSc. Strikingly, the molecular signature of this previously undescribed bovine PrPSc was similar to that encountered in a distinct subtype of sporadic Creutzfeldt-Jakob disease.read more
Citations
More filters
Journal ArticleDOI
The challenge of emerging and re-emerging infectious diseases
TL;DR: Infectious diseases have for centuries ranked with wars and famine as major challenges to human progress and survival and remain among the leading causes of death and disability worldwide.
Journal ArticleDOI
Synthetic Mammalian Prions
Giuseppe Legname,Ilia V. Baskakov,Hoang-Oanh B. Nguyen,Detlev Riesner,Fred E. Cohen,Stephen J. DeArmond,Stanley B. Prusiner +6 more
TL;DR: The results provide compelling evidence that prions are infectious proteins and suggest that a novel prion strain was created.
Monitoring of verotoxigenic Escherichia coli (VTEC) and identification of human pathogenic VTEC types 1 Scientific Opinion of the Panel on Biological Hazards
Olivier Andreoletti,Herbert Budka,Sava Buncic,Pierre Colin,John D. Collins,John W. Griffin,Arie Havelaar,James Hope,Günter Klein,Hilde Kruse,Antonio Martínez López,James McLauchlin,Christophe Nguyen-The,Birgit Noerrung,Miguel Prieto Maradona,Terence Roberts,Ivar Vågsholm,Emmanuel Vanopdenbosch +17 more
Journal ArticleDOI
Molecular mechanisms of prion pathogenesis
TL;DR: The molecular mechanisms leading to neurodegeneration, the role of the immune system in prion pathogenesis, and the existence of prion strains that appear to have different tropisms and biochemical characteristics are discussed.
Journal ArticleDOI
Mortality from Creutzfeldt–Jakob disease and related disorders in Europe, Australia, and Canada
Anna Ladogana,Maria Puopolo,Esther A. Croes,Herbert Budka,C. Jarius,Steven J. Collins,Genevieve M Klug,T. Sutcliffe,Antonio Giulivi,Annick Alpérovitch,N. Delasnerie-Laupretre,J.-P. Brandel,Sigrid Poser,Hans A. Kretzschmar,Ingrid Rietveld,Eva Mitrova,J de Pedro Cuesta,Pablo Martinez-Martin,Markus Glatzel,Adriano Aguzzi,Richard Knight,Hester J.T. Ward,Maurizio Pocchiari,C M van Duijn,Robert G. Will,Inga Zerr +25 more
TL;DR: Overall epidemiologic characteristics for Creutzfeldt–Jakob disease (CJD) of all types in a multinational population–based study are established and the occurrence of a novel form of human bovine spongiform encephalopathy infection other than variant CJD is not suggested.
References
More filters
Journal ArticleDOI
A new variant of Creutzfeldt-Jakob disease in the UK
Robert G. Will,James W. Ironside,M. Zeidler,Simon Cousens,K Estibeiro,Annick Alpérovitch,Sigrid Poser,Maurizio Pocchiari,Albert Hofman,Pete Smith +9 more
TL;DR: Ten cases of Creutzfeldt-Jakob disease have been identified in the UK in recent months with a new neuropathological profile that raises the possibility that they are causally linked to BSE.
Journal ArticleDOI
Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent
Moira E. Bruce,Robert G. Will,James W. Ironside,I. McConnell,D. Drummond,A. Suttie,L. McCardle,A. Chree,James Hope,Christopher R. Birkett,Simon Cousens,H. Fraser,Christopher J. Bostock +12 more
TL;DR: It is shown that the strain of agent from cattle affected by bovine spongiform encephalopathy (BSE) produces a characteristic pattern of disease in mice that is retained after experimental passage through a variety of intermediate species, providing strong evidence that the same agent strain is involved in both BSE and vCJD.
Journal ArticleDOI
Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
TL;DR: Strain characteristics revealed here suggest that the prion protein may itself encode disease phenotype, consistent with BSE being the source of this new disease.
Journal ArticleDOI
Classification of sporadic Creutzfeldt‐Jakob disease based on molecular and phenotypic analysis of 300 subjects
Piero Parchi,Armin Giese,Sabina Capellari,Paul Brown,Walter J. Schulz-Schaeffer,Otto Windl,Inga Zerr,Herbert Budka,Nicolas Kopp,Pedro Piccardo,Sigrid Poser,Amyn M. Rojiani,Nathalie Streichemberger,Jean Julien,Claude Vital,Bernardino Ghetti,Pierluigi Gambetti,Hans A. Kretzschmar +17 more
TL;DR: The present data demonstrate the existence of six phenotypic variants of sCJD, and the physicochemical properties of PrPSc in conjunction with the PRNP codon 129 genotype largely determine this phenotypesic variability, and allow a molecular classification of the disease variants.