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Jean Manson - One of the best experts on this subject based on the ideXlab platform.
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post translational changes to prp alter Transmissible Spongiform Encephalopathy strain properties
The EMBO Journal, 2013Co-Authors: Enrico Cancellotti, Pedro Piccardo, Robert A Somerville, Sukhvir P Mahal, Abigail B Diack, Deborah Brown, Charles Weissmann, Jean MansonAbstract:The agents responsible for Transmissible Spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrPSc, an abnormal conformer of the host glycoprotein PrPC. TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contain PrPSc with the same amino-acid sequence. If PrP alone carries information defining strain properties, these must be encoded by post-translational events. Here we investigated whether the glycosylation status of host PrP affects TSE strain characteristics. We inoculated wild-type mice with three TSE strains passaged through transgenic mice with PrP devoid of glycans at the first, second or both N-glycosylation sites. We compared the infectious properties of the emerging isolates with TSE strains passaged in wild-type mice by in vivo strain typing and by the standard scrapie cell assay in vitro. Strain-specific characteristics of the 79A TSE strain changed when PrPSc was devoid of one or both glycans. Thus infectious properties of a TSE strain can be altered by post-translational changes to PrP which we propose result in the selection of mutant TSE strains.
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mechanism of prp amyloid formation in mice without Transmissible Spongiform Encephalopathy
Brain Pathology, 2012Co-Authors: Martin Jeffrey, Jean Manson, Gillian Mcgovern, Emily V Chambers, Declan King, Lorenzo Gonzalez, Bernardino Ghetti, Pedro PiccardoAbstract:Gerstmann-Straussler-Scheinker (GSS) P102L disease is a familial form of a Transmissible Spongiform Encephalopathy (TSE) that can present with or without vacuolation of neuropil. Inefficient disease transmission into 101LL transgenic mice was previously observed from GSS P102L without vacuolation. However several aged, healthy mice had large plaques composed of abnormal prion protein (PrP d ). Here we perform the ultrastructural characterisation of such plaques and compare them with PrP d aggregates found in TSE caused by an infectious mechanism. PrP d plaques in 101LL mice varied in maturity with some being composed of deposits without visible amyloid fibrils. PrP d was present on cell membranes in the vicinity of all types of plaques. In contrast to the unicentric plaques seen in infectious murine scrapie the plaques seen in the current model were multi-centric and were initiated by proto-fibrillar forms of PrP d situated on oligodendroglia, astrocytes and neuritic cell membranes. We speculate that the initial conversion process leading to plaque formation begins with membrane-bound PrP C but that subsequent fibrillisation does not require membrane attachment. We also observed that the membrane alterations consistently seen in murine scrapie and other infectious TSEs were not observed in 101LL mice with plaques suggesting differences in the pathogenesis of these conditions.
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glycosylation of prpc determines timing of neuroinvasion and targeting in the brain following Transmissible Spongiform Encephalopathy infection by a peripheral route
Journal of Virology, 2010Co-Authors: Enrico Cancellotti, Nadia L. Tuzi, Barry Bradford, Pedro Piccardo, Rona Barron, Raymond D Hickey, Debbie Brown, Karen Brown, Dorothy Kisielewski, Jean MansonAbstract:Transmissible Spongiform Encephalopathy (TSE) infectivity naturally spreads from site of entry in the periphery to the central nervous system where pathological lesions are formed. Several routes and cells within the host have been identified as important for facilitating the infectious process. Expression of the glycoprotein cellular PrP (PrPC) is considered a key factor for replication of infectivity in the central nervous system (CNS) and its transport to the brain, and it has been suggested that the infectious agent propagates from cell to cell via a domino-like effect. However, precisely how this is achieved and what involvement the different glycoforms of PrP have in these processes remain to be determined. To address this issue, we have used our unique models of gene-targeted transgenic mice expressing different glycosylated forms of PrP. Two TSE strains were inoculated intraperitoneally into these mice to assess the contribution of diglycosylated, monoglycosylated, and unglycosylated PrP in spreading of infectivity to the brain. This study demonstrates that glycosylation of host PrP has a profound effect in determining the outcome of disease. Lack of diglycosylated PrP slowed or prevented disease onset after peripheral challenge, suggesting an important role for fully glycosylated PrP in either the replication of the infectious agent in the periphery or its transport to the CNS. Moreover, mice expressing unglycosylated PrP did not develop clinical disease, and mice expressing monoglycosylated PrP showed strikingly different neuropathologic features compared to those expressing diglycosylated PrP. This demonstrates that targeting in the brain following peripheral inoculation is profoundly influenced by the glycosylation status of host PrP.
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high titers of Transmissible Spongiform Encephalopathy infectivity associated with extremely low levels of prpsc in vivo
Journal of Biological Chemistry, 2007Co-Authors: Rona Barron, Declan King, Susan L Campbell, Anne Bellon, Karen E Chapman, Anthony R Williamson, Jean MansonAbstract:Diagnosis of Transmissible Spongiform Encephalopathy (TSE) disease in humans and ruminants relies on the detection in post-mortem brain tissue of the protease-resistant form of the host glycoprotein PrP. The presence of this abnormal isoform (PrPSc) in tissues is taken as indicative of the presence of TSE infectivity. Here we demonstrate conclusively that high titers of TSE infectivity can be present in brain tissue of animals that show clinical and vacuolar signs of TSE disease but contain low or undetectable levels of PrPSc. This work questions the correlation between PrPSc level and the titer of infectivity and shows that tissues containing little or no proteinase K-resistant PrP can be infectious and harbor high titers of TSE infectivity. Reliance on protease-resistant PrPSc as a sole measure of infectivity may therefore in some instances significantly underestimate biological properties of diagnostic samples, thereby undermining efforts to contain and eradicate TSEs.
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Cre-loxP mediated control of PrP to study Transmissible Spongiform Encephalopathy diseases
Genesis, 2004Co-Authors: Nadia L. Tuzi, L Aitchison, Val Thomson, Alan Richard Clarke, Barry Bradford, Jean MansonAbstract:Expression of the PrP glycoprotein is essential for the development of the Transmissible Spongiform Encephalopathy (TSE) or prion diseases. Although PrP is widely expressed in the mouse, the precise relevance of different PrP-expressing cell types to disease remains unclear. To address this, we generated two lines of floxed PrP gene-targeted transgenic mice using the Cre recombinase-loxP system. These floxed mice allow a functional PrP allele to be either switched “on” or “off.” We demonstrate control of PrP expression for both alleles following Cre-mediated recombination, as determined by PrP mRNA and protein expression in the brain. Moreover, we show that Cre-mediated alteration of PrP expression in these mice has a major influence on the development of TSE disease. These floxed PrP mice will allow the involvement of PrP expression in specific cell types following TSE infection to be defined, which may identify potential sites for therapeutic intervention. genesis 40:1–6, 2004. © 2004 Wiley-Liss, Inc.
Pedro Piccardo - One of the best experts on this subject based on the ideXlab platform.
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post translational changes to prp alter Transmissible Spongiform Encephalopathy strain properties
The EMBO Journal, 2013Co-Authors: Enrico Cancellotti, Pedro Piccardo, Robert A Somerville, Sukhvir P Mahal, Abigail B Diack, Deborah Brown, Charles Weissmann, Jean MansonAbstract:The agents responsible for Transmissible Spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrPSc, an abnormal conformer of the host glycoprotein PrPC. TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contain PrPSc with the same amino-acid sequence. If PrP alone carries information defining strain properties, these must be encoded by post-translational events. Here we investigated whether the glycosylation status of host PrP affects TSE strain characteristics. We inoculated wild-type mice with three TSE strains passaged through transgenic mice with PrP devoid of glycans at the first, second or both N-glycosylation sites. We compared the infectious properties of the emerging isolates with TSE strains passaged in wild-type mice by in vivo strain typing and by the standard scrapie cell assay in vitro. Strain-specific characteristics of the 79A TSE strain changed when PrPSc was devoid of one or both glycans. Thus infectious properties of a TSE strain can be altered by post-translational changes to PrP which we propose result in the selection of mutant TSE strains.
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mechanism of prp amyloid formation in mice without Transmissible Spongiform Encephalopathy
Brain Pathology, 2012Co-Authors: Martin Jeffrey, Jean Manson, Gillian Mcgovern, Emily V Chambers, Declan King, Lorenzo Gonzalez, Bernardino Ghetti, Pedro PiccardoAbstract:Gerstmann-Straussler-Scheinker (GSS) P102L disease is a familial form of a Transmissible Spongiform Encephalopathy (TSE) that can present with or without vacuolation of neuropil. Inefficient disease transmission into 101LL transgenic mice was previously observed from GSS P102L without vacuolation. However several aged, healthy mice had large plaques composed of abnormal prion protein (PrP d ). Here we perform the ultrastructural characterisation of such plaques and compare them with PrP d aggregates found in TSE caused by an infectious mechanism. PrP d plaques in 101LL mice varied in maturity with some being composed of deposits without visible amyloid fibrils. PrP d was present on cell membranes in the vicinity of all types of plaques. In contrast to the unicentric plaques seen in infectious murine scrapie the plaques seen in the current model were multi-centric and were initiated by proto-fibrillar forms of PrP d situated on oligodendroglia, astrocytes and neuritic cell membranes. We speculate that the initial conversion process leading to plaque formation begins with membrane-bound PrP C but that subsequent fibrillisation does not require membrane attachment. We also observed that the membrane alterations consistently seen in murine scrapie and other infectious TSEs were not observed in 101LL mice with plaques suggesting differences in the pathogenesis of these conditions.
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glycosylation of prpc determines timing of neuroinvasion and targeting in the brain following Transmissible Spongiform Encephalopathy infection by a peripheral route
Journal of Virology, 2010Co-Authors: Enrico Cancellotti, Nadia L. Tuzi, Barry Bradford, Pedro Piccardo, Rona Barron, Raymond D Hickey, Debbie Brown, Karen Brown, Dorothy Kisielewski, Jean MansonAbstract:Transmissible Spongiform Encephalopathy (TSE) infectivity naturally spreads from site of entry in the periphery to the central nervous system where pathological lesions are formed. Several routes and cells within the host have been identified as important for facilitating the infectious process. Expression of the glycoprotein cellular PrP (PrPC) is considered a key factor for replication of infectivity in the central nervous system (CNS) and its transport to the brain, and it has been suggested that the infectious agent propagates from cell to cell via a domino-like effect. However, precisely how this is achieved and what involvement the different glycoforms of PrP have in these processes remain to be determined. To address this issue, we have used our unique models of gene-targeted transgenic mice expressing different glycosylated forms of PrP. Two TSE strains were inoculated intraperitoneally into these mice to assess the contribution of diglycosylated, monoglycosylated, and unglycosylated PrP in spreading of infectivity to the brain. This study demonstrates that glycosylation of host PrP has a profound effect in determining the outcome of disease. Lack of diglycosylated PrP slowed or prevented disease onset after peripheral challenge, suggesting an important role for fully glycosylated PrP in either the replication of the infectious agent in the periphery or its transport to the CNS. Moreover, mice expressing unglycosylated PrP did not develop clinical disease, and mice expressing monoglycosylated PrP showed strikingly different neuropathologic features compared to those expressing diglycosylated PrP. This demonstrates that targeting in the brain following peripheral inoculation is profoundly influenced by the glycosylation status of host PrP.
Paul Brown - One of the best experts on this subject based on the ideXlab platform.
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high pressure inactivation of Transmissible Spongiform Encephalopathy agents prions in processed meats
2016Co-Authors: Paul Brown, Franco Cardone, Richard J Meyer, Maurizio PocchiariAbstract:The epidemic of bovine Spongiform Encephalopathy (BSE) that began in the late 1980s and has so far been responsible for over 200 human fatalities caused by the ingestion of contaminated beef products stimulated research into disinfection methods appropriate for both animal feed and human food. As it turned out, the risk of infection was almost entirely eliminated by government and industry bans, first on the use of recycled bovine tissues in cattle feed (the source of the epidemic in bovines) and, second, the exclusion of potentially contaminated bovine tissues from beef products consumed by humans. A third approach, had the first two not been successful, was a disinfection method compatible with the aesthetic and nutritional quality of beef products. In this chapter, we review the results of a series of experiments that were undertaken to explore optimal conditions for the commercial use of a combined high-temperature and high-pressure inactivation of BSE prions in processed meats. In repeated experiments, we were unable to detect any significant effect on infectivity from a two-hour exposure to 60 °C at pressures between 400 and 800 MPa. In a further large series of experiments conducted with a variety of machines at different facilities, we found that a 5-min exposure to temperatures and pressures in the range of 120–130 °C and 600–700 MPa yielded, on average, a 100-fold (2 log) reduction in infectivity. Depending on assumptions about the potential infectious load in a given beef product, this level of disinfection, although useful, cannot be guaranteed to eliminate the risk of disease transmission to humans.
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Transmissible Spongiform Encephalopathy in the 21st century neuroscience for the clinical neurologist
Neurology, 2008Co-Authors: Paul BrownAbstract:There is no shortage of recent reviews on various aspects of Transmissible Spongiform Encephalopathy (TSE),1–12 but none has been addressed to clinical neurologists in the hope of providing a reasonably brief and non-technical summary of the more important advances since the turn of the century. The beneficiary of opinions from members of both the basic and clinical research communities, this synopsis was undertaken to strike a readable compromise between the depths of specialized reviews and the shallows of abstracts generated by Internet search engines (PubMed lists 934 entries for Creutzfeldt-Jakob disease [CJD], 2,170 entries for TSE, and 4,729 entries for prion disease published since the turn of the century). After more than 60 years of study, the most basic questions concerning the infectious agent—exactly what it is, and how it replicates—have not been fully answered. Because of 1) the consistent failure to find any disease-specific foreign nucleic acid or protein and 2) the almost equally consistent finding of a host-encoded but misfolded prion protein (PrPTSE) in the brains of affected humans and animals, a consensus has arisen (but still not formally proven) that favors the protein as the principal if not sole cause of disease. Over 30 different mutations in its encoding gene ( PRNP ) on chromosome 20 are responsible for the different forms of familial CJD, and one important polymorphism at codon 129 (encoding methionine or valine) influences susceptibility and clinical characteristics in all forms of human disease. The first convincing evidence for a physiologic role of the normal protein (PrPC) is the recent surprising finding that it regulates β-secretase cleavage of the Alzheimer amyloid precursor protein.13 The proposed sequence of events in TSE is that the normal protein, which is a soluble proteinase-sensitive and α-helix-rich glycoprotein of approximately 35 kD molecular weight, misfolds via one …
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Working with Transmissible Spongiform Encephalopathy agents.
ILAR journal, 2005Co-Authors: Paul Brown, Christian R. AbeeAbstract:The family of illnesses called Transmissible Spongiform encephalopathies (TSEs), or "prion" diseases, is composed of a small number of human and animal neurodegenerative diseases caused by unique pathogenic agents that are still not fully defined. They are best considered as "protein-misfolding diseases" (together with Alzheimer's disease, Parkinson's disease, and a few other rare examples) resulting from the conversion of a normal body protein into a misfolded amyloid multimer. The pathogenic agents display a unique resistance to conventional disinfection methods and an extraordinary environmental durability, which has led the US Department of Agriculture to designate the causative agent of bovine Spongiform Encephalopathy as a bioterrorism security threat. In this review, precautions and regulations concerning the handling of TSE agents are discussed in relation to personnel and environmental biosafety.
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similar levels of infectivity in the blood of mice infected with human derived vcjd and gss strains of Transmissible Spongiform Encephalopathy
Transfusion, 2003Co-Authors: Larisa Cervenakova, William N. Drohan, Lisa M Mcshane, Oksana Yakovleva, Carroll Mckenzie, Svetlana Kolchinsky, Paul BrownAbstract:BACKGROUND: The possible transmission of variant CJD (vCJD) through blood transfusion or use of plasma-derived products prompted this study comparing infectivity in murine models of vCJD and Gerstmann-Straussler-Scheinker (GSS) disease, a non-vCJD form of Transmissible Spongiform Encephalopathy (TSE). STUDY DESIGN AND METHODS: RIII/Fa/Dk (RIII) or Swiss-Webster (Swiss) mice were inoculated intracerebrally (IC) with mouse-adapted strains of vCJD or GSS (Fukuoka-1) of similar infectivity. Groups of RIII mice were euthanized 17 weeks after inoculation (during the incubation period), and another 23 weeks after inoculation (when symptomatic). Blood was collected, separated into components, and inoculated into groups of healthy mice; brains and spleens from all mice were harvested and tested for the presence of PrPres by Western blot using 6H4 MoAb. RESULTS: Levels of 20-30 infectious doses per mL were present in buffy coat and plasma during both the incubation and symptomatic stages of disease; PLT pellet infectivity was lower (10 ID/mL) and RBCs were not infectious. The disease was transmitted more efficiently by IV than IC inoculation of plasma, but there was no difference observed with inoculation of buffy coat. The incubation period was shorter after IC inoculation of GSS- than vCJD-brain inocula. The amount of PrPres in spleens was similar for both TSE agents, but was slightly lower in brains of vCJD than GSS mice. CONCLUSION: Infectivity was detected in blood components of mice infected with a human-derived strain of vCJD during both the preclinical and clinical phases of disease in a similarly low range of concentrations as in mice infected with a human-derived nonvariant strain (GSS, Fukuoka-1). Other measures of virulence, including brain infectivity titers, incubation periods, and the accumulation of PrPres in spleens and brains, were also comparable in both experimental models.
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Transmissible Spongiform Encephalopathy update and implications for blood safety.
Clinics in laboratory medicine, 2003Co-Authors: Maura N Ricketts, Paul BrownAbstract:This article reviews the evidence regarding the risk of transmission of the human Transmissible Spongiform encephalopathies (TSEs) through transfusion and the implications for blood safety. At this time, the accumulated evidence does not support the implementation of measures targeted against the risk of transfusion transmission of sporadic, familial, or iatrogenic Creutzfeldt-Jakob disease (CJD). Evolving information about variant CJD (vCJD), however, suggests that policy makers need to consider implementing measures to protect against exposure to vCJD, if such measures themselves do not lead to decreased blood safety. Surveillance of TSEs and investigation of the risk of transfusion transmission must continue in order to provide further refinements in blood safety policy.
P. Brown - One of the best experts on this subject based on the ideXlab platform.
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an historical perspective on efforts to treat Transmissible Spongiform Encephalopathy
Cns & Neurological Disorders-drug Targets, 2009Co-Authors: P. BrownAbstract:Efforts to treat Transmissible Spongiform Encephalopathy (TSE) date back to the middle of the 20 th century. Early studies were colored by the belief that TSE was caused by a 'slow' or 'unconventional' virus, and a variety of anti-infective agents, together with scores of drugs drawn at random from other categories, predictably failed to provide any benefit, apart from polyanionic compounds and polyene antibiotics that prolonged the incubation period of disease in experimental animals. With the discovery in the 1980's that TSE apparently results from the malformation of a normal host protein, attempts at treatment could at last be rationally focused, and can be broadly categorized as genetic, immunologic, and pharmacologic. Genetic 'neutralization' of the pathogen has shown excellent results in experimental animals but is unlikely to be useful until the same kind of engineering can be effectively applied to humans. Immunologic methods to accomplish the same result have also shown some success in animals, but forays into the pharmacologic realm have been generally disappointing. Most reported 'successes' have been limited to prolonged incubation periods, and even then only when the treatment was begun at or near the time of infection, which is not known in sporadic or familial human disease. However, a few methods using the more rigorous model of treatment nearer the onset of symptomatic disease have begun to yield promising results that, if coupled with a practical screening test for pre-clinical infection, would be the optimal strategy for prevention or cure.
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Transmissible Spongiform Encephalopathy prion disease
Foodborne Pathogens (Second edition)#R##N#Hazards Risk Analysis and Control, 2009Co-Authors: P. BrownAbstract:Abstract: A variant form of Creutzfeldt-Jakob disease (vCJD) resulted from human exposure to beef products contaminated with bovine Spongiform Encephalopathy (BSE). In this chapter, the chronology of both disease outbreaks is recounted, with special attention to pathogenesis, difficulty of decontamination, past and present risk from BSE and other animal prion diseases and, despite the waning number of new cases of both BSE and vCJD, the need for continuing surveillance and protective measures.
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Blood infectivity, processing and screening tests in Transmissible Spongiform Encephalopathy.
Vox sanguinis, 2005Co-Authors: P. BrownAbstract:Surprising advances have been made in the areas of blood infectivity, infectivity removal and, especially, blood screening tests for Transmissible Spongiform Encephalopathy (TSE) in the past few years. In fact, if anyone as recently as last year had suggested that a screening test for preclinical human infection might be available before the end of 2005, the statement would have been met with smiling disbelief. Nevertheless, it can be confidently predicted that the diagnostic misfolded 'prion' protein (PrP(TSE)) will soon be reliably detectable in blood during the symptomatic phase of disease, and it is highly probable that it will also be detectable in blood from at least a proportion of infected individuals during the preclinical phase of disease.
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Factor VIII and Transmissible Spongiform Encephalopathy: the case for safety.
Haemophilia : the official journal of the World Federation of Hemophilia, 2002Co-Authors: Larisa Cervenakova, P. Brown, David J. Hammond, C. A. Lee, Evgueni L. SaenkoAbstract:Haemophilia A is the most common inherited bleeding disorder, caused by a deficiency in coagulation factor VIII (FVIII). Current treatment of haemophilia A is based on repeated infusions of plasma-derived FVIII concentrate or of recombinant FVIII, which may be exposed to plasma-derived material of human or animal origin used in its tissue culture production process. We review epidemiological and experimental studies relevant to blood infectivity in the Transmissible Spongiform encephalopathies (TSEs, or `prion' diseases), and evaluate the hypothetical risk of TSE transmission through treatment with plasma-derived or recombinant FVIII.
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The pathogenesis of Transmissible Spongiform Encephalopathy: routes to the brain and the erection of therapeutic barricades.
Cellular and molecular life sciences : CMLS, 2001Co-Authors: P. BrownAbstract:Classical and modern studies of the pathogenesis of Transmissible Spongiform Encephalopathy are reviewed, with particular attention paid to recent investigations of the routes of neuroinvasion. In various experimental models, a heirarchy of paths to the brain includes direct neural transit from the site of infection, replication in the spleen and neural entry through the spinal cord, and hematogenous spread. Possible modes and sites of therapeutic intervention are suggested.
W. Van Wassenhove - One of the best experts on this subject based on the ideXlab platform.
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Risk communication: the European Commission TSE Roadmap Model for policy relaxation
International Journal of Risk Assessment and Management, 2012Co-Authors: Kerstin Dressel, W. Van Wassenhove, Alice PerazziniAbstract:The Bovine Spongiform Encephalopathy (BSE) crisis forced the European Commission to impose strict regulations, the most significant and overarching of which was Regulation (EC) No 999/2001. These regulations were responsible for the abatement of the BSE epidemic in Europe in the years that followed. The Transmissible Spongiform Encephalopathy (TSE) Roadmap was published by the European Commission several years later, on 15 July 2005. This roadmap proposed the relaxation of BSE measures in the short, medium and long term. It was seen as a proactive way to prepare for the implementation of new regulations and, in terms of risk communication, was a very interesting approach. This paper presents the 'roadmap model' as an effective tool for risk communication. It proposes several recommendations to help decision-makers in the difficult task of risk communication and establishes some conditions for generating public trust.
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A comparative study of stakeholder risk perception and risk communication in Europe: A bovine Spongiform Encephalopathy case study
Journal of Risk Research, 2012Co-Authors: W. Van Wassenhove, Kerstin Dressel, Alice PerazziniAbstract:The 'Transmissible Spongiform Encephalopathy (TSE) Roadmap' was published by the European Commission on 15 July 2005. The TSE Roadmap proposes the relaxation of bovine Spongiform Encephalopathy (BSE) measures in the short, medium and long term. According to the Roadmap, any relaxation of BSE measures following the scientific assessment should be initiated by an open discussion with all stakeholders and supported by a strong communication strategy. This paper discusses the risk perception, risk communication and risk management of TSEs in Europe, exemplified by the TSE Roadmap. The main conclusion is that in general, BSE is no longer a 'hot' topic for stakeholders, but there are slight differences between countries with respect to specific measures. Another important conclusion is that the TSE Roadmap is a very effective tool for risk communication with stakeholders.
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Public Risk Perception of Relaxation of Transmissible Spongiform Encephalopathies (Tse) Measures in Europe
Journal of toxicology and environmental health. Part A, 2011Co-Authors: Kerstin Dressel, Alice Perazzini, W. Van WassenhoveAbstract:The so-called “TSE roadmap” was published by the European Commission on July 15, 2005. The Transmissible Spongiform Encephalopathy (TSE) roadmap suggests relaxation of bovine Spongiform Encephalopathy (BSE) in cattle and other animal Transmissible Spongiform encephalopathies measures in the short, medium, and long term. According to the TSE roadmap, “Any relaxation of BSE measures following the scientific assessment should be initiated by an open discussion with all stakeholders and supported by a strong communication strategy” (European Commission 2005, 5). Bearing this in mind, a social scientific project was designed to (1) involve different stakeholder groups, governmental risk managers, and their scientific advisors and (2) obtain their perception of the TSE roadmap and of its implications for precautionary consumer protection in five European Union (EU) Member States. This study describes the risk perception and risk management of TSE in Europe as exemplified by the TSE roadmap. The following query ...
