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Fighting Prion Diseases such as BSE, PrioNet Canada Announces $3 Million towards Research19 July 2006
Canadian contributions to international prion research efforts were consolidated through PrioNet Canada, a new Networks of Centres of Excellence established in November 2005. Prions are mysterious, misfolded protein agents that cause a range of diseases, the most notable being Bovine Spongiform Encephalopathy or BSE. PrioNet Canada recently announced ten successful recipients from across Canada for its first open call for project proposals. $3 million has been awarded over two years (2006-2008) to the various projects.
Each of the awarded projects complement PrioNet's five core research themes of BSE (cattle); Chronic Wasting Disease (CWD) (cervids); Creutzfeldt-Jakob Disease (humans); Prion Protein Structure and Function; and Prion Disease Risk Management. Selected project topics include: vaccine developments for BSE and CWD; tests to detect infectious prions; how prions turn from benign to disease-causing agents; surveillance and monitoring of CWD; and the impact of prion diseases on farm family community health.
"We were thrilled with the number of applications and high-caliber response to our open call," remarks Dr. Neil Cashman, PrioNet's Scientific Director. "Prion diseases have devastating economic, social, environmental, and health consequences. PrioNet is proud to be a part of enabling solutions for prion diseases in Canada." PrioNet's next open call will take place in early 2008.
PrioNet Canada (www.prionetcanada.ca) is a federally-funded Networks of Centres of Excellence established to address the many challenges of Transmissible Spongiform Encephalopathies (TSEs) or prion diseases in Canada. TSEs are fatal, transmissible diseases of humans and animals such as Bovine Spongiform Encephalopathy, Chronic Wasting disease, and Creutzfeldt-Jakob disease. PrioNet's collaborative network includes over 60 diverse scientific members, students, young professionals as well as government, NGOs, and industry partners. PrioNet funds multidisciplinary research, provides training and network opportunities, facilitates knowledge transfer, and disseminates prion information to the public. PrioNet's goal is to develop strategies to eradicate prion diseases altogether and deliver sound scientific advice upon which the Canadian Government can base future policies and regulations.
NB: Dr. Neil Cashman and selected researchers (attached) are available for interviews.
BACKGROUNDER
------------
PrioNet Canada Open Call Research Projects Summary 2006-2008
Principal Investigator: Dr. Trent Bollinger, University of Saskatchewan
"Factors affecting prevalence and geographic spread of chronic wasting
disease (CWD)"
The goal of this research project is to further the understanding of how CWD is transmitted and spread in wild deer. Bollinger's team will combine radio-telemetry studies with state-of-the-art techniques in population genetics to characterize population structure, deer movement patterns, and contact rates in order to predict the geographic spread of CWD. They will evaluate risk factors for CWD specific to deer populations on the Canadian prairies, such as genetic susceptibility and deer densities. These findings will be integrated with results of ongoing CWD surveillance programs for wild deer in Saskatchewan and Alberta, and with published information on the biology and epidemiology of CWD, in order to develop a predictive model which can be used to better manage and hopefully eradicate CWD.
Principal Investigator: Dr. Julie Forman-Kay, Hospital for Sick Children
"NMR Characterization of intermediate states and binding interactions of
PrP"
The prion protein (PrP), the major causative agent of neurodegenerative prion diseases, contains a large region with only fluctuating structure followed by a stably folded domain. PrP converts from a benign form to the infectious form, which has altered structure, primarily for residues of the folded domain. The disordered region interacts with other proteins potentially relevant to toxicity in prion diseases. Using nuclear magnetic resonance spectroscopy, Forman-Kay's team will study intermediate structures on the pathway of conversion between the benign and pathological forms. They will also identify fluctuating structure and its role in interactions with other proteins. Results will provide information about the mechanism of infectivity, toxicity, and the normal function of PrP, facilitating development of medical treatments for prion diseases.
Principal Investigator: Dr. John Glover, University of Toronto
"The PrP interactome: toward a comprehensive compendium of PrP
interacting proteins"
Two outstanding questions regarding PrP, the prion protein, are "What is the normal function of the protein?" and "How is the formation of infectious prions influenced by the other proteins present in cells?" To address these questions, John Glover and Igor Stagljar in the Department of Biochemistry at the University of Toronto, will be compiling a list of proteins that physically interact with PrP using innovative approaches. John Glover has been involved in work that showed that yeast have prions, too, and continues to work on proteins that dissolve protein aggregates, including yeast prions. Igor Stagljar recently moved to the University of Toronto from Switzerland where he was involved in developing state-of-the-art methods for discovering interactions between proteins that, like PrP, are attached to cell membranes.
Principal Investigator: Dr. Gordon Hayward, University of Guelph
"Acoustic prion sensor"
An acoustic prion sensor ("test") has been developed and proven capable of detecting infectious prions. Prions are the proteins associated with "mad cow" and similar diseases in other mammals. The test is quick, simple, and inexpensive. The sensor response is based on the protein folding mechanism of the disease which gives the sensor its unique advantages. The sensor uses a piezoelectric crystal to detect the refolding of recombinant prion protein on its surface. PrioNet's funding will support the sensor's continued development including proving its capability in urine and blood, verifying the sensor mechanism and understanding disease transmission. This project is in partnership with Canadian Food Inspection Agency's National Reference Laboratory for Scrapie in sheep and Chronic Wasting Disease in deer.
Principal Investigator: Dr. Stephen Moore, University of Alberta
"A comparative approach examining host response to TSE infection by
serial analysis of gene expression (microSAGE) in Cervids and Ovids"
Chronic Wasting Disease (CWD) and Scrapie are endemic TSE diseases in North America. CWD and scrapie share some key characteristics, the most important being that the infectious agent in both of these diseases can be horizontally transmitted and can lead to environmental contamination. Understanding the process of infection, disease progression, and detecting transmission at an early stage are vital to controlling these diseases.
Approved diagnostic methods for CWD and scrapie are based on post mortem identification of disease-associated prion proteins. The limitation to these methods means that detection of a single positive animal forces control programs to depopulate animals within a certain radius of the index case, despite the fact they may be perfectly healthy. In the project, they will approach the problems of late diagnosis and lack of disease understanding using gene expression analysis. The project will identify and adopt technologies that will serve to improve our understanding of TSE diseases and their interactions with their hosts. This improved understanding could lead to more efficient and effective diagnostic, control, and eradication programs and reduce the impact of disease outbreaks.
Principal Investigator: Dr. Andrew Potter, Vaccine & Infectious Diseases
Organization
"Immunoprophylaxis of bovine spongiform encephalopathy"
Prion diseases in a wide variety of mammalian species are characterized by the conversion of the normal host protein (PrP(c)) to an abnormal infectious form (PrP(Sc)). A research team led by Dr. Neil Cashman has identified and characterized a surface-exposed antibody-binding site which is present on PrP(Sc) but not PrP(c). This site is conserved among PrP(Sc) of a wide variety of mammalian species, thus making it an excellent universal vaccine target for prevention and therapy of diseases such as Bovine Spongiform Encephalopathy and Chronic Wasting Disease. The primary objective of this proposal is to develop vaccine formulations and vaccination protocols for ruminants which generate sustained levels of antibodies that react specifically with PrP(Sc) but not PrP(c). They have developed a proprietary vaccine carrier system which has been used previously to induce sustained, high titre antibody responses to "self-proteins" making it an ideal system to produce an anti-prion vaccine. The safety of a prion vaccine will also be evaluated through a collaboration with Drs. Charles Press and Ingrid Olsaker at the Norwegian Veterinary School.
Principal Investigator: Dr. Xavier Roucou, Université de Sherbrooke
"Pathobiology of prion protein aggregates: mechanism of propogation and
toxicity of aggregates produced in the cytoplasm"
Prion diseases are fatal transmissible neurodegenerative diseases. The infectious particle responsible for the transmission of these diseases has been discovered, and is composed of an aggregated form of the prion protein. However, the molecule responsible for untimely demise of neurons is still unknown. To find how neurons die represents a major current issue. Unless neurotoxic molecules and the cellular pathways used to promote neuronal death are identified, efficient preventive or curative therapies are unlikely to be developed. In this project, Roucou's team is investigating the molecular function of a recently discovered form of the prion protein, termed cytoplasmic prion protein. The results will help developing new strategies against the formation and propagation of neurotoxic prion molecules.
Principal Co-Investigators: Dr. Wilfreda Thurston, University of Calgary
and Dr. Carol Amaratunga, University of Ottawa
"A cohort study of the impact of prion disease on farm family community
health"
This national Farm Family and Community Health project addresses the lack of attention to the impacts of BSE on individuals, families, and communities. The project will establish a dynamic program of social science research on population health and BSE and how to manage risks and consequences. New questions will be asked about gender and culture, community capacity, and individual level psychological factors, particularly stress. A national cohort of farmers (men and women) who are willing to participate in a longitudinal study of the impact of BSE on the determinants of health will be created. The project will influence and shape public policy through a dissemination strategy which will target communities, provincial and federal policy makers and decision planners. For more information, please visit http://webapps2.ucalgary.ca/~fchnet/.
Principal Investigator: Dr. David Wishart, University of Alberta
"A novel approach to characterize prion aggregates and the prion
propagation complex"
Prion proteins are natural and relatively harmless proteins found in the bodies of humans and almost all animals; however, prion proteins are quite unique in that they can change shape and thereby "morph" from a harmless protein to a harmful protein complex. A key question that is still unanswered is: what is the shape or conformation of this harmful form of the prion protein? We will be using a technique called mass spectrometry in combination with specialized chemical modifications to help us figure out what this harmful version of the prion protein actually looks like. Determining the structure of this prion protein complex could lead to new ways to distinguish between the "healthy" and the "harmful" version of the prion protein. This can possibly lead to new ways that prevent the harmful version forming in the first place.
Principal Investigator: Dr. Shoshana Wodak, Hospital for Sick Children
"Mechanism of domain-swapped oligomer formation of prion proteins"
The neurodegenerative prion diseases result from a self-perpetuating conversion of the prion protein from the normal cellular form to the infectious disease causing form of the protein. This conversion involves a change in the structure of the protein, causing it to aggregate into large fibrous deposits. This project will use advanced techniques of molecular simulations to describe the very early steps of the aggregation process at the atomic level, a feat that few if any experimental procedure can presently accomplish. Results will show which portions of the protein are essential for this process. The derived information should be instrumental for the design of molecules that inhibit conversion, enabling the formulation of treatment strategies.
For further information: Media Inquiries: Sandra Haney, Communications Manager, PrioNet Canada, tel: (604) 222-3611, shaney@prionetcanada.ca; Attachment: Open Call Research Projects, Summary 2006-2008
Source: newswire
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