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The CReSA is working on a new strategy to combat spongiforms
November 01, 2006Researchers at the Animal Health Research Centre (CReSA) are developing immunotherapeutical strategies against diseases produced by prion, such as Bovine Spongiform Encephalitis. The most recent results, published in the Journal of Virology, show that important advances have been made in tests using DNA vaccines on animal models, enabling a significant delay in the arrival of symptoms. In the long term, this research could lead to the production of treatment for humans.
The infectious agent responsible for transmissible spongiform encephalopathies, also known as prion diseases, (which include mad cow disease), is a protein known as the infectious prion (PrPi), which has no nucleic acid and which produces contagious neurodegenerative diseases in different species of animals. The PrPi changes shape to that of an existing natural protein in the organism, the cellular prion (PrPc), but does not change its amino acid sequence. In certain circumstances, when the PrPi comes into contact with the original proteins, the proteins take on the shape of the in the infectious protein. Once this accumulates in the central nervous system, it destroys neural mass and makes the brain of affected animals take on a sponge form, which is where the term "spongiform diseases" comes from.
The researchers' work focuses on producing a vaccine that will provide an immune response that is as complete as possible, including both a humoral response (production of antibodies) and a cellular response (eliminating "infected" cells and activating the "memory", enabling the animal cells to continue responding to the infectious agent).
The main obstacle to achieving this objective is that the prions do not produce an immune response since the metabolism of the affected animal identifies it as one of its own antigens. The challenge, therefore, is to overcome the tolerance barrier, that is, that the animal's body produces an immune response to one of its antigens.
The researchers have achieved this objective using a DNA vaccine based on a plasmid (an extrachromosomal DNA molecule) that expresses the prion gene with a small sequence that acts as a transport signal to cellular compartments called lysosomes. Once the vaccination is administered, the prion quickly degrades in the lysosome, allowing a marked improvement in the presentation of the cells of the immune system and inducing a powerful antibody and cellular response.
The results of the research have shown that in vaccinated mice, and only in those vaccinated, there is a significant delay in the appearance of symptoms after the intracerebral infection produced by the infectious prion.
The group is continuing its research to further investigate new administration routes for the vaccine and to eliminate the side effects observed in vaccinated animals.
This work may also enable advances to be made in the development of reactive agents for the diagnosis of diseases produced by the prion that until now could only be achieved post mortem.
Universitat Autonoma de Barcelona
The main obstacle to achieving this objective is that the prions do not produce an immune response since the metabolism of the affected animal identifies it as one of its own antigens. The challenge, therefore, is to overcome the tolerance barrier, that is, that the animal's body produces an immune response to one of its antigens.
The researchers have achieved this objective using a DNA vaccine based on a plasmid (an extrachromosomal DNA molecule) that expresses the prion gene with a small sequence that acts as a transport signal to cellular compartments called lysosomes. Once the vaccination is administered, the prion quickly degrades in the lysosome, allowing a marked improvement in the presentation of the cells of the immune system and inducing a powerful antibody and cellular response.
The results of the research have shown that in vaccinated mice, and only in those vaccinated, there is a significant delay in the appearance of symptoms after the intracerebral infection produced by the infectious prion.
The group is continuing its research to further investigate new administration routes for the vaccine and to eliminate the side effects observed in vaccinated animals.
This work may also enable advances to be made in the development of reactive agents for the diagnosis of diseases produced by the prion that until now could only be achieved post mortem.
Universitat Autonoma de Barcelona
Prion Current Events and Prion News RSSThe Protein Srebp2 Drives Cholesterol Formation in Prion-Infected Neuronal Cells Which May Promote Prion-Dependent Diseases
The regulating protein Srebp2 drives cholesterol formation, which prions need for their propagation, in prion-infected neuronal cells.
Prion study reveals first direct information about the protein's molecular structure
A collaboration between scientists at Vanderbilt University and the University of California, San Francisco has led to the first direct information about the molecular structure of prions.
U of T led research team uncovers evolutionary origins of prion disease gene
A University of Toronto-led team has uncovered the evolutionary ancestry of the prion gene, which may reveal new understandings of how the prion protein causes diseases such as bovine spongiform encephalopathy (BSE), also known as "mad cow disease."
Species barrier may protect macaques from chronic wasting disease
Data from an ongoing multi-year study suggest that people who consume deer and elk with chronic wasting disease (CWD) may be protected from infection by an inability of the CWD infectious agent to spread to people.
A Penny for Your Prions
North Carolina State University researchers have discovered a link between copper and the normal functioning of prion proteins, which are associated with transmissible spongiform encephalopathy diseases such as Cruetzfeldt-Jakob in humans or "mad cow" disease in cattle.
Scripps Florida scientists devise accelerated method to determine infectious prion strainsScripps Florida scientists devise accelerated method to determine infectious prion strains
Current tests to identify specific strains of infectious prions, which cause a range of transmissible diseases (such as mad cow) in animals and humans, can take anywhere from six months to a year to yield results - a time-lag that may put human populations at risk.
Prevalence of variant CJD agent in Britain remains uncertain
First results from a large tissue survey in Britain of the agent that causes variant Creutzfeldt-Jakob disease (vCJD) are unable so far to establish that the prevalence is lower than that given by previous estimates, concludes a study published on bmj.com today.
Redefining what it means to be a prion
Whitehead Institute researchers have quintupled the number of identifiable prion proteins in yeast and have further clarified the role prions play in the inheritance of both beneficial and detrimental traits.
Iron is involved in prion disease-associated neuronal demise
Imbalance of iron homeostasis is a common feature of prion disease-affected human, mouse, and hamster brains, according to a new study by Dr. Neena Singh and colleagues at Case Western Reserve University School of Medicine, alongside collaborators from Creighton University.
Prion discovery gives clue to control of mass gene expression
The discovery in common brewer's yeast of a new, infectious, misfolded protein -- or prion -- by University of Illinois at Chicago molecular biologists raises new questions about the roles played by these curious molecules, often associated with degenerative brain diseases like "mad cow" and its human counterpart, Creutzfeldt-Jakob.
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