For the first time, experimental results indicate that it is possible to use a resin filter to remove harmful prion proteins from the blood of an infected animal, //a finding that has major implications for the removal of infectious prion proteins – the agents associated with variant Creutzfeldt-Jakob disease, mad cow disease, scrapie and other prion diseases in animals – during blood transfusions.
Dr. Ruben Carbonell, Frank Hawkins Kenan Professor of Chemical and Biomolecular Engineering and director of the Kenan Institute for Engineering, Technology and Science at North Carolina State University, and scientists from the University of Maryland at Baltimore’s VA Medical Center, the American Red Cross and ProMetic BioSciences, a biotechnology company, developed small resin beads with molecules that are able to bind to harmful prion proteins. The beads serve as an adsorption filter, capturing the bad proteins and allowing other blood components to be effectively cleansed of the prion-disease-causing agents.
A paper describing the research was published in the Dec. 23/30 version of The Lancet.
In prion diseases, which are called transmissible spongiform encephalopathies, prion proteins unfold and cause plaques in animal and human brains. Transmission of prion diseases has impacted the availability and cost of blood donations, especially in Europe.
In the Lancet study, the researchers took the blood of scrapie-infected hamsters and removed the white blood cells using a device called a leukofilter. The leukoreduced blood was then passed through another filter containing the new resin particles engineered to capture the prion proteins. A group of disease-free hamsters was inoculated with the blood that passed through the leukofilter only. A second group was inoculated with the blood that passed through both the leukofilter and the prion-capture filter.
The researchers found that while leukoreduction itself removePage: 1 2 Related medicine news :1
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