Protecting a Life-saving Blood Product from Human Form of Mad Cow Disease

Article ID: 539091

Released: 27-Mar-2008 3:45 PM EDT

Source Newsroom: American Chemical Society (ACS)

  • Credit: Credit: Photo courtesy of MacoPharma.

    Researchers report development of a special blood filter (shown) that removes the human form of mad cow disease when used during blood transfusions.

Newswise — Amid concern that recipients of certain blood transfusions may risk infection with a deadly protein responsible for the human form of mad cow disease, researchers in Canada now report development of a special filter that quickly and effectively removes the protein from blood.

In addition to causing mad cow disease, these so-called prion proteins cause a variant form of the human neurological disorder, Creutzfeldt-Jakob disease. Termed variant Creutzfeldt-Jakob Disease (vCJD), its emergence triggered recent bans on exportation of beef from Europe. Variant CJD also can be transmitted in blood transfusions.

"The use of the device will significantly decrease the risk of acquiring vCJD through blood transfusions," co-author Patrick V. Gurgel, Ph.D., reported at the 235th national meeting of the American Chemical Society. The device has been approved for use in Europe "and has no competitor at the moment," said Gurgel.

About the size of a person's hand, the device contains a specially-designed material that recognizes and binds to prions. "This technology adds a needed layer of protection against the transmission of vCJD through blood transfusion," said Gurgel, senior research scientist at ProMetic Life Sciences in Mont-Royal, Quebec, Canada. "Our research shows that it works."

The new filter can remove prions from red blood cell concentrate in less than an hour. Transfusions of red blood cells go to thousands of patients with chronic anemia resulting from kidney failure, cancer, gastrointestinal bleeding, and acute blood loss resulting from trauma.

The researchers needed five years to develop the device and are now working on ways to remove prion proteins from other blood components, including plasma and plasma proteins, Gurgel said.

In previous studies, the scientists showed that the device could successfully remove prions from the blood of infected hamsters and that the disinfected blood could be injected into healthy hamsters without causing disease. More recently, the researchers demonstrated that the device can also filter healthy human blood without damaging the red blood cells and other blood components, a finding that demonstrates that the technique is safe for use on human blood, they said.

Human clinical studies using the device, called the P-Capt® Prion Capture Filter, are now underway in Europe, where it has received approval for commercialization, the scientists say. The first commercialization will be in Ireland and the United Kingdom (UK) and is expected in mid 2008, in an effort to help safeguard blood supplies, Gurgel suggested.

Experts believe that vCJD is acquired from eating beef from prion-infected cattle. As in cows, the disease is characterized by a slow destruction of the brain tissue, which results in nerve damage, paralysis, and eventually death. So far, vCJD has killed at least 200 people in Europe alone. Health officials are increasingly concerned that the disease may spread elsewhere, including the United States, through blood transfusions from infected individuals.

There is currently no reliable blood test for detecting the disease or a way of destroying the infectious prion proteins in blood. As a result, blood donation centers in the U.S. have imposed restrictions on blood donations from individuals who have lived in Europe for at least five years, particularly in the UK, where most vCJD cases have occurred.

Funding for the development was provided by ProMetic Life Sciences, The American Red Cross, and MacoPharma, which are partners in the project.

The American Chemical Society — the world's largest scientific society — is a nonprofit organization chartered by the U.S. Congress and a global leader in providing access to chemistry-related research through its multiple databases, peer-reviewed journals and scientific conferences. Its main offices are in Washington, D.C., and Columbus, Ohio.

Note for reporters' use only: For full information about the New Orleans meeting, including access to abstracts of more than 9,000 scientific papers and hundreds of non-technical summaries, visit http://www.eurekalert.org/acsmeet.php.

The paper on this research, I&EC 064, will be presented at 1:30 p.m. on Tuesday, April 8, at the Morial Convention Center, Room 231, during the symposium, "Industrial and Engineering Chemistry Divisional Fellow Award Symposium " Dr. Ruben Carbonell."

Patrick V. Gurgel, Ph.D., is a Senior Research Scientist in the Department of Chemical and Biomolecular Engineering at PromMetic Life Sciences in Mont-Royal, Quebec, Canada. He is also an Adjunct Assistant Professor in the Department of Chemical and Biomolecular Engineering at North Carolina State University in Raleigh, North Carolina. ALL PAPERS ARE EMBARGOED UNTIL DATE AND TIME OF PRESENTATION, UNLESS OTHERWISE NOTED The paper on this research, I&EC 064, will be presented at 1:30 PM, Tuesday, April 8, 2008, during the symposium, "Industrial and Engineering Chemistry Divisional Fellow Award Symposium - Dr. Ruben Carbonell." I&EC 064Development of a device for prion reduction based on affinity ligand Program Selection: Division of Industrial & Engineering ChemistryTopic Selection: Industrial and Engineering Chemistry Divisional Fellow Award Symposium - Dr. Ruben Carbonell

Abstract The potential presence of disease-associated prion proteins in blood and its derivatives poses a challenge for the blood transfusion industry. Prion inactivation has been suggested, but not reduced to practice while removal strategies focused on blood, such as leukodepletion reduce infectivity by less than one log. The use of affinity resins to capture specific targets from a complex medium is a viable complement for leukodepletion. In order to overcome the difficulties of passing a particulated material (red blood cell concentrate) through a packed-bed column, a device containing multiple layers of particle-impregnated membranes was developed. Its performance was evaluated in regards to prion capture, blood quality, and removal of other proteins, among other parameters, with very good results. A comparison with resin in column format showed similar capacities and dissociation constants, indicating that the trapped resin particles are still accessible to the target material. ________________________________________Researcher Provided Non-Technical Summary Briefly explain in lay language what you have done, why it is significant and what are its implications (particularly to the general public)

We have developed a device for removing the prion protein (responsible for vCJD) from a widely used blood product, red blood cell concentrate. The use of the device will significantly decrease the risk of acquiring vCJD through blood transfusions.

How new is this work and how does it differ from that of others who may be doing similar research?

P-Capt (the registered name of the device) is a device based on the capture of prions through the use of specific ligands developed to recognize and bind the prion protein in a complex mixture. The device has received approval for commercialization in Europe (CE mark) and has no competitor at the moment.


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