FRIDAY, Dec. 22, 2006 (HealthDay News) -- A method of removing prion infectivity from scrapie-infected animal blood proved effective in tests on hamsters, says a U.S. study.
The research, published in this week's issue of The Lancet, may help in the development of a way to prevent the spread of variant Creutzfeldt-Jakob disease (vCJD), the human form of mad cow disease.
Sheep scrapie is a fatal neurodegenerative prion disease -- like bovine spongiform encephalopathy in cows and vCJD in humans -- that occurs after years of incubation and no apparent symptoms.
In the case of vCJD, being able to remove prion infectivity from donated blood may be one way to reduce transmission of the disease.
Researchers identified a molecule called L13 that selectively binds to the prion protein. They passed scrapie-infected hamster blood through devices that contained the L13 molecule and then injected the blood into 96 hamsters. None of them became infected, the study said.
The scientists said they also found that L13 could selectively bind to the prion protein from human infections of vCJD, which suggests that L13 may also be able to remove prion infectivity from human blood.
"Removal of vCJD infectivity by absorption gets around the extremely difficult problem of detecting the very low concentrations of these agents in blood, especially during the long asymptomatic period of the disease when people donate [blood]. For these disease agents, removal may be our best and perhaps our only option," researcher Robert Rohwer, of the Veterans Affairs Medical Center, University of Maryland, said in a prepared statement.
The U.S. National Library of Medicine has more about prion diseases.