Research by North Carolina State University scientists, in conjunction with scientists from the Netherlands and BioResource International, an NC State spin-off biotechnology company, has shown that, under proper conditions, an enzyme can fully degrade the prion – or protein particle – believed to be responsible for mad cow disease and other related animal and human diseases.
These transmissible prions – believed to be the cause of bovine spongiform encephalopathy (BSE), the technical name for mad cow disease, as well as the human and sheep versions, called Creutzfeldt-Jakob disease and scrapie, respectively – are highly resistant to degradation, says Dr. Jason Shih, professor of biotechnology and poultry science at NC State. But the new research, which tested the effects of a bacterial enzyme keratinase on brain tissues from cows with BSE and sheep with scrapie, showed that, when the tissue was pretreated and in the presence of a detergent, the enzyme fully degraded the prion, rendering it undetectable.
The research was published in the Dec. 1 edition of The Journal of Infectious Diseases.
Mick Kulikowski, | NC State University
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