Enzyme Treatment Eliminates Prion Protein
By Biotechdaily staff writers
Posted on 21 Jan 2004
Researchers have found an enzymatic method to degrade the prion protein, responsible for bovine spongiform encephalopathy (BSE) and related diseases, which may be employed to disinfect surfaces that have been contaminated with the prion particles.Posted on 21 Jan 2004
Investigators at North Carolina State University (Raleigh, USA) found that keratinase from Bacillus licheniformis as well as proteinase K and two other subtilisin proteases, but not trypsin and pepsin, could effectively degrade the prion protein in the presence of detergent and after heat pretreatment. After this treatment, the prion protein could no longer be detected by immunologic techniques. These findings were published in the December 1,2003, issue of The Journal of Infectious Diseases.
"Our work has been done in vitro, or in test tubes, and we have reduced the prion to undetectable levels,” explained senior author Dr. Jason Shih, professor of biotechnology and poultry science at North Carolina State University. "Our work with mice will show whether these undetectable levels of prion are indeed noninfectious.”
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North Carolina State University