14 June 2001. Abnormal forms of the prion protein are thought to be the infective
agent responsible for bovine spongiform encephalopathy (BSE, or "mad cow disease")
and its human form, variant Creutzfeldt-Jakob disease (vCJD). The pathogenic
prion can spread disease through contaminated beef products as well as though
human blood and tissue. The protein is expressed highly only in the brain, and
the lack of methods to detect the low amounts in blood and other tissues has
fueled public alarm over the potential spread of vCJD. In this week's Nature
Claudio Soto and colleagues at the Serono Pharmaceutical Research Institute
in Geneva, Switzerland, describe a method by which the abnormal, pathogenic
form of the prion protein can convert large amounts of normal prion into the
abnormal state. The method could form the basis for a test to detect trace amounts
of infective prion in the blood of infected animals or humans. The technique
could also be used to produce large quantities of abnormal prion protein in
the test tube, enabling the prion to be studies with greater ease.-June Kinoshita.
Reference:Saborio GP, Permanne B, Soto C. Sensitive detection of pathologic prion protein by cyclic amplification of protein misfolding. Nature. 2001 June 14;(411):810-3. Abstract
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