At present, diseases like scrapie, BSE and its human counterpart, new variant Creutzfeldt Jackob disease (vCJD) can be diagnosed only by post-mortem examination of brain tissue for evidence of faulty prions – the rogue proteins suspected of causing the disease. This is because prions accumulate solely in the brain and are present only at very low concentrations elsewhere in the body.
In this week's Nature (Vol. 411, No. 6839, 14 Jun 2001), Claudio Soto and colleagues at the Serono Pharmaceutical Research Institute in Geneva, Switzerland, report that minute amounts of abnormal prion protein can convert large amounts of normal prion into its faulty state, thereby lowering the threshold of detection considerably. Because trace amounts of abnormal prion are suspected to be circulating in the blood of infected animals or people, the technique could in principle form the basis of a sensitive test for prion diseases.
The method could also be used to produce large amounts of infectious prion protein in vitro (something not possible at present). This would allow the infectivity and pathogenicity of prions to be studied better than is currently possible, the researchers claim.
Nick Miles (Serono S.A. communications office)
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