Research published in the September issue of Nature Medicine may help minimize the spread of prion diseases in the human body.
Prion diseases, like BSE (bovine spongiform encephalopathy) and CJD (Creutzfeldt-Jakob disease) are caused by a misfolded prion protein referred to as PrPSc. Minimizing spread of the disease could be facilitated by the ability to detect PrPSc in blood. Claudio Soto and colleagues have devised an automated method, termed protein misfolding cyclic amplification, to help do just that.
The extremely small amount of PrPSc that appears in blood makes it difficult to detect it and diagnose the disease. But the researchers' new technique, analogous to polymerase chain reaction for amplifying tiny samples of genetic material, amplifies PrPSc in the test tube, which allows the detection of PrPSc with 89% sensitivity (a measure of the probability of correct diagnosis) and 100% specificity (i.e., the method detects no false positives).
This is the first time PrPSc has been biochemically detected in the blood, so the authors have raised several issues for discussion. These issues include investigating whether all diseased animals carry PrPSc in their blood, and how early and sensitive diagnosis will facilitate therapeutic intervention before the appearance of clinical signs and permanent brain damage.
Claudio Soto (University of Texas Medical Branch, Galveston, TX, USA)
For abstract, click here.
(C) Nature Medicine press release.
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