Abstract
A new procedure for amplification of prion proteins has been described by researchers from Geneva, Switzerland. Reporting in the June 14 issue of Nature, Soto and colleagues present a technique analogous to PCR cycling that involves cyclic amplification of protein misfolding. This allows rapid conversion of a large excess of PrPc (the normal cell surface protein) into a proteasome-resistant, PrPSc-like form in the presence of minute quantities of PrPSc template (the abnormal protein and principal component of prions). Currently available methods of PrPSc detection are limited by the low amounts of abnormal protein. Therefore, this new method could lead to a diagnostic test for the presence of prions in tissue and biological fluids. CJ
Published Version
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