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In human and animal transmissible spongiform encephalopathies (TSEs) or prion disorders, biochemical analysis of disease-associated prion protein (PrPTSE) is a first-line approach for large scale routine testing and for a rapid molecular typing. This characterization is based on conformational properties of PrP enciphered in its secondary and tertiary structures and on glycosylation profile. Several biochemical approaches are helpful in distinguishing PrP forms in human prion diseases. In particular, in sporadic Creutzfedlt-Jakob disease (CJD), PrPTSE is characterized by two main glycotypes conventionally named PrP type 1 and PrP type 2 based on the apparent gel migration at 19 kDa and 17.5 kDa and glycofrom ratio. Further, there are PrP low molecular weight fragments which correlate to distinct phenotypes of sCJD. Finally, by using two-dimensional PAGE analysis, which separates PrP on both isoelectric point and molecular size, we were able to detect two distinct migration pattern in PrP type 2, one in subjects with MM at codon 129 and another in MV, VV. We here provide an extensive PrP biochemical analysis in humans and animals affected with prion disorders. Further, we showed that PrPTSE glycotypes observed in CJD shared similarities with PrP in bovine spongiform encephalopathies (BSEs). These signature similarities obtained by a biochemical analysis had been further confirmed by experimental transmission.

Molecular Signature in Human and Animal Prion Disorders