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26 April 2024 |
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Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity | | G C Telling
; P Parchi
; S J DeArmond
; P Cortelli
; P Montagna
; R Gabizon
; J Mastrianni
; E Lugaresi
; P Gambetti
; S B Prusiner
; | | Date: |
20 Dec 1996 | | Journal: | Science, 274 (5295), 2079-82 | | Abstract: | The fundamental event in prion diseases seems to be a conformational change in cellular prion protein (PrPC) whereby it is converted into the pathologic isoform PrPSc. In fatal familial insomnia (FFI), the protease-resistant fragment of PrPSc after deglycosylation has a size of 19 kilodaltons, whereas that from other inherited and sporadic prion diseases is 21 kilodaltons. Extracts from the brains of FFI patients transmitted disease to transgenic mice expressing a chimeric human-mouse PrP gene about 200 days after inoculation and induced formation of the 19-kilodalton PrPSc fragment, whereas extracts from the brains of familial and sporadic Creutzfeldt-Jakob disease patients produced the 21-kilodalton PrPSc fragment in these mice. The results presented indicate that the conformation of PrPSc functions as a template in directing the formation of nascent PrPSc and suggest a mechanism to explain strains of prions where diversity is encrypted in the conformation of PrPSc. | | Source: | PubMed, pmid8953038 | | Services: | Forum | Review | Favorites | |
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