Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-39979
Polymenidou, M; Prokop, S; Jung, H H; Hewer, E; Peretz, D; Moos, R; Tolnay, M; Aguzzi, A (2011). Atypical prion protein conformation in familial prion disease with PRNP P105T mutation. Brain Pathology, 21(2):209-214.
- Registered users only
View at publisher
Protease-resistant prion protein (PrP(Sc) ) is diagnostic of prion disease, yet its detection is frequently difficult. Here, we describe a patient with a PRNP P105T mutation and typical familial prion disease. Brain PrP(Sc) was undetectable by conventional Western blotting and barely detectable after phosphotungstate precipitation, where it displayed an atypical pattern suggestive of noncanonical conformation. Therefore, we used a novel misfolded protein assay (MPA) that detects PrP aggregates independently of their protease resistance. The MPA revealed the presence of aggregated PrP in similar amounts as in typical sporadic Creutzfeldt-Jakob disease. These findings suggest that measurements of PrP aggregation with the MPA may be potentially more sensitive than protease-based methodologies.
6 downloads since deposited on 20 Jan 2011
1 download since 12 months
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > University Hospital Zurich > Clinic for Neurology
04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
|Dewey Decimal Classification:||570 Life sciences; biology
610 Medicine & health
|Deposited On:||20 Jan 2011 08:32|
|Last Modified:||27 Nov 2013 23:27|
Users (please log in): suggest update or correction for this item
Repository Staff Only: item control page