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.
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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.
|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
|DDC:||570 Life sciences; biology|
610 Medicine & health
|Deposited On:||20 Jan 2011 09:32|
|Last Modified:||28 Nov 2013 00:27|
|Citations:||Web of Science®. Times Cited: 6|
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