Quick Search:

uzh logo
Browse by:
bullet
bullet
bullet
bullet

Zurich Open Repository and Archive 

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.

[img]PDF - Registered users only
1502Kb

Abstract

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
Language:English
Date:2011
Deposited On:20 Jan 2011 09:32
Last Modified:28 Nov 2013 00:27
Publisher:Wiley-Blackwell
ISSN:1015-6305
Publisher DOI:10.1111/j.1750-3639.2010.00439.x
PubMed ID:20875062
Citations:Web of Science®. Times Cited: 6
Google Scholar™

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page