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@ARTICLE{Mehra:271073,
author = {Mehra, Surabhi and Bourkas, Matthew Ec and Kaczmarczyk,
Lech and Stuart, Erica and Arshad, Hamza and Griffin,
Jennifer K and Frost, Kathy L and Walsh, Daniel J and
Supattapone, Surachai and Booth, Stephanie A and Jackson,
Walker Scot and Watts, Joel C},
title = {{C}onvergent generation of atypical prions in knockin mouse
models of genetic prion disease.},
journal = {The journal of clinical investigation},
volume = {134},
number = {15},
issn = {0021-9738},
address = {Ann Arbor, Mich.},
publisher = {ASCJ},
reportid = {DZNE-2024-00945},
pages = {e176344},
year = {2024},
abstract = {Most cases of human prion disease arise due to spontaneous
misfolding of WT or mutant prion protein, yet recapitulating
this event in animal models has proven challenging. It
remains unclear whether spontaneous prion generation can
occur within the mouse lifespan in the absence of protein
overexpression and how disease-causing mutations affect
prion strain properties. To address these issues, we
generated knockin mice that express the misfolding-prone
bank vole prion protein (BVPrP). While mice expressing WT
BVPrP (I109 variant) remained free from neurological
disease, a subset of mice expressing BVPrP with mutations
(D178N or E200K) causing genetic prion disease developed
progressive neurological illness. Brains from spontaneously
ill knockin mice contained prion disease-specific
neuropathological changes as well as atypical
protease-resistant BVPrP. Moreover, brain extracts from
spontaneously ill D178N- or E200K-mutant BVPrP-knockin mice
exhibited prion seeding activity and transmitted disease to
mice expressing WT BVPrP. Surprisingly, the properties of
the D178N- and E200K-mutant prions appeared identical before
and after transmission, suggesting that both mutations guide
the formation of a similar atypical prion strain. These
findings imply that knockin mice expressing mutant BVPrP
spontaneously develop a bona fide prion disease and that
mutations causing prion diseases may share a uniform initial
mechanism of action.},
keywords = {Animals / Mice / Prion Diseases: genetics / Prion Diseases:
pathology / Prion Diseases: metabolism / Gene Knock-In
Techniques / Disease Models, Animal / Mice, Transgenic /
Prion Proteins: genetics / Prion Proteins: metabolism /
Brain: metabolism / Brain: pathology / Mutation, Missense /
Humans / Arvicolinae: genetics / Arvicolinae: metabolism /
Amino Acid Substitution / Prions: genetics / Prions:
metabolism / Protein Folding / Neurodegeneration (Other) /
Neuroscience (Other) / Prions (Other) / Prion Proteins (NLM
Chemicals) / Prions (NLM Chemicals)},
cin = {AG Jackson},
ddc = {610},
cid = {I:(DE-2719)1013019},
pnm = {352 - Disease Mechanisms (POF4-352)},
pid = {G:(DE-HGF)POF4-352},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:39087478},
pmc = {pmc:PMC11291267},
doi = {10.1172/JCI176344},
url = {https://pub.dzne.de/record/271073},
}