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Huntington's disease cerebrospinal fluid seeds aggregation of mutant huntingtin
Journal article   Open access   Peer reviewed

Huntington's disease cerebrospinal fluid seeds aggregation of mutant huntingtin

Z Tan, W Dai, T G M van Erp, J Overman, A Demuro, M A Digman, A Hatami, R Albay, E M Sontag, K T Potkin, …
Molecular psychiatry, Vol.20(11), pp.1286-1293
11/2015
DOI: 10.1038/mp.2015.81
PMCID: PMC4718563
PMID: 26100538
url
https://doi.org/10.1038/mp.2015.81View
Published (Version of record) Open Access

Abstract

Huntington's disease (HD), a progressive neurodegenerative disease, is caused by an expanded CAG triplet repeat producing a mutant huntingtin protein (mHTT) with a polyglutamine-repeat expansion. Onset of symptoms in mutant huntingtin gene-carrying individuals remains unpredictable. We report that synthetic polyglutamine oligomers and cerebrospinal fluid (CSF) from BACHD transgenic rats and from human HD subjects can seed mutant huntingtin aggregation in a cell model and its cell lysate. Our studies demonstrate that seeding requires the mutant huntingtin template and may reflect an underlying prion-like protein propagation mechanism. Light and cryo-electron microscopy show that synthetic seeds nucleate and enhance mutant huntingtin aggregation. This seeding assay distinguishes HD subjects from healthy and non-HD dementia controls without overlap (blinded samples). Ultimately, this seeding property in HD patient CSF may form the basis of a molecular biomarker assay to monitor HD and evaluate therapies that target mHTT.
Animals Cells, Cultured Female Humans Huntingtin Protein Huntington Disease - cerebrospinal fluid Huntington Disease - genetics Male Microscopy, Electron Mutation Nerve Tissue Proteins - genetics Peptides - cerebrospinal fluid Protein Aggregation, Pathological - cerebrospinal fluid Protein Aggregation, Pathological - pathology Rats Rats, Transgenic Transfection

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