TDP-43 amyloids in neurodegenerative diseases

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• Diana Arseni, MRC-Laboratory of Molecular Biology
• Thursday 21 October 2021, 13:00-14:00
• Richard King Room.

If you have a question about this talk, please contact Laura Pellegrini.

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My research interests lie in understanding the structure of pathological protein assembly in neurodegenerative diseases, including Alzheimer’s disease and other dementias, with the goal of translating findings into new therapies and improving human health. Neurodegeneration involves progressive damage of the nervous system leading to loss of cognitive abilities and/or motor functions. Currently there are no available treatments, indicating that neurodegeneration is one of the world’s most pressing medical and societal challenges.

Pathological assemblies in neurodegeneration are formed from a small number of proteins that can bind to each other and form amyloid filamentous structures. Filaments accumulate in neurons and occasionally in glia or form extracellular plaques, leading to cell death. Examples include β-amyloid and tau proteins in Alzheimer’s disease, -synuclein protein in Parkinson’s disease and TDP -43 protein in amyotrophic lateral sclerosis (ALS) and multiple forms of frontotemporal lobar degeneration (FTLD). ALS is the most common adult-onset motor neuron disease and FTLD is the second most common form of dementia after Alzheimer’s disease. We use cryo-electron microscopy to determine the structures of aggregated TDP -43 extracted from patients’ brain. Recently, we uncovered the first structure of aggregated TDP -43 from human brain. This work enhances our understanding of the molecular pathogenesis of ALS and FTLD and informs the development of diagnostic and therapeutic agents targeting TDP -43 aggregates.

This talk is part of the Lunchtime Science Seminars series.

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