α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties Article Swipe
Surabhi Mehra
,
Sahil Ahlawat
,
Harish Kumar
,
Nitu Singh
,
Ambuja Navalkar
,
Komal Patel
,
Pradeep Kadu
,
Rakesh Kumar
,
Narendra Nath Jha
,
Jayant B. Udgaonkar
,
Vipin Agarwal
,
Samir K. Maji
·
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1101/2020.05.03.074765
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1101/2020.05.03.074765
α-Synuclein (α-Syn) amyloid fibrils in synucleinopathies (such as Parkinson’s disease (PD), multiple system atrophy (MSA)) are structurally and functionally different, reminiscent of prion-like strains. However, how a single protein can form different fibril polymorphs in various synucleinopathies is not known. Here, we demonstrate the structure-function relationship of two distinct α-Syn fibril polymorphs, the pre-matured fibrils (PMF) and helix-matured fibrils (HMF) based on α-Syn aggregation intermediates. These polymorphs not only display the structural differences, including their fibril core structure as demonstrated by solid-state nuclear magnetic resonance (NMR) spectroscopy and H/D-exchange coupled with mass spectrometry but also possess different cellular activities such as seeding, cellular internalization, and cell-to-cell transmission. The HMF with a compact core structure exhibits low seeding potency in cells but readily internalizes and transmits from one cell to another. Whereas the less structured PMF lacks the cell-to-cell transmission ability but induces abundant α-Syn pathology and triggers the formation of aggresomes in cells . Overall, the study highlights how the conformational heterogeneity in the aggregation pathway may lead to fibril polymorphs with distinct prion-like behavior in PD.
Related Topics
Concepts
Fibril
Synucleinopathies
Chemistry
Biophysics
Nuclear magnetic resonance spectroscopy
Internalization
Alpha-synuclein
Crystallography
Cell
Biochemistry
Stereochemistry
Biology
Pathology
Disease
Medicine
Parkinson's disease
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2020.05.03.074765
- https://www.biorxiv.org/content/biorxiv/early/2020/05/05/2020.05.03.074765.full.pdf
- OA Status
- green
- Cited By
- 7
- References
- 68
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3022140978
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W3022140978Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2020.05.03.074765Digital Object Identifier
- Title
-
α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like propertiesWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2020Year of publication
- Publication date
-
2020-05-04Full publication date if available
- Authors
-
Surabhi Mehra, Sahil Ahlawat, Harish Kumar, Nitu Singh, Ambuja Navalkar, Komal Patel, Pradeep Kadu, Rakesh Kumar, Narendra Nath Jha, Jayant B. Udgaonkar, Vipin Agarwal, Samir K. MajiList of authors in order
- Landing page
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https://doi.org/10.1101/2020.05.03.074765Publisher landing page
- PDF URL
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https://www.biorxiv.org/content/biorxiv/early/2020/05/05/2020.05.03.074765.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2020/05/05/2020.05.03.074765.full.pdfDirect OA link when available
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Fibril, Synucleinopathies, Chemistry, Biophysics, Nuclear magnetic resonance spectroscopy, Internalization, Alpha-synuclein, Crystallography, Cell, Biochemistry, Stereochemistry, Biology, Pathology, Disease, Medicine, Parkinson's diseaseTop concepts (fields/topics) attached by OpenAlex
- Cited by
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7Total citation count in OpenAlex
- Citations by year (recent)
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2024: 1, 2022: 3, 2021: 3Per-year citation counts (last 5 years)
- References (count)
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68Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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