Endogenous retroviruses and TDP-43 proteinopathy form a sustaining feedback driving intercellular spread of Drosophila neurodegeneration
Open accessAbstract
Inter-cellular movement of “prion-like” proteins is thought to explain propagation of neurodegeneration between cells. For example, propagation of abnormally phosphorylated cytoplasmic inclusions of TAR-DNA-Binding protein (TDP-43) is proposed to underlie progression of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). But unlike transmissible prion diseases, ALS and FTD are not infectious and injection of aggregated TDP-43 is not sufficient to cause disease. This suggests a missing component of a positive feedback necessary to sustain disease progression. We demonstrate that endogenous retrovirus (ERV) expression and TDP-43 proteinopathy are mutually reinforcing. Expression of either Drosophila mdg4-ERV (gypsy) or the human ERV, HERV-K (HML-2) are each sufficient to stimulate cytoplasmic aggregation of human TDP-43. Viral ERV transmission also triggers TDP-43 pathology in recipient cells that express physiological levels of TDP-43, whether they are in contact or at a distance. This mechanism potentially underlies the TDP-43 proteinopathy-caused neurodegenerative propagation through neuronal tissue.
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Expression of HERV-K in SH-SY5Y cells is associated with reduced expression of Stathmin-2 (STMN2) and POLDIP3α, two established targets of TDP-43.
“This is associated with reduced expression of Stathmin-2 (STMN2) and POLDIP3α, two established targets of TDP-43.”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
Expression of HERV-K in SH-SY5Y human neuroblastoma cells is sufficient to trigger nuclear clearance of TDP-43 and accumulation of hyperphosphorylated pathological TDP-43 in the cytoplasm.
“Expression of HERV-K in SH-SY5Y human neuroblastoma cells is sufficient to trigger nuclear clearance of TDP-43 and accumulation of hyperphosphorylated pathological TDP-43 in the cytoplasm (Chang & Dubnau 2023).”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
mdg4-ERV expression in Drosophila S2 cells triggers the accumulation of cytoplasmic inclusions of hyperphosphorylated human TDP-43.
“Similarly, mdg4-ERV expression in Drosophila S2 cells triggers the accumulation of cytoplasmic inclusions of hyperphosphorylated human TDP-43 (Chang & Dubnau 2023).”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
Overexpression of human TDP-43 in Drosophila surface glia results in the accumulation of hyperphosphorylated human TDP-43 in nearby neurons, even though the neurons only express physiological levels of human TDP-43.
“Overexpression of human TDP-43 in Drosophila surface glia results in the accumulation of hyperphosphorylated human TDP-43 in nearby neurons, even though the neurons only express physiological levels of human TDP-43 (Chang & Dubnau 2023).”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
When human Drosophila S2 cells expressing human TDP-43 are grown in the presence of cells expressing a fluorescently tagged mdg4-ERV, they can become infected with the tagged ERV, triggering the loss of nuclear TDP-43 and the accumulation of cytoplasmic phosphorylated TDP-43 in the recipient cells.
“When human Drosophila S2 cells expressing human TDP-43 are grown in the presence of cells expressing a fluorescently tagged mdg4-ERV, they can become infected with the tagged ERV, triggering the loss of nuclear TDP-43 and the accumulation of cytoplasmic phosphorylated TDP-43 in the recipient cells (Chang & Dubnau 2023).”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
This non-cell-autonomous propagation of TDP-43 pathology requires the expression of the mdg4-ERV in glia.
“This non-cell-autonomous propagation of TDP-43 pathology requires the expression of the mdg4-ERV in glia.”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
A similar phenomenology underlies the propagation of TDP-43-mediated toxicity from Drosophila glial cells to neurons in vivo.
“A similar phenomenology underlies the propagation of TDP-43-mediated toxicity from Drosophila glial cells to neurons in vivo.”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Chang & Dubnau 2023
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Arc mediates intercellular tau transmission via extracellular vesicles
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The Scientific and Therapeutic Rationale for Off‐Label Treatments in Amyotrophic Lateral Sclerosis
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Glial reactivity and cognitive decline follow chronic heterochromatin loss in neurons
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Virus-like particles of retroviral origin in protein aggregation and neurodegenerative diseases
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TYK2 as a novel therapeutic target in Alzheimer’s Disease with TDP-43 inclusionsPreprint
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Self-citationDrosophila appear resistant to trans-synaptic tau propagation
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Dynamic dysregulation of retrotransposons in neurodegenerative diseases at the single-cell levelPreprint
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TDP-43: [GU]-ardian of the transcriptome
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Endogenous retroviruses can propagate TDP-43 proteinopathy
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Meeting report: transposable elements at the crossroads of evolution, health and disease 2023
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Inclusion body myositis, viral infections, and TDP-43: a narrative review
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Retrotransposons in embryogenesis and neurodevelopment
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Role of Retroelements in Frontotemporal Dementia Development
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The retroelement-derived human protein PEG10 is a regulator of mRNA splicing in neuronsPreprint
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Self-citationThe Role of Transposable Elements in Therapeutics
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TYK2 mediates neuroinflammation in Alzheimer’s disease brains with TDP-43 pathology
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Modulation of retroviral capsid assembly halts ARC-mediated TDP-43 intercellular spreadingPreprint
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HUSH, NEXT PROMPT: Epigenetics and the Nuclear RNA Exosome in Human Aging and Disease
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Glial cell toxicity in a Drosophila C9orf72 neurodegeneration model
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- Authors
- Chang, Y.-H., & Dubnau, J.
- Affiliations
- Stony Brook School (US)
- Corresponding author
- Chang, Yung-Heng
- Dubnau, Josh
- Venue
- Nature Communications
- Published
- 2023-02-21
- Volume
- 14
- Issue
- 1
- Pages
- 966-966
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9944888
- OpenAlex
- W4321446819
- Cited by
- 49
- References
- 67
- Citations by year
- 2026: 14 · 2025: 15 · 2024: 14 · 2023: 6
- FWCI
- 8.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute on Aging (R01AG078788, RF1AG076493, RF1AG057338)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- endogenous retroviruses, TDP-43 proteinopathy, intercellular spread, amyotrophic lateral sclerosis, frontotemporal dementia, prion-like proteins, positive feedback, HERV-K, TDP-43 aggregation, Drosophila
- MeSH terms
- Amyotrophic Lateral Sclerosis, Animals, DNA-Binding Proteins, Drosophila, Feedback, Humans, Endogenous Retroviruses, TDP-43 Proteinopathies, Frontotemporal Dementia
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