ArticlePLoS pathogens2019
TDP-43 proteinopathy in Theiler's murine encephalomyelitis virus infection.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- TDP-43 promotes efficient HSV-1 replication in human DRG-derived neurons.Journal of virology · 2025Article
- TDP43 augments astrocyte inflammatory activity through mtDNA-cGAS-STING axis in NMOSD.Journal of neuroinflammation · 2025Article
- Underestimated virus impaired cognition-more evidence and more work to do.Frontiers in immunology · 2025Review
- Implications of TDP-43 in non-neuronal systems.Cell communication and signaling : CCS · 2023Review
- Reviewing the Potential Links between Viral Infections and TDP-43 Proteinopathies.International journal of molecular sciences · 2023Review
- Viruses in neurodegenerative diseases: More than just suspects in crimes.PLoS pathogens · 2022Review
- Protein clearance strategies for disease intervention.Journal of neural transmission (Vienna, Austria : 1996) · 2022Review
- Glial TDP-43 and TDP-43 induced glial pathology, focus on neurodegenerative proteinopathy syndromes.Glia · 2022Review
- Ribosomal control in RNA virus-infected cells.Frontiers in microbiology · 2022Review
- Pro-Inflammatory Cytokines and Antibodies Induce hnRNP A1 Dysfunction in Mouse Primary Cortical Neurons.Brain sciences · 2021Article
- FUS/TLS Suppresses Enterovirus Replication and Promotes Antiviral Innate Immune Responses.Journal of virology · 2021Article
- TAR DNA-Binding Protein 43 is Cleaved by the Protease 3C of Enterovirus A71.Virologica Sinica · 2021Article
- A Deletion of the Nuclear Localization Signal Domain in the Fus Protein Induces Stable Post-stress Cytoplasmic Inclusions in SH-SY5Y Cells.Frontiers in neuroscience · 2021Article
- Microbial Infections Are a Risk Factor for Neurodegenerative Diseases.Frontiers in cellular neuroscience · 2021Review
- Neuronal RNA-binding protein dysfunction in multiple sclerosis cortex.Annals of clinical and translational neurology · 2020Article
- The Potential Contribution of Dysfunctional RNA-Binding Proteins to the Pathogenesis of Neurodegeneration in Multiple Sclerosis and Relevant Models.International journal of molecular sciences · 2020Review
- RNA-binding protein altered expression and mislocalization in MS.Neurology(R) neuroimmunology & neuroinflammation · 2020Article
- Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral Sclerosis.Cell reports · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
TDP-43, an RNA-binding protein that is primarily nuclear and important in splicing and RNA metabolism, is mislocalized from the nucleus to the cytoplasm of neural cells in amyotrophic lateral sclerosis (ALS), and contributes to disease. We sought to investigate whether TDP-43 is mislocalized in infections with the acute neuronal GDVII strain and the persistent demyelinating DA strain of Theiler's virus murine encephalomyelitis virus (TMEV), a member of the Cardiovirus genus of Picornaviridae because: i) L protein of both strains is known to disrupt nucleocytoplasmic transport, including transport of polypyrimidine tract binding protein, an RNA-binding protein, ii) motor neurons and oligodendrocytes are targeted in both TMEV infection and ALS. TDP-43 phosphorylation, cleavage, and cytoplasmic mislocalization to an aggresome were observed in wild type TMEV-infected cultured cells, with predicted splicing abnormalities. In contrast, cells infected with DA and GDVII strains that have L deletion had rare TDP-43 mislocalization and no aggresome formation. TDP-43 mislocalization was also present in neural cells of TMEV acutely-infected mice. Of note, TDP-43 was mislocalized six weeks after DA infection to the cytoplasm of oligodendrocytes and other glial cells in demyelinating lesions of spinal white matter. A recent study showed that TDP-43 knock down in oligodendrocytes in mice led to demyelination and death of this neural cell [1], suggesting that TMEV infection mislocalization of TDP-43 and other RNA-binding proteins is predicted to disrupt key cellular processes and contribute to the pathogenesis of TMEV-induced diseases. Drugs that inhibit nuclear export may have a role in antiviral therapy.
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Registered trials
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