Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral Sclerosis

Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy. Mutant FUS incorporates into stress granules (SGs) and can spontaneously form cytoplasmic R...

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Published inCell reports (Cambridge) Vol. 29; no. 13; pp. 4496 - 4508.e4
Main Authors Shelkovnikova, Tatyana A., An, Haiyan, Skelt, Lucy, Tregoning, John S., Humphreys, Ian R., Buchman, Vladimir L.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 24.12.2019
Cell Press
Elsevier
Subjects
Active Transport, Cell Nucleus - genetics
Active Transport, Cell Nucleus - immunology
ALS
amyotrophic lateral sclerosis
Amyotrophic Lateral Sclerosis - immunology
Amyotrophic Lateral Sclerosis - metabolism
Amyotrophic Lateral Sclerosis - pathology
Amyotrophic Lateral Sclerosis - virology
antiviral response
Cell Cycle Proteins - genetics
Cell Cycle Proteins - immunology
Cell Line
Cytoplasmic Granules - genetics
Cytoplasmic Granules - immunology
Cytoplasmic Granules - virology
dopamine
dsRNA
Fibroblasts - cytology
Fibroblasts - drug effects
Fibroblasts - immunology
FUS
FUS proteinopathy
fused in sarcoma
Gene Expression Regulation
Host-Pathogen Interactions - drug effects
Host-Pathogen Interactions - genetics
Host-Pathogen Interactions - immunology
Humans
Inclusion Bodies - genetics
Inclusion Bodies - immunology
Inclusion Bodies - virology
Interferon Type I - genetics
Interferon Type I - immunology
Male
Membrane Transport Proteins - genetics
Membrane Transport Proteins - immunology
Motor Neurons - immunology
Motor Neurons - metabolism
Motor Neurons - virology
Neuroglia - immunology
Neuroglia - metabolism
Neuroglia - virology
nucleocytoplasmic transport
Nucleocytoplasmic Transport Proteins - genetics
Nucleocytoplasmic Transport Proteins - immunology
optineurin
Poly I-C - pharmacology
Primary Cell Culture
Protein Aggregates - genetics
Protein Aggregates - immunology
Respiratory Syncytial Virus
Respiratory Syncytial Viruses - immunology
Respiratory Syncytial Viruses - pathogenicity
RNA granule
RNA Stability
RNA, Messenger - genetics
RNA, Messenger - immunology
RNA-Binding Protein FUS - genetics
RNA-Binding Protein FUS - immunology
Spinal Cord - immunology
Spinal Cord - metabolism
Spinal Cord - pathology
Spinal Cord - virology
stress granule
dsRNA
Respiratory Syncytial Virus
FUS
stress granule
RNA granule
ALS
FUS proteinopathy
amyotrophic lateral sclerosis
fused in sarcoma
antiviral response
optineurin
nucleocytoplasmic transport
dopamine
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Abstract Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy. Mutant FUS incorporates into stress granules (SGs) and can spontaneously form cytoplasmic RNA granules in cultured cells. However, it is unclear what can trigger the persistence of mutant FUS assemblies and lead to inclusion formation. Using CRISPR/Cas9 cell lines and patient fibroblasts, we find that the viral mimic dsRNA poly(I:C) or a SG-inducing virus causes the sustained presence of mutant FUS assemblies. These assemblies sequester the autophagy receptor optineurin and nucleocytoplasmic transport factors. Furthermore, an integral component of the antiviral immune response, type I interferon, promotes FUS protein accumulation by increasing FUS mRNA stability. Finally, mutant FUS-expressing cells are hypersensitive to dsRNA toxicity. Our data suggest that the antiviral immune response is a plausible second hit for FUS proteinopathy. [Display omitted] •Viral infection or its mimic induce large, persistent assemblies of mutant FUS•These assemblies sequester optineurin and nucleocytoplasmic transport factors•Mutant FUS-expressing cells are hypersensitive to virus-induced toxicity•Type I interferon induced by viral infections promotes accumulation of FUS protein Amyotrophic lateral sclerosis caused by mutations in the FUS gene is characterized by cytoplasmic FUS pathology (FUS proteinopathy). Shelkovnikova et al. find that the antiviral immune response promotes FUS protein accumulation and its coalescence into persistent cytoplasmic assemblies. Viral infection can serve as a trigger of FUS proteinopathy in ALS.
AbstractList Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy. Mutant FUS incorporates into stress granules (SGs) and can spontaneously form cytoplasmic RNA granules in cultured cells. However, it is unclear what can trigger the persistence of mutant FUS assemblies and lead to inclusion formation. Using CRISPR/Cas9 cell lines and patient fibroblasts, we find that the viral mimic dsRNA poly(I:C) or a SG-inducing virus causes the sustained presence of mutant FUS assemblies. These assemblies sequester the autophagy receptor optineurin and nucleocytoplasmic transport factors. Furthermore, an integral component of the antiviral immune response, type I interferon, promotes FUS protein accumulation by increasing FUS mRNA stability. Finally, mutant FUS-expressing cells are hypersensitive to dsRNA toxicity. Our data suggest that the antiviral immune response is a plausible second hit for FUS proteinopathy.
Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy. Mutant FUS incorporates into stress granules (SGs) and can spontaneously form cytoplasmic RNA granules in cultured cells. However, it is unclear what can trigger the persistence of mutant FUS assemblies and lead to inclusion formation. Using CRISPR/Cas9 cell lines and patient fibroblasts, we find that the viral mimic dsRNA poly(I:C) or a SG-inducing virus causes the sustained presence of mutant FUS assemblies. These assemblies sequester the autophagy receptor optineurin and nucleocytoplasmic transport factors. Furthermore, an integral component of the antiviral immune response, type I interferon, promotes FUS protein accumulation by increasing FUS mRNA stability. Finally, mutant FUS-expressing cells are hypersensitive to dsRNA toxicity. Our data suggest that the antiviral immune response is a plausible second hit for FUS proteinopathy. : Amyotrophic lateral sclerosis caused by mutations in the FUS gene is characterized by cytoplasmic FUS pathology (FUS proteinopathy). Shelkovnikova et al. find that the antiviral immune response promotes FUS protein accumulation and its coalescence into persistent cytoplasmic assemblies. Viral infection can serve as a trigger of FUS proteinopathy in ALS. Keywords: fused in sarcoma, FUS, dopamine, amyotrophic lateral sclerosis, ALS, stress granule, FUS proteinopathy, antiviral response, dsRNA, optineurin, nucleocytoplasmic transport, Respiratory Syncytial Virus, RNA granule
Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy. Mutant FUS incorporates into stress granules (SGs) and can spontaneously form cytoplasmic RNA granules in cultured cells. However, it is unclear what can trigger the persistence of mutant FUS assemblies and lead to inclusion formation. Using CRISPR/Cas9 cell lines and patient fibroblasts, we find that the viral mimic dsRNA poly(I:C) or a SG-inducing virus causes the sustained presence of mutant FUS assemblies. These assemblies sequester the autophagy receptor optineurin and nucleocytoplasmic transport factors. Furthermore, an integral component of the antiviral immune response, type I interferon, promotes FUS protein accumulation by increasing FUS mRNA stability. Finally, mutant FUS-expressing cells are hypersensitive to dsRNA toxicity. Our data suggest that the antiviral immune response is a plausible second hit for FUS proteinopathy. [Display omitted] •Viral infection or its mimic induce large, persistent assemblies of mutant FUS•These assemblies sequester optineurin and nucleocytoplasmic transport factors•Mutant FUS-expressing cells are hypersensitive to virus-induced toxicity•Type I interferon induced by viral infections promotes accumulation of FUS protein Amyotrophic lateral sclerosis caused by mutations in the FUS gene is characterized by cytoplasmic FUS pathology (FUS proteinopathy). Shelkovnikova et al. find that the antiviral immune response promotes FUS protein accumulation and its coalescence into persistent cytoplasmic assemblies. Viral infection can serve as a trigger of FUS proteinopathy in ALS.
Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy. Mutant FUS incorporates into stress granules (SGs) and can spontaneously form cytoplasmic RNA granules in cultured cells. However, it is unclear what can trigger the persistence of mutant FUS assemblies and lead to inclusion formation. Using CRISPR/Cas9 cell lines and patient fibroblasts, we find that the viral mimic dsRNA poly(I:C) or a SG-inducing virus causes the sustained presence of mutant FUS assemblies. These assemblies sequester the autophagy receptor optineurin and nucleocytoplasmic transport factors. Furthermore, an integral component of the antiviral immune response, type I interferon, promotes FUS protein accumulation by increasing FUS mRNA stability. Finally, mutant FUS-expressing cells are hypersensitive to dsRNA toxicity. Our data suggest that the antiviral immune response is a plausible second hit for FUS proteinopathy. • Viral infection or its mimic induce large, persistent assemblies of mutant FUS • These assemblies sequester optineurin and nucleocytoplasmic transport factors • Mutant FUS-expressing cells are hypersensitive to virus-induced toxicity • Type I interferon induced by viral infections promotes accumulation of FUS protein Amyotrophic lateral sclerosis caused by mutations in the FUS gene is characterized by cytoplasmic FUS pathology (FUS proteinopathy). Shelkovnikova et al. find that the antiviral immune response promotes FUS protein accumulation and its coalescence into persistent cytoplasmic assemblies. Viral infection can serve as a trigger of FUS proteinopathy in ALS.
Author Tregoning, John S.
Buchman, Vladimir L.
An, Haiyan
Shelkovnikova, Tatyana A.
Skelt, Lucy
Humphreys, Ian R.
AuthorAffiliation 2 Medicines Discovery Institute, Cardiff University, Cardiff CF10 3AT, UK
4 Systems Immunity Research Institute, School of Medicine, Cardiff University, Cardiff CF14 4XN, UK
3 Department of Infectious Disease, St Mary’s Campus, Imperial College London, London W2 1PG, UK
5 Institute of Physiologically Active Compounds of RAS, Chernogolovka 142432, Russian Federation
1 Biomedicine Division, School of Biosciences, Cardiff University, Cardiff CF10 3AX, UK
AuthorAffiliation_xml – name: 3 Department of Infectious Disease, St Mary’s Campus, Imperial College London, London W2 1PG, UK
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  surname: Skelt
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  givenname: Vladimir L.
  surname: Buchman
  fullname: Buchman, Vladimir L.
  email: buchmanvl@cardiff.ac.uk
  organization: Biomedicine Division, School of Biosciences, Cardiff University, Cardiff CF10 3AX, UK
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31875556$$D View this record in MEDLINE/PubMed
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Issue 13
Keywords dsRNA
Respiratory Syncytial Virus
FUS
stress granule
RNA granule
ALS
FUS proteinopathy
amyotrophic lateral sclerosis
fused in sarcoma
antiviral response
optineurin
nucleocytoplasmic transport
dopamine
Language English
License This is an open access article under the CC BY license.
Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.
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These authors contributed equally
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Snippet Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons...
Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons...
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SubjectTerms Active Transport, Cell Nucleus - genetics
Active Transport, Cell Nucleus - immunology
ALS
amyotrophic lateral sclerosis
Amyotrophic Lateral Sclerosis - immunology
Amyotrophic Lateral Sclerosis - metabolism
Amyotrophic Lateral Sclerosis - pathology
Amyotrophic Lateral Sclerosis - virology
antiviral response
Cell Cycle Proteins - genetics
Cell Cycle Proteins - immunology
Cell Line
Cytoplasmic Granules - genetics
Cytoplasmic Granules - immunology
Cytoplasmic Granules - virology
dopamine
dsRNA
Fibroblasts - cytology
Fibroblasts - drug effects
Fibroblasts - immunology
FUS
FUS proteinopathy
fused in sarcoma
Gene Expression Regulation
Host-Pathogen Interactions - drug effects
Host-Pathogen Interactions - genetics
Host-Pathogen Interactions - immunology
Humans
Inclusion Bodies - genetics
Inclusion Bodies - immunology
Inclusion Bodies - virology
Interferon Type I - genetics
Interferon Type I - immunology
Male
Membrane Transport Proteins - genetics
Membrane Transport Proteins - immunology
Motor Neurons - immunology
Motor Neurons - metabolism
Motor Neurons - virology
Neuroglia - immunology
Neuroglia - metabolism
Neuroglia - virology
nucleocytoplasmic transport
Nucleocytoplasmic Transport Proteins - genetics
Nucleocytoplasmic Transport Proteins - immunology
optineurin
Poly I-C - pharmacology
Primary Cell Culture
Protein Aggregates - genetics
Protein Aggregates - immunology
Respiratory Syncytial Virus
Respiratory Syncytial Viruses - immunology
Respiratory Syncytial Viruses - pathogenicity
RNA granule
RNA Stability
RNA, Messenger - genetics
RNA, Messenger - immunology
RNA-Binding Protein FUS - genetics
RNA-Binding Protein FUS - immunology
Spinal Cord - immunology
Spinal Cord - metabolism
Spinal Cord - pathology
Spinal Cord - virology
stress granule
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Title Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral Sclerosis
URI https://dx.doi.org/10.1016/j.celrep.2019.11.094
https://www.ncbi.nlm.nih.gov/pubmed/31875556
https://pubmed.ncbi.nlm.nih.gov/PMC6941233
https://doaj.org/article/44b362b201e6491bbd5c03b86903760f
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