Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins

Abstract Cell‐to‐cell transmission of protein aggregates is an emerging theme in neurodegenerative disease. Here, we analyze the dipeptide repeat (DPR) proteins that form neuronal inclusions in patients with hexanucleotide repeat expansion C9orf72, the most common known cause of amyotrophic lateral...

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Main Authors: Qihui Zhou, Carina Lehmer, Meike Michaelsen, Kohji Mori, Dominik Alterauge, Dirk Baumjohann, Martin H Schludi, Johanna Greiling, Daniel Farny, Andrew Flatley, Regina Feederle, Stephanie May, Franziska Schreiber, Thomas Arzberger, Christoph Kuhm, Thomas Klopstock, Andreas Hermann, Christian Haass, Dieter Edbauer
Format: Article
Language:English
Published: Springer Nature 2017-03-01
Series:EMBO Molecular Medicine
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Online Access:https://doi.org/10.15252/emmm.201607054
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author Qihui Zhou
Carina Lehmer
Meike Michaelsen
Kohji Mori
Dominik Alterauge
Dirk Baumjohann
Martin H Schludi
Johanna Greiling
Daniel Farny
Andrew Flatley
Regina Feederle
Stephanie May
Franziska Schreiber
Thomas Arzberger
Christoph Kuhm
Thomas Klopstock
Andreas Hermann
Christian Haass
Dieter Edbauer
author_facet Qihui Zhou
Carina Lehmer
Meike Michaelsen
Kohji Mori
Dominik Alterauge
Dirk Baumjohann
Martin H Schludi
Johanna Greiling
Daniel Farny
Andrew Flatley
Regina Feederle
Stephanie May
Franziska Schreiber
Thomas Arzberger
Christoph Kuhm
Thomas Klopstock
Andreas Hermann
Christian Haass
Dieter Edbauer
author_sort Qihui Zhou
collection DOAJ
description Abstract Cell‐to‐cell transmission of protein aggregates is an emerging theme in neurodegenerative disease. Here, we analyze the dipeptide repeat (DPR) proteins that form neuronal inclusions in patients with hexanucleotide repeat expansion C9orf72, the most common known cause of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Sense and antisense transcripts of the (G4C2)n repeat are translated by repeat‐associated non‐ATG (RAN) translation in all reading frames into five aggregating DPR proteins. We show that the hydrophobic DPR proteins poly‐GA, poly‐GP, and poly‐PA are transmitted between cells using co‐culture assays and cell extracts. Moreover, uptake or expression of poly‐GA induces nuclear RNA foci in (G4C2)80‐expressing cells and patient fibroblasts, suggesting an unexpected positive feedback loop. Exposure to recombinant poly‐GA and cerebellar extracts of C9orf72 patients increases repeat RNA levels and seeds aggregation of all DPR proteins in receiver cells expressing (G4C2)80. Treatment with anti‐GA antibodies inhibits intracellular poly‐GA aggregation and blocks the seeding activity of C9orf72 brain extracts. Poly‐GA‐directed immunotherapy may thus reduce DPR aggregation and disease progression in C9orf72 ALS/FTD.
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spelling doaj-art-a6497801d247415ea63dace2fed0150e2025-08-20T03:42:56ZengSpringer NatureEMBO Molecular Medicine1757-46761757-46842017-03-019568770210.15252/emmm.201607054Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteinsQihui Zhou0Carina Lehmer1Meike Michaelsen2Kohji Mori3Dominik Alterauge4Dirk Baumjohann5Martin H Schludi6Johanna Greiling7Daniel Farny8Andrew Flatley9Regina Feederle10Stephanie May11Franziska Schreiber12Thomas Arzberger13Christoph Kuhm14Thomas Klopstock15Andreas Hermann16Christian Haass17Dieter Edbauer18German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)Biomedical Center, Biochemistry, Ludwig Maximilians‐Universität MünchenInstitute for Immunology, Biomedical Center Munich, Ludwig Maximilians‐Universität MünchenInstitute for Immunology, Biomedical Center Munich, Ludwig Maximilians‐Universität MünchenGerman Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)Monoclonal Antibody Core Facility and Research Group, Institute for Diabetes and Obesity, Helmholtz Zentrum München, German Research Center for Environmental Health (GmbH)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)Department of Neurology and Center for Regenerative Therapies Dresden (CRTD), Technische Universität Dresden and German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)Abstract Cell‐to‐cell transmission of protein aggregates is an emerging theme in neurodegenerative disease. Here, we analyze the dipeptide repeat (DPR) proteins that form neuronal inclusions in patients with hexanucleotide repeat expansion C9orf72, the most common known cause of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Sense and antisense transcripts of the (G4C2)n repeat are translated by repeat‐associated non‐ATG (RAN) translation in all reading frames into five aggregating DPR proteins. We show that the hydrophobic DPR proteins poly‐GA, poly‐GP, and poly‐PA are transmitted between cells using co‐culture assays and cell extracts. Moreover, uptake or expression of poly‐GA induces nuclear RNA foci in (G4C2)80‐expressing cells and patient fibroblasts, suggesting an unexpected positive feedback loop. Exposure to recombinant poly‐GA and cerebellar extracts of C9orf72 patients increases repeat RNA levels and seeds aggregation of all DPR proteins in receiver cells expressing (G4C2)80. Treatment with anti‐GA antibodies inhibits intracellular poly‐GA aggregation and blocks the seeding activity of C9orf72 brain extracts. Poly‐GA‐directed immunotherapy may thus reduce DPR aggregation and disease progression in C9orf72 ALS/FTD.https://doi.org/10.15252/emmm.201607054amyotrophic lateral sclerosisC9orf72immunotherapyRAN translationseeding
spellingShingle Qihui Zhou
Carina Lehmer
Meike Michaelsen
Kohji Mori
Dominik Alterauge
Dirk Baumjohann
Martin H Schludi
Johanna Greiling
Daniel Farny
Andrew Flatley
Regina Feederle
Stephanie May
Franziska Schreiber
Thomas Arzberger
Christoph Kuhm
Thomas Klopstock
Andreas Hermann
Christian Haass
Dieter Edbauer
Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins
EMBO Molecular Medicine
amyotrophic lateral sclerosis
C9orf72
immunotherapy
RAN translation
seeding
title Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins
title_full Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins
title_fullStr Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins
title_full_unstemmed Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins
title_short Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins
title_sort antibodies inhibit transmission and aggregation of c9orf72 poly ga dipeptide repeat proteins
topic amyotrophic lateral sclerosis
C9orf72
immunotherapy
RAN translation
seeding
url https://doi.org/10.15252/emmm.201607054
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