An in vivo Caenorhabditis elegans model for therapeutic research in human prion diseases

Human prion diseases are fatal neurodegenerative disorders that include sporadic, infectious and genetic forms. Inherited Creutzfeldt-Jakob disease due to the E200K mutation of the prion protein-coding gene is the most common form of genetic prion disease. The phenotype resembles that of sporadic Cr...

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Veröffentlicht in:Brain (London, England : 1878) England : 1878), 2021-10, Vol.144 (9), p.2745-2758
Hauptverfasser: Bizat, Nicolas, Parrales, Valeria, Laoues, Sofian, Normant, Sébastien, Levavasseur, Etienne, Roussel, Julian, Privat, Nicolas, Gougerot, Alexianne, Ravassard, Philippe, Beaudry, Patrice, Brandel, Jean-Philippe, Laplanche, Jean-Louis, Haïk, Stéphane
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container_title Brain (London, England : 1878)
container_volume 144
creator Bizat, Nicolas
Parrales, Valeria
Laoues, Sofian
Normant, Sébastien
Levavasseur, Etienne
Roussel, Julian
Privat, Nicolas
Gougerot, Alexianne
Ravassard, Philippe
Beaudry, Patrice
Brandel, Jean-Philippe
Laplanche, Jean-Louis
Haïk, Stéphane
description Human prion diseases are fatal neurodegenerative disorders that include sporadic, infectious and genetic forms. Inherited Creutzfeldt-Jakob disease due to the E200K mutation of the prion protein-coding gene is the most common form of genetic prion disease. The phenotype resembles that of sporadic Creutzfeldt-Jakob disease at both the clinical and pathological levels, with a median disease duration of 4 months. To date, there is no available treatment for delaying the occurrence or slowing the progression of human prion diseases. Existing in vivo models do not allow high-throughput approaches that may facilitate the discovery of compounds targeting pathological assemblies of human prion protein or their effects on neuronal survival. Here, we generated a genetic model in the nematode Caenorhabditis elegans, which is devoid of any homologue of the prion protein, by expressing human prion protein with the E200K mutation in the mechanosensitive neuronal system. Expression of E200K prion protein induced a specific behavioural pattern and neurodegeneration of green fluorescent protein-expressing mechanosensitive neurons, in addition to the formation of intraneuronal inclusions associated with the accumulation of a protease-resistant form of the prion protein. We demonstrated that this experimental system is a powerful tool for investigating the efficacy of anti-prion compounds on both prion-induced neurodegeneration and prion protein misfolding, as well as in the context of human prion protein. Within a library of 320 compounds that have been approved for human use and cross the blood-brain barrier, we identified five molecules that were active against the aggregation of the E200K prion protein and the neurodegeneration it induced in transgenic animals. This model breaks a technological limitation in prion therapeutic research and provides a key tool to study the deleterious effects of misfolded prion protein in a well-described neuronal system.
doi_str_mv 10.1093/brain/awab152
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Inherited Creutzfeldt-Jakob disease due to the E200K mutation of the prion protein-coding gene is the most common form of genetic prion disease. The phenotype resembles that of sporadic Creutzfeldt-Jakob disease at both the clinical and pathological levels, with a median disease duration of 4 months. To date, there is no available treatment for delaying the occurrence or slowing the progression of human prion diseases. Existing in vivo models do not allow high-throughput approaches that may facilitate the discovery of compounds targeting pathological assemblies of human prion protein or their effects on neuronal survival. Here, we generated a genetic model in the nematode Caenorhabditis elegans, which is devoid of any homologue of the prion protein, by expressing human prion protein with the E200K mutation in the mechanosensitive neuronal system. Expression of E200K prion protein induced a specific behavioural pattern and neurodegeneration of green fluorescent protein-expressing mechanosensitive neurons, in addition to the formation of intraneuronal inclusions associated with the accumulation of a protease-resistant form of the prion protein. We demonstrated that this experimental system is a powerful tool for investigating the efficacy of anti-prion compounds on both prion-induced neurodegeneration and prion protein misfolding, as well as in the context of human prion protein. Within a library of 320 compounds that have been approved for human use and cross the blood-brain barrier, we identified five molecules that were active against the aggregation of the E200K prion protein and the neurodegeneration it induced in transgenic animals. 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Expression of E200K prion protein induced a specific behavioural pattern and neurodegeneration of green fluorescent protein-expressing mechanosensitive neurons, in addition to the formation of intraneuronal inclusions associated with the accumulation of a protease-resistant form of the prion protein. We demonstrated that this experimental system is a powerful tool for investigating the efficacy of anti-prion compounds on both prion-induced neurodegeneration and prion protein misfolding, as well as in the context of human prion protein. Within a library of 320 compounds that have been approved for human use and cross the blood-brain barrier, we identified five molecules that were active against the aggregation of the E200K prion protein and the neurodegeneration it induced in transgenic animals. 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subjects Animals
Animals, Genetically Modified
Benzocaine - administration & dosage
Benzocaine - analogs & derivatives
Brain - drug effects
Brain - metabolism
Brain - pathology
Caenorhabditis elegans
Caenorhabditis elegans Proteins - genetics
Disease Models, Animal
Humans
Naloxone - administration & dosage
Piroxicam - administration & dosage
Piroxicam - analogs & derivatives
Prion Diseases - drug therapy
Prion Diseases - genetics
Prion Diseases - metabolism
Prion Proteins - genetics
Prion Proteins - metabolism
Protein Aggregation, Pathological - drug therapy
Protein Aggregation, Pathological - genetics
Protein Aggregation, Pathological - metabolism
Tubulin - genetics
title An in vivo Caenorhabditis elegans model for therapeutic research in human prion diseases
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