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 |
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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. 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.</description><identifier>ISSN: 0006-8950</identifier><identifier>EISSN: 1460-2156</identifier><identifier>DOI: 10.1093/brain/awab152</identifier><identifier>PMID: 34687213</identifier><language>eng</language><publisher>England</publisher><subject>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</subject><ispartof>Brain (London, England : 1878), 2021-10, Vol.144 (9), p.2745-2758</ispartof><rights>The Author(s) (2021). Published by Oxford University Press on behalf of the Guarantors of Brain. All rights reserved. For permissions, please email: journals.permissions@oup.com.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c332t-75f23634759c05311cd7bc09d362d65eb05f8d61e1fdbd953a2c76d172eb07a13</citedby><cites>FETCH-LOGICAL-c332t-75f23634759c05311cd7bc09d362d65eb05f8d61e1fdbd953a2c76d172eb07a13</cites><orcidid>0000-0001-9643-4417</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34687213$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bizat, Nicolas</creatorcontrib><creatorcontrib>Parrales, Valeria</creatorcontrib><creatorcontrib>Laoues, Sofian</creatorcontrib><creatorcontrib>Normant, Sébastien</creatorcontrib><creatorcontrib>Levavasseur, Etienne</creatorcontrib><creatorcontrib>Roussel, Julian</creatorcontrib><creatorcontrib>Privat, Nicolas</creatorcontrib><creatorcontrib>Gougerot, Alexianne</creatorcontrib><creatorcontrib>Ravassard, Philippe</creatorcontrib><creatorcontrib>Beaudry, Patrice</creatorcontrib><creatorcontrib>Brandel, Jean-Philippe</creatorcontrib><creatorcontrib>Laplanche, Jean-Louis</creatorcontrib><creatorcontrib>Haïk, Stéphane</creatorcontrib><title>An in vivo Caenorhabditis elegans model for therapeutic research in human prion diseases</title><title>Brain (London, England : 1878)</title><addtitle>Brain</addtitle><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.</description><subject>Animals</subject><subject>Animals, Genetically Modified</subject><subject>Benzocaine - administration & dosage</subject><subject>Benzocaine - analogs & derivatives</subject><subject>Brain - drug effects</subject><subject>Brain - metabolism</subject><subject>Brain - pathology</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Disease Models, Animal</subject><subject>Humans</subject><subject>Naloxone - administration & dosage</subject><subject>Piroxicam - administration & dosage</subject><subject>Piroxicam - analogs & derivatives</subject><subject>Prion Diseases - drug therapy</subject><subject>Prion Diseases - genetics</subject><subject>Prion Diseases - metabolism</subject><subject>Prion Proteins - genetics</subject><subject>Prion Proteins - metabolism</subject><subject>Protein Aggregation, Pathological - drug therapy</subject><subject>Protein Aggregation, Pathological - genetics</subject><subject>Protein Aggregation, Pathological - metabolism</subject><subject>Tubulin - genetics</subject><issn>0006-8950</issn><issn>1460-2156</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kD1PwzAQhi0EoqUwsiKPLKH-iO1krCq-JCQWkNgix74Qo8QudlLEvyelhemku-d9dXoQuqTkhpKSL-uonV_qL11TwY7QnOaSZIwKeYzmhBCZFaUgM3SW0gchNOdMnqIZz2WhGOVz9Lby2Hm8dduA1xp8iK2urRtcwtDBu_YJ98FCh5sQ8dBC1BsYB2dwhAQ6mnaXbsdee7yJLnhs3bRPkM7RSaO7BBeHuUCvd7cv64fs6fn-cb16ygznbMiUaBiXPFeiNERwSo1VtSGl5ZJZKaAmoimspEAbW9tScM2MkpYqNp2UpnyBrve9mxg-R0hD1btkoOu0hzCmiokiV6WSrJzQbI-aGFKK0FTTy72O3xUl1U5m9SuzOsic-KtD9Vj3YP_pP3v8B7W0ckk</recordid><startdate>20211022</startdate><enddate>20211022</enddate><creator>Bizat, Nicolas</creator><creator>Parrales, Valeria</creator><creator>Laoues, Sofian</creator><creator>Normant, Sébastien</creator><creator>Levavasseur, Etienne</creator><creator>Roussel, Julian</creator><creator>Privat, Nicolas</creator><creator>Gougerot, Alexianne</creator><creator>Ravassard, Philippe</creator><creator>Beaudry, Patrice</creator><creator>Brandel, Jean-Philippe</creator><creator>Laplanche, Jean-Louis</creator><creator>Haïk, Stéphane</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-9643-4417</orcidid></search><sort><creationdate>20211022</creationdate><title>An in vivo Caenorhabditis elegans model for therapeutic research in human prion diseases</title><author>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</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c332t-75f23634759c05311cd7bc09d362d65eb05f8d61e1fdbd953a2c76d172eb07a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Animals</topic><topic>Animals, Genetically Modified</topic><topic>Benzocaine - administration & dosage</topic><topic>Benzocaine - analogs & derivatives</topic><topic>Brain - drug effects</topic><topic>Brain - metabolism</topic><topic>Brain - pathology</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Disease Models, Animal</topic><topic>Humans</topic><topic>Naloxone - administration & dosage</topic><topic>Piroxicam - administration & dosage</topic><topic>Piroxicam - analogs & derivatives</topic><topic>Prion Diseases - drug therapy</topic><topic>Prion Diseases - genetics</topic><topic>Prion Diseases - metabolism</topic><topic>Prion Proteins - genetics</topic><topic>Prion Proteins - metabolism</topic><topic>Protein Aggregation, Pathological - drug therapy</topic><topic>Protein Aggregation, Pathological - genetics</topic><topic>Protein Aggregation, Pathological - metabolism</topic><topic>Tubulin - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bizat, Nicolas</creatorcontrib><creatorcontrib>Parrales, Valeria</creatorcontrib><creatorcontrib>Laoues, Sofian</creatorcontrib><creatorcontrib>Normant, Sébastien</creatorcontrib><creatorcontrib>Levavasseur, Etienne</creatorcontrib><creatorcontrib>Roussel, Julian</creatorcontrib><creatorcontrib>Privat, Nicolas</creatorcontrib><creatorcontrib>Gougerot, Alexianne</creatorcontrib><creatorcontrib>Ravassard, Philippe</creatorcontrib><creatorcontrib>Beaudry, Patrice</creatorcontrib><creatorcontrib>Brandel, Jean-Philippe</creatorcontrib><creatorcontrib>Laplanche, Jean-Louis</creatorcontrib><creatorcontrib>Haïk, Stéphane</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Brain (London, England : 1878)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bizat, Nicolas</au><au>Parrales, Valeria</au><au>Laoues, Sofian</au><au>Normant, Sébastien</au><au>Levavasseur, Etienne</au><au>Roussel, Julian</au><au>Privat, Nicolas</au><au>Gougerot, Alexianne</au><au>Ravassard, Philippe</au><au>Beaudry, Patrice</au><au>Brandel, Jean-Philippe</au><au>Laplanche, Jean-Louis</au><au>Haïk, Stéphane</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An in vivo Caenorhabditis elegans model for therapeutic research in human prion diseases</atitle><jtitle>Brain (London, England : 1878)</jtitle><addtitle>Brain</addtitle><date>2021-10-22</date><risdate>2021</risdate><volume>144</volume><issue>9</issue><spage>2745</spage><epage>2758</epage><pages>2745-2758</pages><issn>0006-8950</issn><eissn>1460-2156</eissn><abstract>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.</abstract><cop>England</cop><pmid>34687213</pmid><doi>10.1093/brain/awab152</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-9643-4417</orcidid><oa>free_for_read</oa></addata></record> |
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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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