Human Prion Protein with Valine 129 Prevents Expression of Variant CJD Phenotype
Variant Creutzfeldt-Jakob disease (vCJD) is a unique and highly distinctive clinicopathological and molecular phenotype of human prion disease associated with infection with bovine spongiform encephalopathy (BSE)-like prions. Here, we found that generation of this phenotype in transgenic mice requir...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2004-12, Vol.306 (5702), p.1793-1796 |
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| creator | Jonathan D. F. Wadsworth Asante, Emmanuel A. Desbruslais, Melanie Linehan, Jacqueline M. Joiner, Susan Gowland, Ian Welch, Julie Stone, Lisa Lloyd, Sarah E. Hill, Andrew F. Brandner, Sebastian Collinge, John |
| description | Variant Creutzfeldt-Jakob disease (vCJD) is a unique and highly distinctive clinicopathological and molecular phenotype of human prion disease associated with infection with bovine spongiform encephalopathy (BSE)-like prions. Here, we found that generation of this phenotype in transgenic mice required expression of human prion protein (PrP) with methionine 129. Expression of human PrP with valine 129 resulted in a distinct phenotype and, remarkably, persistence of a barrier to transmission of BSE-derived prions on subpassage. Polymorphic residue 129 of human PrP dictated propagation of distinct prion strains after BSE prion infection. Thus, primary and secondary human infection with BSE-derived prions may result in sporadic CJD-like or novel phenotypes in addition to vCJD, depending on the genotype of the prion source and the recipient. |
| doi_str_mv | 10.1126/science.1103932 |
| format | Article |
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F. Wadsworth ; Asante, Emmanuel A. ; Desbruslais, Melanie ; Linehan, Jacqueline M. ; Joiner, Susan ; Gowland, Ian ; Welch, Julie ; Stone, Lisa ; Lloyd, Sarah E. ; Hill, Andrew F. ; Brandner, Sebastian ; Collinge, John</creator><creatorcontrib>Jonathan D. F. Wadsworth ; Asante, Emmanuel A. ; Desbruslais, Melanie ; Linehan, Jacqueline M. ; Joiner, Susan ; Gowland, Ian ; Welch, Julie ; Stone, Lisa ; Lloyd, Sarah E. ; Hill, Andrew F. ; Brandner, Sebastian ; Collinge, John</creatorcontrib><description>Variant Creutzfeldt-Jakob disease (vCJD) is a unique and highly distinctive clinicopathological and molecular phenotype of human prion disease associated with infection with bovine spongiform encephalopathy (BSE)-like prions. Here, we found that generation of this phenotype in transgenic mice required expression of human prion protein (PrP) with methionine 129. Expression of human PrP with valine 129 resulted in a distinct phenotype and, remarkably, persistence of a barrier to transmission of BSE-derived prions on subpassage. Polymorphic residue 129 of human PrP dictated propagation of distinct prion strains after BSE prion infection. Thus, primary and secondary human infection with BSE-derived prions may result in sporadic CJD-like or novel phenotypes in addition to vCJD, depending on the genotype of the prion source and the recipient.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1103932</identifier><identifier>PMID: 15539564</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Amyloid - genetics ; Animals ; Biological and medical sciences ; Bovine spongiform encephalopathy ; Brain ; Brain - pathology ; Cattle ; Codon ; Codons ; Creutzfeldt-Jakob disease ; Creutzfeldt-Jakob Syndrome - genetics ; Creutzfeldt-Jakob Syndrome - metabolism ; Creutzfeldt-Jakob Syndrome - pathology ; Creutzfeldt-Jakob Syndrome - transmission ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Disease models ; Encephalopathy, Bovine Spongiform - pathology ; Encephalopathy, Bovine Spongiform - transmission ; Genetic aspects ; Genotype & phenotype ; Humans ; Infections ; Medical sciences ; Methionine ; Mice ; Mice, Transgenic ; Neurology ; Pathology ; Persistence ; Phenotype ; Phenotypes ; Polymorphism, Genetic ; Prevention ; Prion diseases ; Prion Proteins ; Prions ; Prions (Proteins) ; Protein Conformation ; Protein Precursors - genetics ; PrPC Proteins - chemistry ; PrPC Proteins - genetics ; PrPC Proteins - metabolism ; PrPSc Proteins - metabolism ; PrPSc Proteins - pathogenicity ; Rodents ; Transgenic animals ; Valine</subject><ispartof>Science (American Association for the Advancement of Science), 2004-12, Vol.306 (5702), p.1793-1796</ispartof><rights>Copyright 2004 American Association for the Advancement of Science</rights><rights>2005 INIST-CNRS</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Dec 3, 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c759t-df9ab4a338c8caa000c3107de15665642558543c880aea5558952654e22228523</citedby><cites>FETCH-LOGICAL-c759t-df9ab4a338c8caa000c3107de15665642558543c880aea5558952654e22228523</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3839785$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3839785$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16341351$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15539564$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jonathan D. F. Wadsworth</creatorcontrib><creatorcontrib>Asante, Emmanuel A.</creatorcontrib><creatorcontrib>Desbruslais, Melanie</creatorcontrib><creatorcontrib>Linehan, Jacqueline M.</creatorcontrib><creatorcontrib>Joiner, Susan</creatorcontrib><creatorcontrib>Gowland, Ian</creatorcontrib><creatorcontrib>Welch, Julie</creatorcontrib><creatorcontrib>Stone, Lisa</creatorcontrib><creatorcontrib>Lloyd, Sarah E.</creatorcontrib><creatorcontrib>Hill, Andrew F.</creatorcontrib><creatorcontrib>Brandner, Sebastian</creatorcontrib><creatorcontrib>Collinge, John</creatorcontrib><title>Human Prion Protein with Valine 129 Prevents Expression of Variant CJD Phenotype</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Variant Creutzfeldt-Jakob disease (vCJD) is a unique and highly distinctive clinicopathological and molecular phenotype of human prion disease associated with infection with bovine spongiform encephalopathy (BSE)-like prions. Here, we found that generation of this phenotype in transgenic mice required expression of human prion protein (PrP) with methionine 129. Expression of human PrP with valine 129 resulted in a distinct phenotype and, remarkably, persistence of a barrier to transmission of BSE-derived prions on subpassage. Polymorphic residue 129 of human PrP dictated propagation of distinct prion strains after BSE prion infection. Thus, primary and secondary human infection with BSE-derived prions may result in sporadic CJD-like or novel phenotypes in addition to vCJD, depending on the genotype of the prion source and the recipient.</description><subject>Amyloid - genetics</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bovine spongiform encephalopathy</subject><subject>Brain</subject><subject>Brain - pathology</subject><subject>Cattle</subject><subject>Codon</subject><subject>Codons</subject><subject>Creutzfeldt-Jakob disease</subject><subject>Creutzfeldt-Jakob Syndrome - genetics</subject><subject>Creutzfeldt-Jakob Syndrome - metabolism</subject><subject>Creutzfeldt-Jakob Syndrome - pathology</subject><subject>Creutzfeldt-Jakob Syndrome - transmission</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. 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Wadsworth</au><au>Asante, Emmanuel A.</au><au>Desbruslais, Melanie</au><au>Linehan, Jacqueline M.</au><au>Joiner, Susan</au><au>Gowland, Ian</au><au>Welch, Julie</au><au>Stone, Lisa</au><au>Lloyd, Sarah E.</au><au>Hill, Andrew F.</au><au>Brandner, Sebastian</au><au>Collinge, John</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Prion Protein with Valine 129 Prevents Expression of Variant CJD Phenotype</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2004-12-03</date><risdate>2004</risdate><volume>306</volume><issue>5702</issue><spage>1793</spage><epage>1796</epage><pages>1793-1796</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Variant Creutzfeldt-Jakob disease (vCJD) is a unique and highly distinctive clinicopathological and molecular phenotype of human prion disease associated with infection with bovine spongiform encephalopathy (BSE)-like prions. Here, we found that generation of this phenotype in transgenic mice required expression of human prion protein (PrP) with methionine 129. Expression of human PrP with valine 129 resulted in a distinct phenotype and, remarkably, persistence of a barrier to transmission of BSE-derived prions on subpassage. Polymorphic residue 129 of human PrP dictated propagation of distinct prion strains after BSE prion infection. Thus, primary and secondary human infection with BSE-derived prions may result in sporadic CJD-like or novel phenotypes in addition to vCJD, depending on the genotype of the prion source and the recipient.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>15539564</pmid><doi>10.1126/science.1103932</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2004-12, Vol.306 (5702), p.1793-1796 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743082786 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Amyloid - genetics Animals Biological and medical sciences Bovine spongiform encephalopathy Brain Brain - pathology Cattle Codon Codons Creutzfeldt-Jakob disease Creutzfeldt-Jakob Syndrome - genetics Creutzfeldt-Jakob Syndrome - metabolism Creutzfeldt-Jakob Syndrome - pathology Creutzfeldt-Jakob Syndrome - transmission Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Disease models Encephalopathy, Bovine Spongiform - pathology Encephalopathy, Bovine Spongiform - transmission Genetic aspects Genotype & phenotype Humans Infections Medical sciences Methionine Mice Mice, Transgenic Neurology Pathology Persistence Phenotype Phenotypes Polymorphism, Genetic Prevention Prion diseases Prion Proteins Prions Prions (Proteins) Protein Conformation Protein Precursors - genetics PrPC Proteins - chemistry PrPC Proteins - genetics PrPC Proteins - metabolism PrPSc Proteins - metabolism PrPSc Proteins - pathogenicity Rodents Transgenic animals Valine |
| title | Human Prion Protein with Valine 129 Prevents Expression of Variant CJD Phenotype |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-31T20%3A30%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Human%20Prion%20Protein%20with%20Valine%20129%20Prevents%20Expression%20of%20Variant%20CJD%20Phenotype&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Jonathan%20D.%20F.%20Wadsworth&rft.date=2004-12-03&rft.volume=306&rft.issue=5702&rft.spage=1793&rft.epage=1796&rft.pages=1793-1796&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.1103932&rft_dat=%3Cgale_proqu%3EA126195036%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213600535&rft_id=info:pmid/15539564&rft_galeid=A126195036&rft_jstor_id=3839785&rfr_iscdi=true |