Rabbits are not resistant to prion infection
The ability of prions to infect some species and not others is determined by the transmission barrier. This unexplained phenomenon has led to the belief that certain species were not susceptible to transmissible spongiform encephalopathies (TSEs) and therefore represented negligible risk to human he...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-03, Vol.109 (13), p.5080-5085 |
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| creator | Chianini, Francesca Fernández-Borges, Natalia Vidal, Enric Gibbard, Louise Pintado, Belén de Castro, Jorge Priola, Suzette A Hamilton, Scott Eaton, Samantha L Finlayson, Jeanie Pang, Yvonne Steele, Philip Reid, Hugh W Dagleish, Mark P Castilla, Joaquín |
| description | The ability of prions to infect some species and not others is determined by the transmission barrier. This unexplained phenomenon has led to the belief that certain species were not susceptible to transmissible spongiform encephalopathies (TSEs) and therefore represented negligible risk to human health if consumed. Using the protein misfolding cyclic amplification (PMCA) technique, we were able to overcome the species barrier in rabbits, which have been classified as TSE resistant for four decades. Rabbit brain homogenate, either unseeded or seeded in vitro with disease-related prions obtained from different species, was subjected to serial rounds of PMCA. De novo rabbit prions produced in vitro from unseeded material were tested for infectivity in rabbits, with one of three intracerebrally challenged animals succumbing to disease at 766 d and displaying all of the characteristics of a TSE, thereby demonstrating that leporids are not resistant to prion infection. Material from the brain of the clinically affected rabbit containing abnormal prion protein resulted in a 100% attack rate after its inoculation in transgenic mice overexpressing rabbit PrP. Transmissibility to rabbits (>470 d) has been confirmed in 2 of 10 rabbits after intracerebral challenge. Despite rabbits no longer being able to be classified as resistant to TSEs, an outbreak of "mad rabbit disease" is unlikely. |
| doi_str_mv | 10.1073/pnas.1120076109 |
| format | Article |
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This unexplained phenomenon has led to the belief that certain species were not susceptible to transmissible spongiform encephalopathies (TSEs) and therefore represented negligible risk to human health if consumed. Using the protein misfolding cyclic amplification (PMCA) technique, we were able to overcome the species barrier in rabbits, which have been classified as TSE resistant for four decades. Rabbit brain homogenate, either unseeded or seeded in vitro with disease-related prions obtained from different species, was subjected to serial rounds of PMCA. De novo rabbit prions produced in vitro from unseeded material were tested for infectivity in rabbits, with one of three intracerebrally challenged animals succumbing to disease at 766 d and displaying all of the characteristics of a TSE, thereby demonstrating that leporids are not resistant to prion infection. Material from the brain of the clinically affected rabbit containing abnormal prion protein resulted in a 100% attack rate after its inoculation in transgenic mice overexpressing rabbit PrP. Transmissibility to rabbits (>470 d) has been confirmed in 2 of 10 rabbits after intracerebral challenge. Despite rabbits no longer being able to be classified as resistant to TSEs, an outbreak of "mad rabbit disease" is unlikely.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1120076109</identifier><identifier>PMID: 22416127</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animal migration behavior ; Animals ; Biochemistry ; Biological Sciences ; Brain ; Brain - metabolism ; Brain - pathology ; Ca super(2+)-transporting ATPase ; Disease Resistance ; Disease transmission ; Electrophoresis, Polyacrylamide Gel ; Endopeptidase K - metabolism ; gene overexpression ; human health ; Humans ; Immunohistochemistry ; Infection ; Infections ; Infectivity ; Inoculation ; Leporidae ; Male ; Mice ; Mice, Transgenic ; Monoclonal antibodies ; pathogenicity ; Prion diseases ; Prion Diseases - metabolism ; Prion Diseases - pathology ; Prion Diseases - transmission ; Prion protein ; Prions ; Prions - chemistry ; Prions - metabolism ; Prions - pathogenicity ; Protein Denaturation ; Protein Folding ; Proteins ; Rabbits ; risk ; Risk assessment ; Rodents ; Species Specificity ; Spongiform encephalopathies ; Transgenic animals ; Transgenic mice ; Transmissible spongiform encephalopathy</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-03, Vol.109 (13), p.5080-5085</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 27, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-81f06981c4952a9e2515ce61d702e3c503b58625b47595660f53ba97230ba223</citedby><cites>FETCH-LOGICAL-c522t-81f06981c4952a9e2515ce61d702e3c503b58625b47595660f53ba97230ba223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/13.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41588424$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41588424$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22416127$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chianini, Francesca</creatorcontrib><creatorcontrib>Fernández-Borges, Natalia</creatorcontrib><creatorcontrib>Vidal, Enric</creatorcontrib><creatorcontrib>Gibbard, Louise</creatorcontrib><creatorcontrib>Pintado, Belén</creatorcontrib><creatorcontrib>de Castro, Jorge</creatorcontrib><creatorcontrib>Priola, Suzette A</creatorcontrib><creatorcontrib>Hamilton, Scott</creatorcontrib><creatorcontrib>Eaton, Samantha L</creatorcontrib><creatorcontrib>Finlayson, Jeanie</creatorcontrib><creatorcontrib>Pang, Yvonne</creatorcontrib><creatorcontrib>Steele, Philip</creatorcontrib><creatorcontrib>Reid, Hugh W</creatorcontrib><creatorcontrib>Dagleish, Mark P</creatorcontrib><creatorcontrib>Castilla, Joaquín</creatorcontrib><title>Rabbits are not resistant to prion infection</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The ability of prions to infect some species and not others is determined by the transmission barrier. This unexplained phenomenon has led to the belief that certain species were not susceptible to transmissible spongiform encephalopathies (TSEs) and therefore represented negligible risk to human health if consumed. Using the protein misfolding cyclic amplification (PMCA) technique, we were able to overcome the species barrier in rabbits, which have been classified as TSE resistant for four decades. Rabbit brain homogenate, either unseeded or seeded in vitro with disease-related prions obtained from different species, was subjected to serial rounds of PMCA. De novo rabbit prions produced in vitro from unseeded material were tested for infectivity in rabbits, with one of three intracerebrally challenged animals succumbing to disease at 766 d and displaying all of the characteristics of a TSE, thereby demonstrating that leporids are not resistant to prion infection. Material from the brain of the clinically affected rabbit containing abnormal prion protein resulted in a 100% attack rate after its inoculation in transgenic mice overexpressing rabbit PrP. Transmissibility to rabbits (>470 d) has been confirmed in 2 of 10 rabbits after intracerebral challenge. Despite rabbits no longer being able to be classified as resistant to TSEs, an outbreak of "mad rabbit disease" is unlikely.</description><subject>Animal migration behavior</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Brain</subject><subject>Brain - metabolism</subject><subject>Brain - pathology</subject><subject>Ca super(2+)-transporting ATPase</subject><subject>Disease Resistance</subject><subject>Disease transmission</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endopeptidase K - metabolism</subject><subject>gene overexpression</subject><subject>human health</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Infection</subject><subject>Infections</subject><subject>Infectivity</subject><subject>Inoculation</subject><subject>Leporidae</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Monoclonal antibodies</subject><subject>pathogenicity</subject><subject>Prion diseases</subject><subject>Prion Diseases - metabolism</subject><subject>Prion Diseases - pathology</subject><subject>Prion Diseases - transmission</subject><subject>Prion protein</subject><subject>Prions</subject><subject>Prions - chemistry</subject><subject>Prions - metabolism</subject><subject>Prions - pathogenicity</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>risk</subject><subject>Risk assessment</subject><subject>Rodents</subject><subject>Species Specificity</subject><subject>Spongiform encephalopathies</subject><subject>Transgenic animals</subject><subject>Transgenic mice</subject><subject>Transmissible spongiform encephalopathy</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kk2LFDEQhoMo7uzq2ZPaeNGDvVtV-ejkIsiyfsCCoOs5pHvTaw8zyZhkBP-9aWacUQ9ekkCeeqjKG8aeIJwjdPxiE1w-RySATiGYe2xRV2yVMHCfLQCoa7UgccJOc14CgJEaHrITIoEKqVuw159d308lNy75JsTSJJ-nXFwoTYnNJk0xNFMY_VDq6RF7MLpV9o_3-xm7eXd1c_mhvf70_uPl2-t2kESl1TiCMhoHYSQ540miHLzC2w7I80EC76VWJHvRSSOVglHy3pmOOPSOiJ-xNzvtZtuv_e3gQ0luZWsza5d-2ugm-_dNmL7Zu_jDck7c6Fnwci9I8fvW52LXUx78auWCj9tsjTRI2iio5Kv_kggoEARwrOiLf9Bl3KZQ36H6hOLGdLpCFztoSDHn5MdD1wh2TszOidljYrXi2Z_DHvjfEVXg-R6YK486Y5FbCXoe4umOWOYS0wERKPUc_tEwumjdXZqy_fqF6mT1Q6gaQMd_AbTUrAM</recordid><startdate>20120327</startdate><enddate>20120327</enddate><creator>Chianini, Francesca</creator><creator>Fernández-Borges, Natalia</creator><creator>Vidal, Enric</creator><creator>Gibbard, Louise</creator><creator>Pintado, Belén</creator><creator>de Castro, Jorge</creator><creator>Priola, Suzette A</creator><creator>Hamilton, Scott</creator><creator>Eaton, Samantha L</creator><creator>Finlayson, Jeanie</creator><creator>Pang, Yvonne</creator><creator>Steele, Philip</creator><creator>Reid, Hugh W</creator><creator>Dagleish, Mark P</creator><creator>Castilla, Joaquín</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120327</creationdate><title>Rabbits are not resistant to prion infection</title><author>Chianini, Francesca ; Fernández-Borges, Natalia ; Vidal, Enric ; Gibbard, Louise ; Pintado, Belén ; de Castro, Jorge ; Priola, Suzette A ; Hamilton, Scott ; Eaton, Samantha L ; Finlayson, Jeanie ; Pang, Yvonne ; Steele, Philip ; Reid, Hugh W ; Dagleish, Mark P ; Castilla, Joaquín</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-81f06981c4952a9e2515ce61d702e3c503b58625b47595660f53ba97230ba223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animal migration behavior</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Brain</topic><topic>Brain - metabolism</topic><topic>Brain - pathology</topic><topic>Ca super(2+)-transporting ATPase</topic><topic>Disease Resistance</topic><topic>Disease transmission</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endopeptidase K - metabolism</topic><topic>gene overexpression</topic><topic>human health</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Infection</topic><topic>Infections</topic><topic>Infectivity</topic><topic>Inoculation</topic><topic>Leporidae</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Monoclonal antibodies</topic><topic>pathogenicity</topic><topic>Prion diseases</topic><topic>Prion Diseases - metabolism</topic><topic>Prion Diseases - pathology</topic><topic>Prion Diseases - transmission</topic><topic>Prion protein</topic><topic>Prions</topic><topic>Prions - chemistry</topic><topic>Prions - metabolism</topic><topic>Prions - pathogenicity</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>risk</topic><topic>Risk assessment</topic><topic>Rodents</topic><topic>Species Specificity</topic><topic>Spongiform encephalopathies</topic><topic>Transgenic animals</topic><topic>Transgenic mice</topic><topic>Transmissible spongiform encephalopathy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chianini, Francesca</creatorcontrib><creatorcontrib>Fernández-Borges, Natalia</creatorcontrib><creatorcontrib>Vidal, Enric</creatorcontrib><creatorcontrib>Gibbard, Louise</creatorcontrib><creatorcontrib>Pintado, Belén</creatorcontrib><creatorcontrib>de Castro, Jorge</creatorcontrib><creatorcontrib>Priola, Suzette A</creatorcontrib><creatorcontrib>Hamilton, Scott</creatorcontrib><creatorcontrib>Eaton, Samantha L</creatorcontrib><creatorcontrib>Finlayson, Jeanie</creatorcontrib><creatorcontrib>Pang, Yvonne</creatorcontrib><creatorcontrib>Steele, Philip</creatorcontrib><creatorcontrib>Reid, Hugh W</creatorcontrib><creatorcontrib>Dagleish, Mark P</creatorcontrib><creatorcontrib>Castilla, Joaquín</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chianini, Francesca</au><au>Fernández-Borges, Natalia</au><au>Vidal, Enric</au><au>Gibbard, Louise</au><au>Pintado, Belén</au><au>de Castro, Jorge</au><au>Priola, Suzette A</au><au>Hamilton, Scott</au><au>Eaton, Samantha L</au><au>Finlayson, Jeanie</au><au>Pang, Yvonne</au><au>Steele, Philip</au><au>Reid, Hugh W</au><au>Dagleish, Mark P</au><au>Castilla, Joaquín</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rabbits are not resistant to prion infection</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-03-27</date><risdate>2012</risdate><volume>109</volume><issue>13</issue><spage>5080</spage><epage>5085</epage><pages>5080-5085</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The ability of prions to infect some species and not others is determined by the transmission barrier. This unexplained phenomenon has led to the belief that certain species were not susceptible to transmissible spongiform encephalopathies (TSEs) and therefore represented negligible risk to human health if consumed. Using the protein misfolding cyclic amplification (PMCA) technique, we were able to overcome the species barrier in rabbits, which have been classified as TSE resistant for four decades. Rabbit brain homogenate, either unseeded or seeded in vitro with disease-related prions obtained from different species, was subjected to serial rounds of PMCA. De novo rabbit prions produced in vitro from unseeded material were tested for infectivity in rabbits, with one of three intracerebrally challenged animals succumbing to disease at 766 d and displaying all of the characteristics of a TSE, thereby demonstrating that leporids are not resistant to prion infection. Material from the brain of the clinically affected rabbit containing abnormal prion protein resulted in a 100% attack rate after its inoculation in transgenic mice overexpressing rabbit PrP. Transmissibility to rabbits (>470 d) has been confirmed in 2 of 10 rabbits after intracerebral challenge. Despite rabbits no longer being able to be classified as resistant to TSEs, an outbreak of "mad rabbit disease" is unlikely.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22416127</pmid><doi>10.1073/pnas.1120076109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| recordid | cdi_pubmed_primary_22416127 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animal migration behavior Animals Biochemistry Biological Sciences Brain Brain - metabolism Brain - pathology Ca super(2+)-transporting ATPase Disease Resistance Disease transmission Electrophoresis, Polyacrylamide Gel Endopeptidase K - metabolism gene overexpression human health Humans Immunohistochemistry Infection Infections Infectivity Inoculation Leporidae Male Mice Mice, Transgenic Monoclonal antibodies pathogenicity Prion diseases Prion Diseases - metabolism Prion Diseases - pathology Prion Diseases - transmission Prion protein Prions Prions - chemistry Prions - metabolism Prions - pathogenicity Protein Denaturation Protein Folding Proteins Rabbits risk Risk assessment Rodents Species Specificity Spongiform encephalopathies Transgenic animals Transgenic mice Transmissible spongiform encephalopathy |
| title | Rabbits are not resistant to prion infection |
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