Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties
The agents responsible for transmissible spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrP Sc , an abnormal conformer of the host glycoprotein PrP C . TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contai...
Gespeichert in:
Veröffentlicht in: | The EMBO journal 2013-03, Vol.32 (5), p.756-769 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext bestellen |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 769 |
---|---|
container_issue | 5 |
container_start_page | 756 |
container_title | The EMBO journal |
container_volume | 32 |
creator | Cancellotti, Enrico Mahal, Sukhvir P Somerville, Robert Diack, Abigail Brown, Deborah Piccardo, Pedro Weissmann, Charles Manson, Jean C |
description | The agents responsible for transmissible spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrP
Sc
, an abnormal conformer of the host glycoprotein PrP
C
. TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contain PrP
Sc
with the same amino‐acid sequence. If PrP alone carries information defining strain properties, these must be encoded by post‐translational events. Here we investigated whether the glycosylation status of host PrP affects TSE strain characteristics. We inoculated wild‐type mice with three TSE strains passaged through transgenic mice with PrP devoid of glycans at the first, second or both N‐glycosylation sites. We compared the infectious properties of the emerging isolates with TSE strains passaged in wild‐type mice by
in vivo
strain typing and by the standard scrapie cell assay
in vitro
. Strain‐specific characteristics of the 79A TSE strain changed when PrP
Sc
was devoid of one or both glycans. Thus infectious properties of a TSE strain can be altered by post‐translational changes to PrP which we propose result in the selection of mutant TSE strains.
N‐linked glycosylation of the endogenous and wild‐type prion protein, PrP, alters the infectious properties of prion strains in mice. |
doi_str_mv | 10.1038/emboj.2013.6 |
format | Article |
fullrecord | <record><control><sourceid>proquest_C6C</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3590993</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1315135334</sourcerecordid><originalsourceid>FETCH-LOGICAL-c6316-67cdef5193d680ff2a6abec1e41c1ed4fa2b425e6569d819d42e1616b730b6d3</originalsourceid><addsrcrecordid>eNqFksFv0zAUxi0EYmVw44wicdmBdHZe7CQXJDaNwjZGD5OQuFhO8tK6OHGw043-9zhtqQZCcLEt-efvfe99JuQlo1NGIT_FtrSraUIZTMUjMmGpoHFCM_6YTGgiWJyyvDgiz7xfUUp5nrGn5CgBKHhB-YSoufVDPDjVeaMGbTtlomqpugX6aLDR3M0jZQZ00RZptfe6NBj53nYL3VjXRthV2C-Vsb0alpvIB1B3Ue9sj27Q6J-TJ40yHl_s92Ny-_7i9vxDfP159vH83XVcCWAiFllVY8NZAbXIadMkSqgSK4YpC0udNiop04Sj4KKoc1bUaYJMMFFmQEtRwzF5u5Pt12WLdYVdMGJk73Sr3EZapeXvN51eyoW9kxAGURQQBE72As5-X6MfZOi2QmNUh3btJUuDtwwyLv6PAuMMOEAa0Nd_oCu7dmHKWyrNMsiTIlBvdlTlrPcOm4NvRuWYstymLMeU5Vj_1cNeD_CvWAMAO-BeG9z8U0xefDq7HI-jbLx75cOD8APcA69_t7HntR_wx6GKct-kGAclv9zMJL36msHNLJeX8BPtvdSF</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1314773829</pqid></control><display><type>article</type><title>Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties</title><source>Springer Nature OA Free Journals</source><creator>Cancellotti, Enrico ; Mahal, Sukhvir P ; Somerville, Robert ; Diack, Abigail ; Brown, Deborah ; Piccardo, Pedro ; Weissmann, Charles ; Manson, Jean C</creator><creatorcontrib>Cancellotti, Enrico ; Mahal, Sukhvir P ; Somerville, Robert ; Diack, Abigail ; Brown, Deborah ; Piccardo, Pedro ; Weissmann, Charles ; Manson, Jean C</creatorcontrib><description>The agents responsible for transmissible spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrP
Sc
, an abnormal conformer of the host glycoprotein PrP
C
. TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contain PrP
Sc
with the same amino‐acid sequence. If PrP alone carries information defining strain properties, these must be encoded by post‐translational events. Here we investigated whether the glycosylation status of host PrP affects TSE strain characteristics. We inoculated wild‐type mice with three TSE strains passaged through transgenic mice with PrP devoid of glycans at the first, second or both N‐glycosylation sites. We compared the infectious properties of the emerging isolates with TSE strains passaged in wild‐type mice by
in vivo
strain typing and by the standard scrapie cell assay
in vitro
. Strain‐specific characteristics of the 79A TSE strain changed when PrP
Sc
was devoid of one or both glycans. Thus infectious properties of a TSE strain can be altered by post‐translational changes to PrP which we propose result in the selection of mutant TSE strains.
N‐linked glycosylation of the endogenous and wild‐type prion protein, PrP, alters the infectious properties of prion strains in mice.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/emboj.2013.6</identifier><identifier>PMID: 23395905</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; Blotting, Western ; Brain - virology ; Cells, Cultured ; EMBO27 ; EMBO31 ; Female ; Glycoproteins ; Glycosylation ; Immunoenzyme Techniques ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Molecular biology ; Neuroblastoma - metabolism ; Neuroblastoma - pathology ; Neuroblastoma - virology ; phenotypic change ; Polysaccharides - metabolism ; prion ; Prion Diseases - metabolism ; Prion Diseases - transmission ; Prion Diseases - virology ; Protein Processing, Post-Translational ; PrPSc Proteins - genetics ; PrPSc Proteins - metabolism ; PrPSc Proteins - pathogenicity ; Spongiform encephalopathies ; transmissible spongiform encephalopathy ; Virus Replication</subject><ispartof>The EMBO journal, 2013-03, Vol.32 (5), p.756-769</ispartof><rights>European Molecular Biology Organization 2013</rights><rights>Copyright © 2013 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Mar 6, 2013</rights><rights>Copyright © 2013, European Molecular Biology Organization 2013 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6316-67cdef5193d680ff2a6abec1e41c1ed4fa2b425e6569d819d42e1616b730b6d3</citedby><cites>FETCH-LOGICAL-c6316-67cdef5193d680ff2a6abec1e41c1ed4fa2b425e6569d819d42e1616b730b6d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3590993/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3590993/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/emboj.2013.6$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23395905$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cancellotti, Enrico</creatorcontrib><creatorcontrib>Mahal, Sukhvir P</creatorcontrib><creatorcontrib>Somerville, Robert</creatorcontrib><creatorcontrib>Diack, Abigail</creatorcontrib><creatorcontrib>Brown, Deborah</creatorcontrib><creatorcontrib>Piccardo, Pedro</creatorcontrib><creatorcontrib>Weissmann, Charles</creatorcontrib><creatorcontrib>Manson, Jean C</creatorcontrib><title>Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The agents responsible for transmissible spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrP
Sc
, an abnormal conformer of the host glycoprotein PrP
C
. TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contain PrP
Sc
with the same amino‐acid sequence. If PrP alone carries information defining strain properties, these must be encoded by post‐translational events. Here we investigated whether the glycosylation status of host PrP affects TSE strain characteristics. We inoculated wild‐type mice with three TSE strains passaged through transgenic mice with PrP devoid of glycans at the first, second or both N‐glycosylation sites. We compared the infectious properties of the emerging isolates with TSE strains passaged in wild‐type mice by
in vivo
strain typing and by the standard scrapie cell assay
in vitro
. Strain‐specific characteristics of the 79A TSE strain changed when PrP
Sc
was devoid of one or both glycans. Thus infectious properties of a TSE strain can be altered by post‐translational changes to PrP which we propose result in the selection of mutant TSE strains.
N‐linked glycosylation of the endogenous and wild‐type prion protein, PrP, alters the infectious properties of prion strains in mice.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>Brain - virology</subject><subject>Cells, Cultured</subject><subject>EMBO27</subject><subject>EMBO31</subject><subject>Female</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Immunoenzyme Techniques</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Transgenic</subject><subject>Molecular biology</subject><subject>Neuroblastoma - metabolism</subject><subject>Neuroblastoma - pathology</subject><subject>Neuroblastoma - virology</subject><subject>phenotypic change</subject><subject>Polysaccharides - metabolism</subject><subject>prion</subject><subject>Prion Diseases - metabolism</subject><subject>Prion Diseases - transmission</subject><subject>Prion Diseases - virology</subject><subject>Protein Processing, Post-Translational</subject><subject>PrPSc Proteins - genetics</subject><subject>PrPSc Proteins - metabolism</subject><subject>PrPSc Proteins - pathogenicity</subject><subject>Spongiform encephalopathies</subject><subject>transmissible spongiform encephalopathy</subject><subject>Virus Replication</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFksFv0zAUxi0EYmVw44wicdmBdHZe7CQXJDaNwjZGD5OQuFhO8tK6OHGw043-9zhtqQZCcLEt-efvfe99JuQlo1NGIT_FtrSraUIZTMUjMmGpoHFCM_6YTGgiWJyyvDgiz7xfUUp5nrGn5CgBKHhB-YSoufVDPDjVeaMGbTtlomqpugX6aLDR3M0jZQZ00RZptfe6NBj53nYL3VjXRthV2C-Vsb0alpvIB1B3Ue9sj27Q6J-TJ40yHl_s92Ny-_7i9vxDfP159vH83XVcCWAiFllVY8NZAbXIadMkSqgSK4YpC0udNiop04Sj4KKoc1bUaYJMMFFmQEtRwzF5u5Pt12WLdYVdMGJk73Sr3EZapeXvN51eyoW9kxAGURQQBE72As5-X6MfZOi2QmNUh3btJUuDtwwyLv6PAuMMOEAa0Nd_oCu7dmHKWyrNMsiTIlBvdlTlrPcOm4NvRuWYstymLMeU5Vj_1cNeD_CvWAMAO-BeG9z8U0xefDq7HI-jbLx75cOD8APcA69_t7HntR_wx6GKct-kGAclv9zMJL36msHNLJeX8BPtvdSF</recordid><startdate>20130306</startdate><enddate>20130306</enddate><creator>Cancellotti, Enrico</creator><creator>Mahal, Sukhvir P</creator><creator>Somerville, Robert</creator><creator>Diack, Abigail</creator><creator>Brown, Deborah</creator><creator>Piccardo, Pedro</creator><creator>Weissmann, Charles</creator><creator>Manson, Jean C</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130306</creationdate><title>Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties</title><author>Cancellotti, Enrico ; Mahal, Sukhvir P ; Somerville, Robert ; Diack, Abigail ; Brown, Deborah ; Piccardo, Pedro ; Weissmann, Charles ; Manson, Jean C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6316-67cdef5193d680ff2a6abec1e41c1ed4fa2b425e6569d819d42e1616b730b6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Brain - virology</topic><topic>Cells, Cultured</topic><topic>EMBO27</topic><topic>EMBO31</topic><topic>Female</topic><topic>Glycoproteins</topic><topic>Glycosylation</topic><topic>Immunoenzyme Techniques</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Transgenic</topic><topic>Molecular biology</topic><topic>Neuroblastoma - metabolism</topic><topic>Neuroblastoma - pathology</topic><topic>Neuroblastoma - virology</topic><topic>phenotypic change</topic><topic>Polysaccharides - metabolism</topic><topic>prion</topic><topic>Prion Diseases - metabolism</topic><topic>Prion Diseases - transmission</topic><topic>Prion Diseases - virology</topic><topic>Protein Processing, Post-Translational</topic><topic>PrPSc Proteins - genetics</topic><topic>PrPSc Proteins - metabolism</topic><topic>PrPSc Proteins - pathogenicity</topic><topic>Spongiform encephalopathies</topic><topic>transmissible spongiform encephalopathy</topic><topic>Virus Replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cancellotti, Enrico</creatorcontrib><creatorcontrib>Mahal, Sukhvir P</creatorcontrib><creatorcontrib>Somerville, Robert</creatorcontrib><creatorcontrib>Diack, Abigail</creatorcontrib><creatorcontrib>Brown, Deborah</creatorcontrib><creatorcontrib>Piccardo, Pedro</creatorcontrib><creatorcontrib>Weissmann, Charles</creatorcontrib><creatorcontrib>Manson, Jean C</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Cancellotti, Enrico</au><au>Mahal, Sukhvir P</au><au>Somerville, Robert</au><au>Diack, Abigail</au><au>Brown, Deborah</au><au>Piccardo, Pedro</au><au>Weissmann, Charles</au><au>Manson, Jean C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2013-03-06</date><risdate>2013</risdate><volume>32</volume><issue>5</issue><spage>756</spage><epage>769</epage><pages>756-769</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The agents responsible for transmissible spongiform encephalopathies (TSEs), or prion diseases, contain as a major component PrP
Sc
, an abnormal conformer of the host glycoprotein PrP
C
. TSE agents are distinguished by differences in phenotypic properties in the host, which nevertheless can contain PrP
Sc
with the same amino‐acid sequence. If PrP alone carries information defining strain properties, these must be encoded by post‐translational events. Here we investigated whether the glycosylation status of host PrP affects TSE strain characteristics. We inoculated wild‐type mice with three TSE strains passaged through transgenic mice with PrP devoid of glycans at the first, second or both N‐glycosylation sites. We compared the infectious properties of the emerging isolates with TSE strains passaged in wild‐type mice by
in vivo
strain typing and by the standard scrapie cell assay
in vitro
. Strain‐specific characteristics of the 79A TSE strain changed when PrP
Sc
was devoid of one or both glycans. Thus infectious properties of a TSE strain can be altered by post‐translational changes to PrP which we propose result in the selection of mutant TSE strains.
N‐linked glycosylation of the endogenous and wild‐type prion protein, PrP, alters the infectious properties of prion strains in mice.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>23395905</pmid><doi>10.1038/emboj.2013.6</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext_linktorsrc |
identifier | ISSN: 0261-4189 |
ispartof | The EMBO journal, 2013-03, Vol.32 (5), p.756-769 |
issn | 0261-4189 1460-2075 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3590993 |
source | Springer Nature OA Free Journals |
subjects | Animals Blotting, Western Brain - virology Cells, Cultured EMBO27 EMBO31 Female Glycoproteins Glycosylation Immunoenzyme Techniques Male Mice Mice, Inbred C57BL Mice, Transgenic Molecular biology Neuroblastoma - metabolism Neuroblastoma - pathology Neuroblastoma - virology phenotypic change Polysaccharides - metabolism prion Prion Diseases - metabolism Prion Diseases - transmission Prion Diseases - virology Protein Processing, Post-Translational PrPSc Proteins - genetics PrPSc Proteins - metabolism PrPSc Proteins - pathogenicity Spongiform encephalopathies transmissible spongiform encephalopathy Virus Replication |
title | Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T22%3A27%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_C6C&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Post-translational%20changes%20to%20PrP%20alter%20transmissible%20spongiform%20encephalopathy%20strain%20properties&rft.jtitle=The%20EMBO%20journal&rft.au=Cancellotti,%20Enrico&rft.date=2013-03-06&rft.volume=32&rft.issue=5&rft.spage=756&rft.epage=769&rft.pages=756-769&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1038/emboj.2013.6&rft_dat=%3Cproquest_C6C%3E1315135334%3C/proquest_C6C%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1314773829&rft_id=info:pmid/23395905&rfr_iscdi=true |