Glycosylation influences cross‐species formation of protease‐resistant prion protein
A key event in the transmissible spongiform encephalopathies (TSEs) is the formation of aggregated and protease‐resistant prion protein, PrP‐res, from a normally soluble, protease‐sensitive and glycosylated precursor, PrP‐sen. While amino acid sequence similarity between PrP‐sen and PrP‐res influenc...
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| Veröffentlicht in: | The EMBO journal 2001-12, Vol.20 (23), p.6692-6699 |
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| description | A key event in the transmissible spongiform encephalopathies (TSEs) is the formation of aggregated and protease‐resistant prion protein, PrP‐res, from a normally soluble, protease‐sensitive and glycosylated precursor, PrP‐sen. While amino acid sequence similarity between PrP‐sen and PrP‐res influences both PrP‐res formation and cross‐species transmission of infectivity, the influence of co‐ or post‐translational modifications to PrP‐sen is unknown. Here we report that, if PrP‐sen and PrP‐res are derived from different species, PrP‐sen glycosylation can significantly affect PrP‐res formation. Glycosylation affected PrP‐res formation by influencing the amount of PrP‐sen bound to PrP‐res, while the amino acid sequence of PrP‐sen influenced the amount of PrP‐res generated in the post‐binding conversion step. Our results show that in addition to amino acid sequence, co‐ or post‐translational modifications to PrP‐sen influence PrP‐res formation
in vitro
.
In vivo
, these modifications might contribute to the resistance to infection associated with transmission of TSE infectivity across species barriers. |
| doi_str_mv | 10.1093/emboj/20.23.6692 |
| format | Article |
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in vitro
.
In vivo
, these modifications might contribute to the resistance to infection associated with transmission of TSE infectivity across species barriers.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.23.6692</identifier><identifier>PMID: 11726505</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino acids ; Animals ; Anti-Bacterial Agents - pharmacology ; Antiviral Agents - pharmacology ; Cell-Free System ; Cloning, Molecular ; Cricetinae ; Dose-Response Relationship, Drug ; Endopeptidases - metabolism ; Epitopes ; Glycosylation ; Mice ; Precipitin Tests ; Prion Diseases - transmission ; prion protein ; Prions - metabolism ; Protein Binding ; Protein Processing, Post-Translational ; PrP ; PrPC Proteins - metabolism ; PrPSc Proteins - metabolism ; Recombinant Proteins - metabolism ; Recombinant Proteins - pharmacology ; scrapie ; Species Specificity ; Tunicamycin - pharmacology</subject><ispartof>The EMBO journal, 2001-12, Vol.20 (23), p.6692-6699</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Dec 03, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125748/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125748/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27923,27924,45573,45574,46408,46832,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11726505$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Priola, Suzette A.</creatorcontrib><creatorcontrib>Lawson, Victoria A.</creatorcontrib><title>Glycosylation influences cross‐species formation of protease‐resistant prion protein</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>A key event in the transmissible spongiform encephalopathies (TSEs) is the formation of aggregated and protease‐resistant prion protein, PrP‐res, from a normally soluble, protease‐sensitive and glycosylated precursor, PrP‐sen. While amino acid sequence similarity between PrP‐sen and PrP‐res influences both PrP‐res formation and cross‐species transmission of infectivity, the influence of co‐ or post‐translational modifications to PrP‐sen is unknown. Here we report that, if PrP‐sen and PrP‐res are derived from different species, PrP‐sen glycosylation can significantly affect PrP‐res formation. Glycosylation affected PrP‐res formation by influencing the amount of PrP‐sen bound to PrP‐res, while the amino acid sequence of PrP‐sen influenced the amount of PrP‐res generated in the post‐binding conversion step. Our results show that in addition to amino acid sequence, co‐ or post‐translational modifications to PrP‐sen influence PrP‐res formation
in vitro
.
In vivo
, these modifications might contribute to the resistance to infection associated with transmission of TSE infectivity across species barriers.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antiviral Agents - pharmacology</subject><subject>Cell-Free System</subject><subject>Cloning, Molecular</subject><subject>Cricetinae</subject><subject>Dose-Response Relationship, Drug</subject><subject>Endopeptidases - metabolism</subject><subject>Epitopes</subject><subject>Glycosylation</subject><subject>Mice</subject><subject>Precipitin Tests</subject><subject>Prion Diseases - transmission</subject><subject>prion protein</subject><subject>Prions - metabolism</subject><subject>Protein Binding</subject><subject>Protein Processing, Post-Translational</subject><subject>PrP</subject><subject>PrPC Proteins - metabolism</subject><subject>PrPSc Proteins - metabolism</subject><subject>Recombinant Proteins - 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Post-Translational</topic><topic>PrP</topic><topic>PrPC Proteins - metabolism</topic><topic>PrPSc Proteins - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Recombinant Proteins - pharmacology</topic><topic>scrapie</topic><topic>Species Specificity</topic><topic>Tunicamycin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Priola, Suzette A.</creatorcontrib><creatorcontrib>Lawson, Victoria A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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 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Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Priola, Suzette A.</au><au>Lawson, Victoria A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycosylation influences cross‐species formation of protease‐resistant prion protein</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2001-12-03</date><risdate>2001</risdate><volume>20</volume><issue>23</issue><spage>6692</spage><epage>6699</epage><pages>6692-6699</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>A key event in the transmissible spongiform encephalopathies (TSEs) is the formation of aggregated and protease‐resistant prion protein, PrP‐res, from a normally soluble, protease‐sensitive and glycosylated precursor, PrP‐sen. While amino acid sequence similarity between PrP‐sen and PrP‐res influences both PrP‐res formation and cross‐species transmission of infectivity, the influence of co‐ or post‐translational modifications to PrP‐sen is unknown. Here we report that, if PrP‐sen and PrP‐res are derived from different species, PrP‐sen glycosylation can significantly affect PrP‐res formation. Glycosylation affected PrP‐res formation by influencing the amount of PrP‐sen bound to PrP‐res, while the amino acid sequence of PrP‐sen influenced the amount of PrP‐res generated in the post‐binding conversion step. Our results show that in addition to amino acid sequence, co‐ or post‐translational modifications to PrP‐sen influence PrP‐res formation
in vitro
.
In vivo
, these modifications might contribute to the resistance to infection associated with transmission of TSE infectivity across species barriers.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11726505</pmid><doi>10.1093/emboj/20.23.6692</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids Animals Anti-Bacterial Agents - pharmacology Antiviral Agents - pharmacology Cell-Free System Cloning, Molecular Cricetinae Dose-Response Relationship, Drug Endopeptidases - metabolism Epitopes Glycosylation Mice Precipitin Tests Prion Diseases - transmission prion protein Prions - metabolism Protein Binding Protein Processing, Post-Translational PrP PrPC Proteins - metabolism PrPSc Proteins - metabolism Recombinant Proteins - metabolism Recombinant Proteins - pharmacology scrapie Species Specificity Tunicamycin - pharmacology |
| title | Glycosylation influences cross‐species formation of protease‐resistant prion protein |
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