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Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion
The concept that transmissible spongiform encephalopathies (TSEs) are caused only by proteins has changed the traditional paradigm that disease transmission is due solely to an agent that carries genetic information. The central hypothesis for prion diseases proposes that the conversion of a cellula...
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Published in: | Methods (San Diego, Calif.) Calif.), 2011-03, Vol.53 (3), p.306-317 |
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description | The concept that transmissible spongiform encephalopathies (TSEs) are caused only by proteins has changed the traditional paradigm that disease transmission is due solely to an agent that carries genetic information. The central hypothesis for prion diseases proposes that the conversion of a cellular prion protein (PrPC) into a misfolded, β-sheet-rich isoform (PrPSc) accounts for the development of (TSE). There is substantial evidence that the infectious material consists chiefly of a protein, PrPSc, with no genomic coding material, unlike a virus particle, which has both. However, prions seem to have other partners that chaperone their activities in converting the PrPC into the disease-causing isoform. Nucleic acids (NAs) and glycosaminoglycans (GAGs) are the most probable accomplices of prion conversion. Here, we review the recent experimental approaches that have been employed to characterize the interaction of prion proteins with nucleic acids and glycosaminoglycans. A PrP recognizes many nucleic acids and GAGs with high affinities, and this seems to be related to a pathophysiological role for this interaction. A PrP binds nucleic acids and GAGs with structural selectivity, and some PrP:NA complexes can become proteinase K-resistant, undergoing amyloid oligomerization and conversion to a β-sheet-rich structure. These results are consistent with the hypothesis that endogenous polyanions (such as NAs and GAGs) may accelerate the rate of prion disease progression by acting as scaffolds or lattices that mediate the interaction between PrPC and PrPSc molecules. In addition to a still-possible hypothesis that nucleic acids and GAGs, especially those from the host, may modulate the conversion, the recent structural characterization of the complexes has raised the possibility of developing new diagnostic and therapeutic strategies. |
doi_str_mv | 10.1016/j.ymeth.2010.12.002 |
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The central hypothesis for prion diseases proposes that the conversion of a cellular prion protein (PrPC) into a misfolded, β-sheet-rich isoform (PrPSc) accounts for the development of (TSE). There is substantial evidence that the infectious material consists chiefly of a protein, PrPSc, with no genomic coding material, unlike a virus particle, which has both. However, prions seem to have other partners that chaperone their activities in converting the PrPC into the disease-causing isoform. Nucleic acids (NAs) and glycosaminoglycans (GAGs) are the most probable accomplices of prion conversion. Here, we review the recent experimental approaches that have been employed to characterize the interaction of prion proteins with nucleic acids and glycosaminoglycans. A PrP recognizes many nucleic acids and GAGs with high affinities, and this seems to be related to a pathophysiological role for this interaction. A PrP binds nucleic acids and GAGs with structural selectivity, and some PrP:NA complexes can become proteinase K-resistant, undergoing amyloid oligomerization and conversion to a β-sheet-rich structure. These results are consistent with the hypothesis that endogenous polyanions (such as NAs and GAGs) may accelerate the rate of prion disease progression by acting as scaffolds or lattices that mediate the interaction between PrPC and PrPSc molecules. In addition to a still-possible hypothesis that nucleic acids and GAGs, especially those from the host, may modulate the conversion, the recent structural characterization of the complexes has raised the possibility of developing new diagnostic and therapeutic strategies.</description><identifier>ISSN: 1046-2023</identifier><identifier>EISSN: 1095-9130</identifier><identifier>DOI: 10.1016/j.ymeth.2010.12.002</identifier><identifier>PMID: 21145399</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amyloid ; Animals ; Chaperones ; Disease transmission ; DNA - chemistry ; DNA - metabolism ; Encephalopathy ; Gag protein ; genomics ; Glycosaminoglycans ; Glycosaminoglycans - chemistry ; Glycosaminoglycans - metabolism ; Humans ; Neurodegenerative diseases ; Nucleic acids ; Oligomerization ; Polyanions ; Prion Diseases - diagnosis ; Prion Diseases - drug therapy ; Prion Diseases - prevention & control ; Prion protein ; Prions - chemistry ; Prions - metabolism ; Prions - pathogenicity ; Protein Conformation ; Protein Transport ; Proteinase ; PrP ; PrP conversion ; PrP partners ; PrP structure ; Reviews ; RNA - chemistry ; RNA - metabolism ; scaffolds ; Transmissible spongiform ; Transmissible spongiform encephalopathy</subject><ispartof>Methods (San Diego, Calif.), 2011-03, Vol.53 (3), p.306-317</ispartof><rights>2010 Elsevier Inc.</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c435t-d0ed770793aa885f658e7c417c6061d02cfd53671b6b6c7e73d4039ead4c7fd13</citedby><cites>FETCH-LOGICAL-c435t-d0ed770793aa885f658e7c417c6061d02cfd53671b6b6c7e73d4039ead4c7fd13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21145399$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Silva, Jerson L.</creatorcontrib><creatorcontrib>Vieira, Tuane C.R.G.</creatorcontrib><creatorcontrib>Gomes, Mariana P.B.</creatorcontrib><creatorcontrib>Rangel, Luciana P.</creatorcontrib><creatorcontrib>Scapin, Sandra M.N.</creatorcontrib><creatorcontrib>Cordeiro, Yraima</creatorcontrib><title>Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion</title><title>Methods (San Diego, Calif.)</title><addtitle>Methods</addtitle><description>The concept that transmissible spongiform encephalopathies (TSEs) are caused only by proteins has changed the traditional paradigm that disease transmission is due solely to an agent that carries genetic information. The central hypothesis for prion diseases proposes that the conversion of a cellular prion protein (PrPC) into a misfolded, β-sheet-rich isoform (PrPSc) accounts for the development of (TSE). There is substantial evidence that the infectious material consists chiefly of a protein, PrPSc, with no genomic coding material, unlike a virus particle, which has both. However, prions seem to have other partners that chaperone their activities in converting the PrPC into the disease-causing isoform. Nucleic acids (NAs) and glycosaminoglycans (GAGs) are the most probable accomplices of prion conversion. Here, we review the recent experimental approaches that have been employed to characterize the interaction of prion proteins with nucleic acids and glycosaminoglycans. A PrP recognizes many nucleic acids and GAGs with high affinities, and this seems to be related to a pathophysiological role for this interaction. A PrP binds nucleic acids and GAGs with structural selectivity, and some PrP:NA complexes can become proteinase K-resistant, undergoing amyloid oligomerization and conversion to a β-sheet-rich structure. These results are consistent with the hypothesis that endogenous polyanions (such as NAs and GAGs) may accelerate the rate of prion disease progression by acting as scaffolds or lattices that mediate the interaction between PrPC and PrPSc molecules. In addition to a still-possible hypothesis that nucleic acids and GAGs, especially those from the host, may modulate the conversion, the recent structural characterization of the complexes has raised the possibility of developing new diagnostic and therapeutic strategies.</description><subject>Amyloid</subject><subject>Animals</subject><subject>Chaperones</subject><subject>Disease transmission</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>Encephalopathy</subject><subject>Gag protein</subject><subject>genomics</subject><subject>Glycosaminoglycans</subject><subject>Glycosaminoglycans - chemistry</subject><subject>Glycosaminoglycans - metabolism</subject><subject>Humans</subject><subject>Neurodegenerative diseases</subject><subject>Nucleic acids</subject><subject>Oligomerization</subject><subject>Polyanions</subject><subject>Prion Diseases - diagnosis</subject><subject>Prion Diseases - drug therapy</subject><subject>Prion Diseases - prevention & control</subject><subject>Prion protein</subject><subject>Prions - chemistry</subject><subject>Prions - metabolism</subject><subject>Prions - pathogenicity</subject><subject>Protein Conformation</subject><subject>Protein Transport</subject><subject>Proteinase</subject><subject>PrP</subject><subject>PrP conversion</subject><subject>PrP partners</subject><subject>PrP structure</subject><subject>Reviews</subject><subject>RNA - chemistry</subject><subject>RNA - metabolism</subject><subject>scaffolds</subject><subject>Transmissible spongiform</subject><subject>Transmissible spongiform encephalopathy</subject><issn>1046-2023</issn><issn>1095-9130</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNqFkc1u1DAUhS0EoqXwBEjIO1YZ_JPYMRILVJUfqaibsrY89k3jUWIPtlOY1-gT43RKl2Xl66vvHMvnIPSWkg0lVHzYbQ4zlHHDyLphG0LYM3RKieoaRTl5vs6taBhh_AS9ynlHCKFM9i_RCaO07bhSp-ju4s8ekp8hFDNhs9-naOwIGZeIywjYhwLJ2OJjwHG4X-3TeqlgAR_wb19GHBY7gbfYWO8yNsHhm-lgYzazD3EdTcgf8Y_olsmUmPKjlSljvIFQpTaGW0i5Wr9GLwYzZXjzcJ6hn18urs-_NZdXX7-ff75sbMu70jgCTkoiFTem77tBdD1I21JpBRHUEWYH13Eh6VZshZUguWsJV2Bca-XgKD9D74--9Su_FshFzz5bmCYTIC5Zqxpcy7ng_yX7rlOEM6EqyY-kTTHnBIOuac0mHTQlem1N7_R9a3ptTVOma2tV9e7Bf9nO4B41_2qqwKcjADWPWw9JZ-shWHA-gS3aRf_kA38BubutQw</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Silva, Jerson L.</creator><creator>Vieira, Tuane C.R.G.</creator><creator>Gomes, Mariana P.B.</creator><creator>Rangel, Luciana P.</creator><creator>Scapin, Sandra M.N.</creator><creator>Cordeiro, Yraima</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20110301</creationdate><title>Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion</title><author>Silva, Jerson L. ; Vieira, Tuane C.R.G. ; Gomes, Mariana P.B. ; Rangel, Luciana P. ; Scapin, Sandra M.N. ; Cordeiro, Yraima</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-d0ed770793aa885f658e7c417c6061d02cfd53671b6b6c7e73d4039ead4c7fd13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amyloid</topic><topic>Animals</topic><topic>Chaperones</topic><topic>Disease transmission</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>Encephalopathy</topic><topic>Gag protein</topic><topic>genomics</topic><topic>Glycosaminoglycans</topic><topic>Glycosaminoglycans - chemistry</topic><topic>Glycosaminoglycans - metabolism</topic><topic>Humans</topic><topic>Neurodegenerative diseases</topic><topic>Nucleic acids</topic><topic>Oligomerization</topic><topic>Polyanions</topic><topic>Prion Diseases - diagnosis</topic><topic>Prion Diseases - drug therapy</topic><topic>Prion Diseases - prevention & control</topic><topic>Prion protein</topic><topic>Prions - chemistry</topic><topic>Prions - metabolism</topic><topic>Prions - pathogenicity</topic><topic>Protein Conformation</topic><topic>Protein Transport</topic><topic>Proteinase</topic><topic>PrP</topic><topic>PrP conversion</topic><topic>PrP partners</topic><topic>PrP structure</topic><topic>Reviews</topic><topic>RNA - chemistry</topic><topic>RNA - metabolism</topic><topic>scaffolds</topic><topic>Transmissible spongiform</topic><topic>Transmissible spongiform encephalopathy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Silva, Jerson L.</creatorcontrib><creatorcontrib>Vieira, Tuane C.R.G.</creatorcontrib><creatorcontrib>Gomes, Mariana P.B.</creatorcontrib><creatorcontrib>Rangel, Luciana P.</creatorcontrib><creatorcontrib>Scapin, Sandra M.N.</creatorcontrib><creatorcontrib>Cordeiro, Yraima</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Methods (San Diego, Calif.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Silva, Jerson L.</au><au>Vieira, Tuane C.R.G.</au><au>Gomes, Mariana P.B.</au><au>Rangel, Luciana P.</au><au>Scapin, Sandra M.N.</au><au>Cordeiro, Yraima</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion</atitle><jtitle>Methods (San Diego, Calif.)</jtitle><addtitle>Methods</addtitle><date>2011-03-01</date><risdate>2011</risdate><volume>53</volume><issue>3</issue><spage>306</spage><epage>317</epage><pages>306-317</pages><issn>1046-2023</issn><eissn>1095-9130</eissn><abstract>The concept that transmissible spongiform encephalopathies (TSEs) are caused only by proteins has changed the traditional paradigm that disease transmission is due solely to an agent that carries genetic information. The central hypothesis for prion diseases proposes that the conversion of a cellular prion protein (PrPC) into a misfolded, β-sheet-rich isoform (PrPSc) accounts for the development of (TSE). There is substantial evidence that the infectious material consists chiefly of a protein, PrPSc, with no genomic coding material, unlike a virus particle, which has both. However, prions seem to have other partners that chaperone their activities in converting the PrPC into the disease-causing isoform. Nucleic acids (NAs) and glycosaminoglycans (GAGs) are the most probable accomplices of prion conversion. Here, we review the recent experimental approaches that have been employed to characterize the interaction of prion proteins with nucleic acids and glycosaminoglycans. A PrP recognizes many nucleic acids and GAGs with high affinities, and this seems to be related to a pathophysiological role for this interaction. A PrP binds nucleic acids and GAGs with structural selectivity, and some PrP:NA complexes can become proteinase K-resistant, undergoing amyloid oligomerization and conversion to a β-sheet-rich structure. These results are consistent with the hypothesis that endogenous polyanions (such as NAs and GAGs) may accelerate the rate of prion disease progression by acting as scaffolds or lattices that mediate the interaction between PrPC and PrPSc molecules. In addition to a still-possible hypothesis that nucleic acids and GAGs, especially those from the host, may modulate the conversion, the recent structural characterization of the complexes has raised the possibility of developing new diagnostic and therapeutic strategies.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21145399</pmid><doi>10.1016/j.ymeth.2010.12.002</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amyloid Animals Chaperones Disease transmission DNA - chemistry DNA - metabolism Encephalopathy Gag protein genomics Glycosaminoglycans Glycosaminoglycans - chemistry Glycosaminoglycans - metabolism Humans Neurodegenerative diseases Nucleic acids Oligomerization Polyanions Prion Diseases - diagnosis Prion Diseases - drug therapy Prion Diseases - prevention & control Prion protein Prions - chemistry Prions - metabolism Prions - pathogenicity Protein Conformation Protein Transport Proteinase PrP PrP conversion PrP partners PrP structure Reviews RNA - chemistry RNA - metabolism scaffolds Transmissible spongiform Transmissible spongiform encephalopathy |
title | Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion |
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