Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins
The conversion of cellular prion protein (PrPC) to disease-provoking conformer (PrPSc) is crucial in the pathogenesis of prion diseases. Heparin has been shown to enhance mammalian prion protein misfolding. As spontaneous prion disease has not been reported in non-mammalian species, such as chicken,...
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| description | The conversion of cellular prion protein (PrPC) to disease-provoking conformer (PrPSc) is crucial in the pathogenesis of prion diseases. Heparin has been shown to enhance mammalian prion protein misfolding. As spontaneous prion disease has not been reported in non-mammalian species, such as chicken, it is interesting to explore the influence of heparin on the conversion of chicken prion protein (ChPrP). Herein, we investigated the influences of heparin on biochemical properties of full-length recombinant ChPrP, with murine prion protein (MoPrP) as control. The results showed that at low heparin concentration (10 μg/mL), a great loss of solubility was observed for both MoPrP and ChPrP using solubility assays. In contrast, when the concentration of heparin was high (30 μg/mL), the solubility of MoPrP and ChPrP both decreased slightly. Using circular dichroism, PK digestion and transmission electron microscopy, significantly increased β-sheet content, PK resistance and size of aggregates were observed for MoPrP interacted with 30 μg/mL heparin, whereas 30 μg/mL heparin-treated ChPrP showed less PK resistance and slight increase of β-sheet structure. Therefore, heparin can induce conformational changes in both MoPrP and ChPrP and the biochemical properties of the aggregates induced by heparin could be modified by heparin concentration. These results highlight the importance of concentration of cofactors affecting PrP misfolding. |
| doi_str_mv | 10.1371/journal.pone.0247248 |
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Heparin has been shown to enhance mammalian prion protein misfolding. As spontaneous prion disease has not been reported in non-mammalian species, such as chicken, it is interesting to explore the influence of heparin on the conversion of chicken prion protein (ChPrP). Herein, we investigated the influences of heparin on biochemical properties of full-length recombinant ChPrP, with murine prion protein (MoPrP) as control. The results showed that at low heparin concentration (10 μg/mL), a great loss of solubility was observed for both MoPrP and ChPrP using solubility assays. In contrast, when the concentration of heparin was high (30 μg/mL), the solubility of MoPrP and ChPrP both decreased slightly. Using circular dichroism, PK digestion and transmission electron microscopy, significantly increased β-sheet content, PK resistance and size of aggregates were observed for MoPrP interacted with 30 μg/mL heparin, whereas 30 μg/mL heparin-treated ChPrP showed less PK resistance and slight increase of β-sheet structure. Therefore, heparin can induce conformational changes in both MoPrP and ChPrP and the biochemical properties of the aggregates induced by heparin could be modified by heparin concentration. These results highlight the importance of concentration of cofactors affecting PrP misfolding.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0247248</identifier><identifier>PMID: 33600459</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Ablation ; Anticoagulants ; Biology and Life Sciences ; Biomedical research ; Bovine spongiform encephalopathy ; Central nervous system ; Chemical properties ; Chickens ; Comparative analysis ; Creutzfeldt-Jakob disease ; Disease ; Drug development ; Editing ; Electronic mail ; Engineering ; Funding ; Health aspects ; Heparan sulfate ; Heparin ; Laboratories ; Life sciences ; Mail ; Mammals ; Medicine and Health Sciences ; Methodology ; Neurodegeneration ; Neurodegenerative diseases ; Physical Sciences ; Physiological aspects ; Poultry ; Prion protein ; Prions ; Proteins ; Research and Analysis Methods ; Research facilities ; Reviews ; Technology</subject><ispartof>PloS one, 2021-02, Vol.16 (2), p.e0247248-e0247248</ispartof><rights>COPYRIGHT 2021 Public Library of Science</rights><rights>2021 Wang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 Wang et al 2021 Wang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c641t-dc7a8eb64b29b19f7b8d2b5a3e70416474bc110b811d77a2367cef6830b3ef763</cites><orcidid>0000-0001-6505-6900</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7891698/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7891698/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33600459$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Li-Juan</creatorcontrib><creatorcontrib>Gu, Xiao-Dan</creatorcontrib><creatorcontrib>Li, Xiao-Xiao</creatorcontrib><creatorcontrib>Shen, Liang</creatorcontrib><creatorcontrib>Ji, Hong-Fang</creatorcontrib><title>Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The conversion of cellular prion protein (PrPC) to disease-provoking conformer (PrPSc) is crucial in the pathogenesis of prion diseases. Heparin has been shown to enhance mammalian prion protein misfolding. As spontaneous prion disease has not been reported in non-mammalian species, such as chicken, it is interesting to explore the influence of heparin on the conversion of chicken prion protein (ChPrP). Herein, we investigated the influences of heparin on biochemical properties of full-length recombinant ChPrP, with murine prion protein (MoPrP) as control. The results showed that at low heparin concentration (10 μg/mL), a great loss of solubility was observed for both MoPrP and ChPrP using solubility assays. In contrast, when the concentration of heparin was high (30 μg/mL), the solubility of MoPrP and ChPrP both decreased slightly. Using circular dichroism, PK digestion and transmission electron microscopy, significantly increased β-sheet content, PK resistance and size of aggregates were observed for MoPrP interacted with 30 μg/mL heparin, whereas 30 μg/mL heparin-treated ChPrP showed less PK resistance and slight increase of β-sheet structure. Therefore, heparin can induce conformational changes in both MoPrP and ChPrP and the biochemical properties of the aggregates induced by heparin could be modified by heparin concentration. These results highlight the importance of concentration of cofactors affecting PrP misfolding.</description><subject>Ablation</subject><subject>Anticoagulants</subject><subject>Biology and Life Sciences</subject><subject>Biomedical research</subject><subject>Bovine spongiform encephalopathy</subject><subject>Central nervous system</subject><subject>Chemical properties</subject><subject>Chickens</subject><subject>Comparative analysis</subject><subject>Creutzfeldt-Jakob disease</subject><subject>Disease</subject><subject>Drug development</subject><subject>Editing</subject><subject>Electronic mail</subject><subject>Engineering</subject><subject>Funding</subject><subject>Health aspects</subject><subject>Heparan sulfate</subject><subject>Heparin</subject><subject>Laboratories</subject><subject>Life sciences</subject><subject>Mail</subject><subject>Mammals</subject><subject>Medicine and Health 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One</addtitle><date>2021-02-18</date><risdate>2021</risdate><volume>16</volume><issue>2</issue><spage>e0247248</spage><epage>e0247248</epage><pages>e0247248-e0247248</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The conversion of cellular prion protein (PrPC) to disease-provoking conformer (PrPSc) is crucial in the pathogenesis of prion diseases. Heparin has been shown to enhance mammalian prion protein misfolding. As spontaneous prion disease has not been reported in non-mammalian species, such as chicken, it is interesting to explore the influence of heparin on the conversion of chicken prion protein (ChPrP). Herein, we investigated the influences of heparin on biochemical properties of full-length recombinant ChPrP, with murine prion protein (MoPrP) as control. The results showed that at low heparin concentration (10 μg/mL), a great loss of solubility was observed for both MoPrP and ChPrP using solubility assays. In contrast, when the concentration of heparin was high (30 μg/mL), the solubility of MoPrP and ChPrP both decreased slightly. Using circular dichroism, PK digestion and transmission electron microscopy, significantly increased β-sheet content, PK resistance and size of aggregates were observed for MoPrP interacted with 30 μg/mL heparin, whereas 30 μg/mL heparin-treated ChPrP showed less PK resistance and slight increase of β-sheet structure. Therefore, heparin can induce conformational changes in both MoPrP and ChPrP and the biochemical properties of the aggregates induced by heparin could be modified by heparin concentration. These results highlight the importance of concentration of cofactors affecting PrP misfolding.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>33600459</pmid><doi>10.1371/journal.pone.0247248</doi><tpages>e0247248</tpages><orcidid>https://orcid.org/0000-0001-6505-6900</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Ablation Anticoagulants Biology and Life Sciences Biomedical research Bovine spongiform encephalopathy Central nervous system Chemical properties Chickens Comparative analysis Creutzfeldt-Jakob disease Disease Drug development Editing Electronic mail Engineering Funding Health aspects Heparan sulfate Heparin Laboratories Life sciences Mammals Medicine and Health Sciences Methodology Neurodegeneration Neurodegenerative diseases Physical Sciences Physiological aspects Poultry Prion protein Prions Proteins Research and Analysis Methods Research facilities Reviews Technology |
| title | Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins |
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