Introducing a Rigid Loop Structure from Deer into Mouse Prion Protein Increases Its Propensity for Misfolding In Vitro
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{"title"=>"Introducing a Rigid Loop Structure from Deer into Mouse Prion Protein Increases Its Propensity for Misfolding In Vitro", "type"=>"journal", "authors"=>[{"first_name"=>"Leah M.", "last_name"=>"Kyle", "scopus_author_id"=>"56052869000"}, {"first_name"=>"Theodore R.", "last_name"=>"John", "scopus_author_id"=>"55774679600"}, {"first_name"=>"Hermann M.", "last_name"=>"Schätzl", "scopus_author_id"=>"7004486352"}, {"first_name"=>"Randolph V.", "last_name"=>"Lewis", "scopus_author_id"=>"55605773265"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84879356527", "sgr"=>"84879356527", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0066715", "pmid"=>"23825561", "isbn"=>"1932-6203 (Electronic)\r1932-6203 (Linking)", "pui"=>"369184497"}, "id"=>"c272e018-c798-3c15-8d27-af7827af9cfe", "abstract"=>"Prion diseases are fatal neurodegenerative disorders characterized by misfolding of the cellular prion protein (PrP(c)) into the disease-associated isoform (PrP(Sc)) that has increased β-sheet content and partial resistance to proteolytic digestion. Prion diseases from different mammalian species have varying propensities for transmission upon exposure of an uninfected host to the infectious agent. Chronic Wasting Disease (CWD) is a highly transmissible prion disease that affects free ranging and farmed populations of cervids including deer, elk and moose, as well as other mammals in experimental settings. The molecular mechanisms allowing CWD to maintain comparatively high transmission rates have not been determined. Previous work has identified a unique structural feature in cervid PrP, a rigid loop between β-sheet 2 and α-helix 2 on the surface of the protein. This study was designed to test the hypothesis that the rigid loop has a direct influence on the misfolding process. The rigid loop was introduced into murine PrP as the result of two amino acid substitutions: S170N and N174T. Wild-type and rigid loop murine PrP were expressed in E. coli and purified. Misfolding propensity was compared for the two proteins using biochemical techniques and cell free misfolding and conversion systems. Murine PrP with a rigid loop misfolded in cell free systems with greater propensity than wild type murine PrP. In a lipid-based conversion assay, rigid loop PrP converted to a PK resistant, aggregated isoform at lower concentrations than wild-type PrP. Using both proteins as substrates in real time quaking-induced conversion, rigid loop PrP adopted a misfolded isoform more readily than wild type PrP. Taken together, these findings may help explain the high transmission rates observed for CWD within cervids.", "link"=>"http://www.mendeley.com/research/introducing-rigid-loop-structure-deer-mouse-prion-protein-increases-propensity-misfolding-vitro", "reader_count"=>27, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Student > Doctoral Student"=>3, "Researcher"=>7, "Student > Ph. D. Student"=>8, "Other"=>1, "Student > Master"=>2, "Professor"=>5}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Student > Doctoral Student"=>3, "Researcher"=>7, "Student > Ph. D. Student"=>8, "Other"=>1, "Student > Master"=>2, "Professor"=>5}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>9, "Agricultural and Biological Sciences"=>13, "Medicine and Dentistry"=>1, "Neuroscience"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Neuroscience"=>{"Neuroscience"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>13}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>9}, "Unspecified"=>{"Unspecified"=>2}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>2}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1100963"], "description"=>"<p>RT-QuIC reactions containing moPrP<sup>WT</sup> (green lines) and moPrP<sup>RL</sup> (purples lines) were seeded with brain homogenate from terminally ill 22 L prion infected mice (solid lines) or brain homogenate from mock infected controls (dashed lines) at a dilution of 2×10<sup>−2</sup> (A) or 2×10<sup>−3</sup> (B). Relative fluorescence over time was averaged for quadruplicate reactions. Time at beginning of conversion determined as the time point at which fluorescence rose from baseline to above 24,000 fluorescence units was compared for both dilutions of 22 L prion seed using GraphPad Prism software (shown in hours; data from 3 independent experiments) (C). Reactions with moPrP<sup>RL</sup> as a substrate exhibited earlier conversion to a Thioflavin T positive amyloid structure than reactions with moPrP<sup>WT</sup> substrate.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "biophysics", "Protein folding", "Molecular cell biology", "Infectious diseases", "Prion diseases", "Veterinary diseases", "Zoonotic diseases", "Veterinary prion diseases", "thioflavin", "isoform", "rt-quic", "occurs"], "article_id"=>731405, "categories"=>["Physics", "Medicine", "Biological Sciences"], "users"=>["Leah M. Kyle", "Theodore R. John", "Hermann M. Schätzl", "Randolph V. Lewis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0066715.g004", "stats"=>{"downloads"=>1, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Generation_of_a_Thioflavin_T_positive_isoform_via_RT_QuIC_occurs_faster_for_moPrP_RL_than_moPrP_WT_/731405", "title"=>"Generation of a Thioflavin T positive isoform via RT-QuIC occurs faster for moPrP<sup>RL</sup> than moPrP<sup>WT</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-25 03:22:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1100962"], "description"=>"<p>Differences in secondary structure between moPrP<sup>WT</sup> and moPrP<sup>RL</sup> are not detectible by circular dichroism (CD) as shown by their nearly identical CD spectra (solid lines). Upon addition of POPG lipid vesicles, the secondary structure of both moPrP<sup>WT</sup> and moPrP<sup>RL</sup> changed to reflect an increase in β-sheet content (dashed lines). In the presence of lipids, moPrP<sup>WT</sup> and moPrP<sup>RL</sup> do not exhibit identical CD spectra (dashed lines), possibly indicating differences in lipid induced secondary structural changes between these molecules.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "biophysics", "Protein folding", "Molecular cell biology", "Infectious diseases", "Prion diseases", "Veterinary diseases", "Zoonotic diseases", "Veterinary prion diseases", "lipid", "pk-resistant", "isoform", "accompanied"], "article_id"=>731404, "categories"=>["Physics", "Medicine", "Biological Sciences"], "users"=>["Leah M. Kyle", "Theodore R. John", "Hermann M. Schätzl", "Randolph V. Lewis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0066715.g003", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Generation_of_lipid_induced_PK_resistant_isoform_is_accompanied_by_a_structural_change_increasing_946_sheet_content_/731404", "title"=>"Generation of lipid induced, PK-resistant isoform is accompanied by a structural change increasing β-sheet content.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-25 03:22:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1100965"], "description"=>"<p>RT-QuIC reactions containing moPrP<sup>WT</sup> (green lines) and moPrP<sup>RL</sup> (purples lines) were seeded with brain homogenate from terminally ill CWD prion infected white-tailed deer (solid lines) or brain homogenate from uninfected controls (dashed lines) at a dilution of 2×10<sup>−3</sup> (A) or 2×10<sup>−4</sup> (B). Reactions were prepared in quadruplicate and average fluorescence over time was averaged for two independent experiments (C). Reactions with moPrP<sup>RL</sup> as a substrate exhibited earlier conversion than reactions with moPrP<sup>WT</sup> substrate when seeded with CWD prions from the brain of an infected white-tailed deer.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "biophysics", "Protein folding", "Molecular cell biology", "Infectious diseases", "Prion diseases", "Veterinary diseases", "Zoonotic diseases", "Veterinary prion diseases", "converts", "rt-quic", "reactions", "seeded", "cwd", "prions"], "article_id"=>731407, "categories"=>["Physics", "Medicine", "Biological Sciences"], "users"=>["Leah M. Kyle", "Theodore R. John", "Hermann M. Schätzl", "Randolph V. Lewis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0066715.g006", "stats"=>{"downloads"=>1, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_moPrP_RL_converts_faster_than_moPrP_WT_in_RT_QuIC_reactions_seeded_with_CWD_prions_from_deer_/731407", "title"=>"moPrP<sup>RL</sup> converts faster than moPrP<sup>WT</sup> in RT-QuIC reactions seeded with CWD prions from deer.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-25 03:22:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1100964"], "description"=>"<p>RT-QuIC reactions containing moPrP<sup>WT</sup> (green lines) and moPrP<sup>RL</sup> (purples lines) were seeded with brain homogenate from terminally ill CWD prion infected transgenic mice expressing deer PrP<sup>c</sup> (solid lines) or brain homogenate from mock infected control mice (dashed lines) at a dilution of 2×10<sup>−2</sup> (A) or 2×10<sup>−3</sup> (B). Data shown is the average of relative fluorescence over time for quadruplicate samples from two independent experiments. Reactions with moPrP<sup>RL</sup> as a substrate exhibited earlier conversion when seeded with mouse CWD prions than reactions with moPrP<sup>WT</sup> substrate (C).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "biophysics", "Protein folding", "Molecular cell biology", "Infectious diseases", "Prion diseases", "Veterinary diseases", "Zoonotic diseases", "Veterinary prion diseases", "converts", "rt-quic", "reactions", "seeded", "cwd", "prions", "transgenic"], "article_id"=>731406, "categories"=>["Physics", "Medicine", "Biological Sciences"], "users"=>["Leah M. Kyle", "Theodore R. John", "Hermann M. Schätzl", "Randolph V. Lewis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0066715.g005", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_moPrP_RL_converts_faster_than_moPrP_WT_in_RT_QuIC_reactions_seeded_with_CWD_prions_from_transgenic_mice_/731406", "title"=>"moPrP<sup>RL</sup> converts faster than moPrP<sup>WT</sup> in RT-QuIC reactions seeded with CWD prions from transgenic mice.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-25 03:22:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1100961"], "description"=>"<p>Lipid- (left panels, A–C) and lipid+ reactions (right panels, D–F) containing 100 µg/mL of moPrP<sup>WT</sup> or moPrP<sup>RL</sup> were assembled such that all incubations were completed simultaneously. Untreated samples (A and D) were removed and the remaining sample was subjected to centrifugation to separate aggregated (C and F) from soluble PrP (B and E). Samples were then analyzed by Western blot analysis using mAb 4H11. Lipid- samples showed lower intensity than lipid+ samples despite equal starting concentration of protein reflecting that POPG lipid vesicles stabilize PrP at 37°C. moPrP<sup>WT</sup> and moPrP<sup>RL</sup> both showed equivalent amounts of soluble (B and E) and insoluble PrP (C and F), indicating that differences in lipid induced generation of PK resistant particles are obviously not the result of differing tendencies to aggregate between the two molecules.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "biophysics", "Protein folding", "Molecular cell biology", "Infectious diseases", "Prion diseases", "Veterinary diseases", "Zoonotic diseases", "Veterinary prion diseases", "lipid", "induced", "misfolding", "differences", "aggregation"], "article_id"=>731403, "categories"=>["Physics", "Medicine", "Biological Sciences"], "users"=>["Leah M. Kyle", "Theodore R. John", "Hermann M. Schätzl", "Randolph V. Lewis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0066715.g002", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Altered_lipid_induced_misfolding_does_not_result_from_differences_in_aggregation_between_moPrP_WT_and_moPrP_RL_/731403", "title"=>"Altered lipid induced misfolding does not result from differences in aggregation between moPrP<sup>WT</sup> and moPrP<sup>RL</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-25 03:22:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/1100960"], "description"=>"<p>moPrP<sup>WT</sup> and moPrP<sup>RL</sup> at three different concentrations were incubated in the presence (E–H) or absence (A–D) of POPG lipid vesicles. Samples were removed for proteolytic digestion by proteinase K (PK) followed by ultra-centrifugation and Western blot analysis at four different time points. Generation of protease resistant, insoluble PrP was compared over time between moPrP<sup>WT</sup> and moPrP<sup>RL</sup>. In POPG vesicle containing samples, generation of material that is both insoluble and resistant to PK digestion was detectible after only five minutes (E) as a 15 kDa PrP band (denoted by large arrow). A smaller molecular weight band of approximately 14.5 kDa (denoted by small arrow) was detectible by 24 hours (F). Conversion to a PK resistant, insoluble form at a concentration of 100 µg/mL is observed for only moPrP<sup>RL</sup>, consistently at all time periods analyzed (E–H, lanes 3 <i>vs</i> 6). Over time, PK treated, ultracentrifuged samples accumulated a 24 kDa band (denoted by double arrow) (E–H). This band may represent undigested rPrP or a dimer of smaller molecular weight, PK cleaved fragments. Generation of aggregated, PK resistant material in the absence of lipids was not detected for either moPrP<sup>WT</sup> or moPrP<sup>RL</sup> (A–D). PK resistant material was also undetectable in the soluble fraction (A–H). Data shown is representative of results from four independent experiments.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "biophysics", "Protein folding", "Molecular cell biology", "Infectious diseases", "Prion diseases", "Veterinary diseases", "Zoonotic diseases", "Veterinary prion diseases", "converts", "pk", "resistant", "isoform", "concentrations"], "article_id"=>731402, "categories"=>["Physics", "Medicine", "Biological Sciences"], "users"=>["Leah M. Kyle", "Theodore R. John", "Hermann M. Schätzl", "Randolph V. Lewis"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0066715.g001", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_moPrP_RL_converts_to_a_PK_resistant_isoform_at_lower_concentrations_than_moPrP_WT_/731402", "title"=>"moPrP<sup>RL</sup> converts to a PK resistant isoform at lower concentrations than moPrP<sup>WT</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-25 03:22:13"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"4", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"2", "full-text"=>"2", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"8", "full-text"=>"9", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"4", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"6", "full-text"=>"9", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
  • {"unique-ip"=>"4", "full-text"=>"3", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"3", "full-text"=>"1", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}

Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[269, 466, 588, 697, 800, 896, 988, 1076, 1165, 1254, 1340, 1417]}, {"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[266, 468, 593, 703, 804, 903, 993, 1084, 1171, 1256, 1339, 1422, 1492]}, {"subject_area"=>"/Biology and life sciences/Veterinary science", "average_usage"=>[313, 571, 709, 825, 944, 1048, 1145, 1261, 1354, 1434, 1524, 1599, 1684]}]}
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