Infectious Prions Accumulate to High Levels in Non Proliferative C2C12 Myotubes
Publication Date
November 07, 2013
Journal
PLOS Pathogens
Authors
Allen Herbst, Pamela Banser, Camilo Duque Velasquez, Charles E. Mays, et al
Volume
9
Issue
11
Pages
e1003755
DOI
https://dx.plos.org/10.1371/journal.ppat.1003755
Publisher URL
http://journals.plos.org/plospathogens/article?id=10.1371%2Fjournal.ppat.1003755
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/24244171
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820720
Europe PMC
http://europepmc.org/abstract/MED/24244171
Web of Science
000330386900026
Scopus
84888219286
Mendeley
http://www.mendeley.com/research/infectious-prions-accumulate-high-levels-non-proliferative-c2c12-myotubes
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Mendeley | Further Information

{"title"=>"Infectious Prions Accumulate to High Levels in Non Proliferative C2C12 Myotubes", "type"=>"journal", "authors"=>[{"first_name"=>"Allen", "last_name"=>"Herbst", "scopus_author_id"=>"7005245546"}, {"first_name"=>"Pamela", "last_name"=>"Banser", "scopus_author_id"=>"57195387942"}, {"first_name"=>"Camilo Duque", "last_name"=>"Velasquez", "scopus_author_id"=>"55938540500"}, {"first_name"=>"Charles E.", "last_name"=>"Mays", "scopus_author_id"=>"23989066600"}, {"first_name"=>"Valerie L.", "last_name"=>"Sim", "scopus_author_id"=>"8946806200"}, {"first_name"=>"David", "last_name"=>"Westaway", "scopus_author_id"=>"7006295116"}, {"first_name"=>"Judd M.", "last_name"=>"Aiken", "scopus_author_id"=>"7101788870"}, {"first_name"=>"Debbie", "last_name"=>"McKenzie", "scopus_author_id"=>"7202305081"}], "year"=>2013, "source"=>"PLoS Pathogens", "identifiers"=>{"issn"=>"15537366", "scopus"=>"2-s2.0-84888219286", "sgr"=>"84888219286", "pui"=>"370341892", "isbn"=>"1553-7374 (Electronic)\r1553-7366 (Linking)", "pmid"=>"24244171", "doi"=>"10.1371/journal.ppat.1003755"}, "id"=>"d2dd4679-fd57-37dd-9c02-94e379a93372", "abstract"=>"Prion diseases are driven by the strain-specific, template-dependent transconformation of the normal cellular prion protein (PrP(C)) into a disease specific isoform PrP(Sc). Cell culture models of prion infection generally use replicating cells resulting in lower levels of prion accumulation compared to animals. Using non-replicating cells allows the accumulation of higher levels of PrP(Sc) and, thus, greater amounts of infectivity. Here, we infect non-proliferating muscle fiber myotube cultures prepared from differentiated myoblasts. We demonstrate that prion-infected myotubes generate substantial amounts of PrP(Sc) and that the level of infectivity produced in these post-mitotic cells, 10(5.5) L.D.50/mg of total protein, approaches that observed in vivo. Exposure of the myotubes to different mouse-adapted agents demonstrates strain-specific replication of infectious agents. Mouse-derived myotubes could not be infected with hamster prions suggesting that the species barrier effect is intact. We suggest that non-proliferating myotubes will be a valuable model system for generating infectious prions and for screening compounds for anti-prion activity.", "link"=>"http://www.mendeley.com/research/infectious-prions-accumulate-high-levels-non-proliferative-c2c12-myotubes", "reader_count"=>21, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>6, "Student > Postgraduate"=>2, "Student > Master"=>2, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>6, "Student > Postgraduate"=>2, "Student > Master"=>2, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>11, "Neuroscience"=>2, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Neuroscience"=>{"Neuroscience"=>2}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>11}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Unspecified"=>{"Unspecified"=>2}}, "reader_count_by_country"=>{"Italy"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1271570"], "description"=>"<p>Gene expression profiling was performed from 3 replicate samples of uninfected and infected C2C12 myotube preparations. (A) Confirmation of PrP<sup>Sc</sup> in cells used for gene expression profiling by immunoblotting with 3F10. Cell lysates were digested with 50 ug/mL of proteinase K (PK50) and 10 µg of protein was loaded in each lane. (B) Gene expression of infected vs. un-infected control cell cultures (N = 3). A scatter plot was created comparing the expression of genes in uninfected cells with that of infected cells. Each data point plotted is the average normalized signal intensity for each gene's expression (uninfected or infected). Data points outside the green lines have greater than 2-fold changes in gene expression. Transcription was globally unchanged in C2C12 cells replicating PrP<sup>Sc</sup>.</p>", "links"=>[], "tags"=>["transcriptional", "c2c12"], "article_id"=>844032, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g004", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_RML_infection_does_not_affect_transcriptional_profile_of_C2C12_myotubes_/844032", "title"=>"RML infection does not affect transcriptional profile of C2C12 myotubes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271568"], "description"=>"<p>(A) Time course of PrP<sup>Sc</sup> accumulation. Confluent myotubes were infected by incubation of cells in media spiked with 100 µL of 1% RML brain homogenate or mock infected with normal brain homogenate overnight. Media was changed daily. After 5, 10 or 15 days in culture, cells were lysed and analyzed for PK-resistant PrP. (B) Myoblasts were infected by incubating in media spiked with 100 µL of 1% RML brain homogenate or normal brain homogenate. Cells were analyzed after passages 7, 8 and 9 which correspond to myotube days 11, 13 and 15 respectively and no PrP<sup>Sc</sup> was observed. For both panels (A,B), 7.5 µg of protein was loaded in PK- lanes. 15 µg of protein equivalent was loaded in lanes treated with PK. 10 µl of 0.15% BH was loaded ∼11.25 µg protein. Anti-PrP antibody SAF 83 was used.</p>", "links"=>[], "tags"=>["replicates"], "article_id"=>844030, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g002", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PrP_Sc_replicates_in_myotubes_/844030", "title"=>"PrP<sup>Sc</sup> replicates in myotubes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271574"], "description"=>"<p>(A) Brain homogenates (BH) from mice clinically affected with prion disease. 10 ul of 1% BH treated with or without 50 µg/ml PK was loaded in each lane. 22L and ME7 prions were generated in tga20 mice. RML prions were from C57Bl/6 mice. PrP<sup>Sc</sup> was detected with 3F10 antibody. (B) C2C12 cells were infected with brain homogenates from 22L, ME7 and RML. At 4, 8 and 14 days post exposure, cells were lysed, lysates treated with 50 ug/mL of proteinase K and immunoblotted to detect the presence of PrP<sup>Sc</sup>. 30 µg of protein equivalent was loaded into each lane for 22L and ME7 samples. 10 µl of 0.1% BH was loaded as a control. 10 µg of protein equivalent from RML infected myotubes was loaded.</p>", "links"=>[], "tags"=>["myotubes", "susceptible", "22l", "me7"], "article_id"=>844035, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g007", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_C2C12_myotubes_are_also_susceptible_to_22L_and_ME7_prions_/844035", "title"=>"C2C12 myotubes are also susceptible to 22L and ME7 prions.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271573"], "description"=>"<p>C2C12 cells were infected with 100 µL of 10% brain homogenates. Two days post infection, pentosan polysulfate (PPS) (1 µg/ml final concentration) was added to the media. PPS was kept on the cells until harvested at the designated dates. Antibody SAF 83 was used for western blot detection.</p>", "links"=>[], "tags"=>["polysulfate", "inhibits", "accumulation", "c2c12"], "article_id"=>844034, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g006", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Pentosan_polysulfate_inhibits_PrP_Sc_accumulation_in_C2C12_myotubes_/844034", "title"=>"Pentosan polysulfate inhibits PrP<sup>Sc</sup> accumulation in C2C12 myotubes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271567"], "description"=>"<p>(A) Morphology of C2C12 myoblasts and myotubes (B) Western blot comparison of PrP<sup>C</sup> expression from mouse brain homogenate, C2C12 myoblasts and myotubes and N2a neuroblastoma cells. Relative loads are based on protein concentration of the brain homogenate (1.78 µg, 0.68 µg protein) and cell lysates (3.4 µg C2C12 myoblasts, myotubes and N2a). Anti-PrP antibody SAF 83 was used.</p>", "links"=>[], "tags"=>["c2c12", "myoblasts"], "article_id"=>844029, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g001", "stats"=>{"downloads"=>3, "page_views"=>31, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_PrP_c_in_C2C12_myoblasts_and_myotubes_/844029", "title"=>"Expression of PrP<sup>c</sup> in C2C12 myoblasts and myotubes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271576", "https://ndownloader.figshare.com/files/1271577", "https://ndownloader.figshare.com/files/1271578"], "description"=>"<div><p>Prion diseases are driven by the strain-specific, template-dependent transconformation of the normal cellular prion protein (PrP<sup>C</sup>) into a disease specific isoform PrP<sup>Sc</sup>. Cell culture models of prion infection generally use replicating cells resulting in lower levels of prion accumulation compared to animals. Using non-replicating cells allows the accumulation of higher levels of PrP<sup>Sc</sup> and, thus, greater amounts of infectivity. Here, we infect non-proliferating muscle fiber myotube cultures prepared from differentiated myoblasts. We demonstrate that prion-infected myotubes generate substantial amounts of PrP<sup>Sc</sup> and that the level of infectivity produced in these post-mitotic cells, 10<sup>5.5</sup> L.D.<sub>50</sub>/mg of total protein, approaches that observed <i>in vivo</i>. Exposure of the myotubes to different mouse-adapted agents demonstrates strain-specific replication of infectious agents. Mouse-derived myotubes could not be infected with hamster prions suggesting that the species barrier effect is intact. We suggest that non-proliferating myotubes will be a valuable model system for generating infectious prions and for screening compounds for anti-prion activity.</p></div>", "links"=>[], "tags"=>["prions", "accumulate", "non", "proliferative", "c2c12"], "article_id"=>844037, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1003755.s001", "https://dx.doi.org/10.1371/journal.ppat.1003755.s002", "https://dx.doi.org/10.1371/journal.ppat.1003755.s003"], "stats"=>{"downloads"=>5, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Infectious_Prions_Accumulate_to_High_Levels_in_Non_Proliferative_C2C12_Myotubes_/844037", "title"=>"Infectious Prions Accumulate to High Levels in Non Proliferative C2C12 Myotubes", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271575"], "description"=>"<p>15 µg of protein was loaded in each lane. RML and HY brain homogenates were 15 µl of 0.1% (A) C2C12 myotubes infected with RML accumulate PrP<sup>Sc</sup> as detected by the SAF83 monoclonal antibody. SAF 83 recognizes mouse and hamster PrP. (B, C) C2C12 myotubes infected with hamster HY prions probed with SAF83 (B) and 3F4 (C) antibodies. 3F4 recognizes hamster PrP but not mouse, including some HY that persists in culture until day five. SAF83 also recognizes mouse prions, but no signal is detected at day 5. This is likely due to the higher affinity of 3F4 vs. the SAF83 antibody.</p>", "links"=>[], "tags"=>["myotubes", "replicate", "rml", "hamster", "hy"], "article_id"=>844036, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g008", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_C2C12_myotubes_replicate_mouse_RML_prions_but_not_hamster_HY_prions_/844036", "title"=>"C2C12 myotubes replicate mouse RML prions, but not hamster HY prions.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271572"], "description"=>"<p>(A) Time dependent increase in PrP<sup>Sc</sup> in C2C12 cells. 10 µg of protein (PK−) or protein equivalent (PK+) was loaded in each lane. (B) Relative abundance of PrP<sup>Sc</sup> in clinically affected mouse brain homogenate and lysates from cell lines (C2C12 myotubes, N2a neuroblastoma cells and SMB scrapie mouse brain cells). All samples are treated with PK (50 µg/mL, final concentration). Relative loading is equivalent to protein amounts prior to proteinase K digestion 0.75 µg, 7.5 µg and 75 µg respectively. Antibody SAF 83 was used.</p>", "links"=>[], "tags"=>["c2c12", "n2a", "neuroblastoma", "cells", "smb", "scrapie"], "article_id"=>844033, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g005", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Accumulation_of_PrP_Sc_in_C2C12_myotubes_N2a_neuroblastoma_cells_and_SMB_scrapie_mouse_brain_cells_/844033", "title"=>"Accumulation of PrP<sup>Sc</sup> in C2C12 myotubes, N2a neuroblastoma cells and SMB scrapie mouse brain cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1271569"], "description"=>"<p>(A) C2C12 myotubes infected with RML were collected at 4 or 15 days post infection by scraping in PBS, centrifuging and resuspending in 500 µL of water. 30 µL of this cell material was inoculated intracranially into weanling C57Bl/6 mice. A statistically significant difference in incubation period was observed between 4 and 15 days indicative of prion replication p<0.05. Parallel inoculation of serial 10-fold dilutions of RML brain homogenates were performed. (B) Plot of infectivity in each inocula standardized per gram of protein inoculated. C2C12 myotubes infected with RML were collected at 4, 6, 8, 10, 13 and 15 days post-infection as in (A) and bioassayed. Infectivity of the C2C12 derived samples was calculated by comparing the observed incubation periods from each sample with those from brain homogenate dilutions and normalizing the data to protein content. Prion infectivity increases in C2C12 myotube cultures from day 4 to day 15 post-infection.</p>", "links"=>[], "tags"=>["myotubes", "replicate", "prions"], "article_id"=>844031, "categories"=>["Biological Sciences"], "users"=>["Allen Herbst", "Pamela Banser", "Camilo Duque Velasquez", "Charles E. Mays", "Valerie L. Sim", "David Westaway", "Judd M. Aiken", "Debbie McKenzie"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003755.g003", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_C2C12_myotubes_replicate_prions_to_high_levels_of_infectivity_/844031", "title"=>"C2C12 myotubes replicate prions to high levels of infectivity.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-11-07 03:17:47"}

PMC Usage Stats | Further Information

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Relative Metric

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