Secretion of Hepatitis C Virus Envelope Glycoproteins Depends on Assembly of Apolipoprotein B Positive Lipoproteins
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{"title"=>"Secretion of hepatitis C virus envelope glycoproteins depends on assembly of apolipoprotein B positive lipoproteins", "type"=>"journal", "authors"=>[{"first_name"=>"Vinca", "last_name"=>"Icard", "scopus_author_id"=>"22034647100"}, {"first_name"=>"Olivier", "last_name"=>"Diaz", "scopus_author_id"=>"7005674018"}, {"first_name"=>"Caroline", "last_name"=>"Scholtes", "scopus_author_id"=>"25632897600"}, {"first_name"=>"Laure", "last_name"=>"Perrin-Cocon", "scopus_author_id"=>"7801521840"}, {"first_name"=>"Cristophe", "last_name"=>"Ramière", "scopus_author_id"=>"25632886300"}, {"first_name"=>"Ralf", "last_name"=>"Bartenschlager", "scopus_author_id"=>"7007011273"}, {"first_name"=>"Francois", "last_name"=>"Penin", "scopus_author_id"=>"7007075375"}, {"first_name"=>"Vincent", "last_name"=>"Lotteau", "scopus_author_id"=>"7003343824"}, {"first_name"=>"Patrice", "last_name"=>"André", "scopus_author_id"=>"7202964602"}], "year"=>2009, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"58849091856", "doi"=>"10.1371/journal.pone.0004233", "issn"=>"19326203", "pui"=>"354109734", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "pmid"=>"19156195", "scopus"=>"2-s2.0-58849091856"}, "id"=>"6493a74c-1e14-36f3-aea4-01e540959c56", "abstract"=>"The density of circulating hepatitis C virus (HCV) particles in the blood of chronically infected patients is very heterogeneous. The very low density of some particles has been attributed to an association of the virus with apolipoprotein B (apoB) positive and triglyceride rich lipoproteins (TRL) likely resulting in hybrid lipoproteins known as lipo-viro-particles (LVP) containing the viral envelope glycoproteins E1 and E2, capsid and viral RNA. The specific infectivity of these particles has been shown to be higher than the infectivity of particles of higher density. The nature of the association of HCV particles with lipoproteins remains elusive and the role of apolipoproteins in the synthesis and assembly of the viral particles is unknown. The human intestinal Caco-2 cell line differentiates in vitro into polarized and apoB secreting cells during asymmetric culture on porous filters. By using this cell culture system, cells stably expressing E1 and E2 secreted the glycoproteins into the basal culture medium after one week of differentiation concomitantly with TRL secretion. Secreted glycoproteins were only detected in apoB containing density fractions. The E1-E2 and apoB containing particles were unique complexes bearing the envelope glycoproteins at their surface since apoB could be co-immunoprecipitated with E2-specific antibodies. Envelope protein secretion was reduced by inhibiting the lipidation of apoB with an inhibitor of the microsomal triglyceride transfer protein. HCV glycoproteins were similarly secreted in association with TRL from the human liver cell line HepG2 but not by Huh-7 and Huh-7.5 hepatoma cells that proved deficient for lipoprotein assembly. These data indicate that HCV envelope glycoproteins have the intrinsic capacity to utilize apoB synthesis and lipoprotein assembly machinery even in the absence of the other HCV proteins. A model for LVP assembly is proposed.", "link"=>"http://www.mendeley.com/research/secretion-hepatitis-c-virus-envelope-glycoproteins-depends-assembly-apolipoprotein-b-positive-lipopr", "reader_count"=>55, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>4, "Student > Doctoral Student"=>4, "Researcher"=>13, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>1, "Student > Master"=>8, "Other"=>1, "Student > Bachelor"=>8, "Lecturer"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>4, "Student > Doctoral Student"=>4, "Researcher"=>13, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>1, "Student > Master"=>8, "Other"=>1, "Student > Bachelor"=>8, "Lecturer"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>3, "Engineering"=>2, "Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>29, "Medicine and Dentistry"=>9, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Chemistry"=>1, "Immunology and Microbiology"=>3}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>2}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>9}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>29}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Unspecified"=>{"Unspecified"=>3}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}}, "reader_count_by_country"=>{"Iran"=>1, "United States"=>1, "France"=>1}, "group_count"=>2}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/910003"], "description"=>"<p>Caco-2 cells maintained under standard culture conditions after transduction with the E1E2-HIV-SIN lentiviral vector express E1 and E2 proteins. (A) Western blot analysis showing E1 and E2 revealed as single bands by anti-E1 antibody, (lane 2), and anti-E2 antibody (lane 4), at their expected molecular weight in transduced cells, but not in control cells (lanes 1 and 3, respectively). (B) Expression of envelope glycoprotein remains stable. Staining of transduced cells with anti-E2 antibody (in red) shows that almost all cells still expressed the envelope protein after at least 40 passages.</p>", "links"=>[], "tags"=>["hcv", "glycoproteins", "e1", "e2", "caco-2"], "article_id"=>580450, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g001", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_the_HCV_glycoproteins_E1_and_E2_in_Caco_2_cells_/580450", "title"=>"Expression of the HCV glycoproteins E1 and E2 in Caco-2 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/910527"], "description"=>"<p>Cells were cultured as in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#pone-0004233-g004\" target=\"_blank\">Figure 4</a>. Basal medium was collected at day 13 after two day incubation in serum free medium. Density of apoB and E1E2 glycoprotein positive fractions in the E1E2-Caco-2 basal medium. Basal medium was run on a iodixanol gradient and fractions were analysed by apoB Elisa (A) and western blotting (B, upper panel) stained with envelope specific H52 and A4 antibodies. E1 and E2 proteins were present in apoB positive fractions with the higher density leaving the upper apoB fractions free of envelope glycoproteins. E1 was only detected in the fractions with the highest density. Intracellular E1 and E2 control proteins were deposited in the last right lane (+). To further assess the specificity of the antibody, fractions obtained from E1E2-Caco-2 and control Caco-2 grown in the same conditions were normalized for apoB concentrations and ran in parallel in one western blot (B, lower panel). Envelope glycoproteins were only detected in fractions obtained from E1E2-Caco-2. (C) Immuno-precipitation of E2 positive particles. Basal culture medium of control Caco-2 and E1E2-Caco-2 cells were collected at day 13 of differentiation after two days of culture in serum free medium. E2 positive particles were captured by E2-specific H48 monoclonal antibody and immuno-precipitated particles were analysed by western blotting and stained with anti-E2 H52 (upper panel), anti-E1 A4 (middle panel) and anti-apoB (lower panel) antibodies as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#s4\" target=\"_blank\">materials and methods</a> section. Molecular weights are indicated on the left, control proteins were deposited in the + lane. Identical volume of precipitated material either from E1E2-Caco-2 or control Caco-2 basal medium were deposited in lanes “E1E2” and “control” respectively for every western blot.</p>", "links"=>[], "tags"=>["apob", "containing", "particles", "secreted", "caco-2", "basal"], "article_id"=>580973, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g005", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Characterization_of_the_apoB_and_envelope_containing_particles_secreted_into_Caco_2_basal_medium_/580973", "title"=>"Characterization of the apoB and envelope containing particles secreted into Caco-2 basal medium.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:05:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/910238"], "description"=>"<p>(A) Analysis of HCV glycoprotein expression by E1E2-Hela by immunofluorescence with E2-specific antibody H52. Cells were grown under standard conditions and stained as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#s4\" target=\"_blank\">materials and methods</a>. Left panel, control cells, right panel, E1E2-Hela. E2 positive cells are stained in red. (B) Caco-2 and E1E2-Caco-2 cells were cultured under differentiating conditions for 11 days followed by 2 days in FCS free medium before baso-lateral medium and cells were collected. Hela and E1E2-Hela cells were cultured in standard conditions until 80% confluence and then kept for two days in FCS free medium before cells and supernatants were collected. Cellular and medium samples for western blotting were adjusted for the total cellular protein contents. HCV glycoproteins were detected in both E1E2-Caco-2 and E1E2-Hela cell and not in control cells (left panel) but the two glycoproteins were only secreted by E1E2-Caco-2 and not by E1E2-Hela and control cells (right panel).</p>", "links"=>[], "tags"=>["hela", "cells", "secrete", "hcv"], "article_id"=>580686, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g003", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Epithelial_Hela_cells_do_not_secrete_HCV_glycoproteins_/580686", "title"=>"Epithelial Hela cells do not secrete HCV glycoproteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:03:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/910375"], "description"=>"<p>E1E2-Caco-2 cells were grown on porous filters under asymmetric medium conditions for 11 days. Upper and lower culture medium were then changed and replaced with foetal calf serum free medium. Cells were incubated for two additional days. Basal medium was collected and run on an iodixanol gradient. (A) Density fractions were collected and apoB concentrations per mL of basal medium were determined by ELISA and expressed in ng/ml. ApoB was only present in fractions with density ≤1.05 g/mL. (B) Density fractions were analysed by western blotting using specific antibodies against apoB, apoE and E2 glycoprotein. ApoB positive fractions contained the two apoB isoforms, apoB100 and apoB48. ApoE and E2 were only detected in the apoB positive fractions. Control proteins were deposited in lane +.</p>", "links"=>[], "tags"=>["apolipoproteins", "hcv", "glycoproteins", "secreted", "caco-2", "basal"], "article_id"=>580824, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g004", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Density_and_nature_of_apolipoproteins_and_HCV_glycoproteins_secreted_into_Caco_2_basal_medium_/580824", "title"=>"Density and nature of apolipoproteins and HCV glycoproteins secreted into Caco-2 basal medium.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:04:23"}
  • {"files"=>["https://ndownloader.figshare.com/files/910116"], "description"=>"<p>(A) Caco-2 cells were grown on porous filters under asymmetric medium conditions as depicted for two weeks after seeding. Media in upper and lower chambers were changed every two days. Under these differentiation conditions, basolateral lipoprotein secretion begins after one week of culture <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#pone.0004233-Chateau1\" target=\"_blank\">[32]</a>. (B) ApoB secreted by control and E1E2 transduced cells into the basal medium was measured by ELISA. Values indicate apoB (ng) secreted by one thousand cells for two days per mL of culture medium. Vertical bars indicate standard deviations. The kinetic is representative of three separate experiments. (C) Expression and secretion of E2 protein by E1E2-Caco-2 cells during differentiation. Content of E2 protein in 40 µl of basal medium, upper pannel, and, in cell lysate, lower panel, (per 20 µg total protein), was analysed every two days by Western blotting with the E2-specific H52 antibody. As indicated in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#pone-0004233-g001\" target=\"_blank\">Figure 1</a>, E2 was detectable in seeded cells and remained present during the two weeks of culture. Its expression increased during the early phase of the differentiation until day 9 when a plateau was reached. E2 secretion into the basal medium began at day 7, concomitantly with apoB secretion. Secreted E2 appeared to have a higher molecular weight than the control intracellular E2 protein likely because of a higher glycosylated state.</p>", "links"=>[], "tags"=>["apob", "hcv", "glycoprotein", "secretion", "caco-2"], "article_id"=>580564, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Kinetic_of_ApoB_and_HCV_glycoprotein_secretion_during_Caco_2_cell_differentiation_/580564", "title"=>"Kinetic of ApoB and HCV glycoprotein secretion during Caco-2 cell differentiation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:02:51"}
  • {"files"=>["https://ndownloader.figshare.com/files/910926"], "description"=>"<p>E1E2-Caco-2 cells were cultured under differentiating condition for 11 days when medium was replaced by FCS free medium with the MTP inhibitor Cp 346084 at 0, 1 or 10 nM. MTP activity was measured on frozen lysates and expressed as described in the <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#s4\" target=\"_blank\">Materials and Methods</a> section. (A) MTP activity in lysate of E1E2-Caco-2, 24 and 48 h after addition of Cp 346084. MTP activity was not completely abrogated by the addition of the inhibitor since its activity continued to increase during the inhibition period. However, there was a dose dependant inhibition of MTP activity by 1 and 10 nM Cp 346084. (B) Concentrations of secreted ApoB in the basal medium were measured by ELISA at 24 and 48 h after addition of 1 or 10 nM Cp 346084. ApoB secretion was inhibited in a dose dependant manner by the MTP inhibitor. (C) Secretion of HCV glycoprotein E1 and E2 in the basal medium was monitored by western-blotting with the E1-specific A4 and E2-specific H52 antibodies at 24 and 48 h after addition of 1 or 10 nM Cp 346084. Control cellular E2 protein was deposited in lanes (+). Amount of secreted E1 and E2 was quantified by densitometry as per cent of secreted glycoprotein in absence of inhibitor (upper panels). Cellular glycoprotein expression was monitored by western-blotting of cell lysates and was not modified by MTP inhibition (lower panel).</p>", "links"=>[], "tags"=>["inhibition", "decreases", "hcv", "glycoprotein", "secretion"], "article_id"=>581374, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g008", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MTP_activity_inhibition_decreases_HCV_envelope_glycoprotein_secretion_by_E1E2_Caco_2_/581374", "title"=>"MTP activity inhibition decreases HCV envelope glycoprotein secretion by E1E2-Caco-2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:07:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/910781"], "description"=>"<p>(A) Analysis of HCV glycoprotein expression by immunofluorescence with E2-specific antibody. Huh-7.5 were grown under standard conditions and stained as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#s4\" target=\"_blank\">materials and methods</a>. Left panel, control cells, right panel, E1E2 transduced Huh-7. E2 positive cells are stained in red. (B) Density of apoB and E1E2 positive fractions in the E1E2-Huh-7.5 supernatant. Three day culture supernatant was run on a iodixanol gradient and fractions were analysed by apoB ELISA, upper panel, and western blotting with E1 and E2-specific antibodies, lower panel. Envelope control proteins were deposited in the last right lane (+). E1 and E2 proteins were only present in apoB positive fractions. (C) Immuno-precipitation of E2 positive particles was performed as in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#pone-0004233-g005\" target=\"_blank\">figure 5</a> with Huh-7.5 supernatant collected three days after seeding. Basal culture medium of control and E1E2-Huh-7.5 were collected after two days of culture in serum free medium. E2 positive particles were captured by E2-specific H48 monoclonal antibody and immuno-precipitated particles were analysed by western blotting and stained with H52 anti-E2 (upper panel), A4 anti-E1 (middle panel) and anti-apoB (lower panel) antibodies. Molecular weight are indicated on the left, control proteins were deposited in the + lane.</p>", "links"=>[], "tags"=>["particles", "secreted"], "article_id"=>581238, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g007", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Characterization_of_particles_secreted_by_Huh_7_5_cells_/581238", "title"=>"Characterization of particles secreted by Huh-7.5 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:06:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/911112"], "description"=>"<p>E1E2-HepG2 and E1E2-Huh-7.5 cells were cultured in standard conditions until 80% confluence when medium was replaced by FCS free medium with 0, 1 or 10 nM of MTP inhibitor Cp 346084 for two days. MTP activity was measured on frozen lysates and expressed as described in the <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#s4\" target=\"_blank\">Materials and Methods</a> section. (A) E1E2-HepG2 and (B) E1E2-Huh-7.5. Upper panels, MTP activity in cells and apoB concentrations in medium in presence of the indicated inhibitor concentrations. Middle panels, quantification of secreted glycoproteins in presence of 1 and 10 nM MTP inhibitor by western blotting and densitometry as per cent of secreted glycoproteins in absence of inhibitor. Lower panels, cellular glycoprotein expression was not modified by the MTP inhibitor as shown by western-blotting of cell lysates.</p>", "links"=>[], "tags"=>["inhibition", "decreases", "hcv", "glycoprotein", "secretion", "e1e2-hepg2"], "article_id"=>581560, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g009", "stats"=>{"downloads"=>1, "page_views"=>20, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MTP_activity_inhibition_decreases_HCV_envelope_glycoprotein_secretion_by_E1E2_HepG2_and_E1E2_Huh_7_5_/581560", "title"=>"MTP activity inhibition decreases HCV envelope glycoprotein secretion by E1E2-HepG2 and E1E2-Huh-7.5.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:08:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/911310"], "description"=>"<p>During its translation at the rough ER, the nascent apoB peptide is translocated within the ER lumen (step 1) where a lipid cavity is formed. This lipid cavity is closed by MTP allowing the recruitment of a small amount of phospholipids and triglycerides (TG) (step 2). Continued apoB translation and MTP-mediated TG transfer form a neutral lipid core and conversion to a spheric particle (step 3) that is then released into the ER lumen after translation completion. This first precursor then moves to a distal compartment of the secretory pathway (step 4). In the smooth ER, a second precursor is formed from the ER membrane and MTP-mediated TG enrichment (step 5) and then traffics to the secretory pathway (step 6) where the two precursors meet and fuse to form mature TRL (fusion step). Several factors are required for the formation of the second precursor and the fusion between the two precursors (see text). HCV envelope glycoproteins are retained in the ER membrane after their maturation and clivages by ER peptidases. We hypothesise that E1E2 dimers might diffuse from the ER membrane constituted of two phospholipid monolayers to the budding second precursor. Transition from a two leaflets membrane to the phospholipid monolayer membrane of the precursor might induce conformation changes favouring the formation of E1E2 trimers triggered by the trimerisation of E1 as recently proposed <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#pone.0004233-Bartosch1\" target=\"_blank\">[34]</a>. The glycoprotein loaded second precursor can then fuse with the first precursor leading to hybrid TRL as observed in Caco-2 and HepG2 but not in Huh-7 cells (see text).</p>", "links"=>[], "tags"=>["trl", "hcv", "glycoprotein", "hybrid", "shelness"], "article_id"=>581755, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g010", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_of_TRL_assembly_and_formation_of_HCV_envelope_glycoprotein_hybrid_TRL_adapted_from_Shelness_41_/581755", "title"=>"Model of TRL assembly and formation of HCV envelope glycoprotein hybrid TRL (adapted from Shelness [41]).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:09:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/910670"], "description"=>"<p>(A) Analysis of HCV glycoprotein expression by immunofluorescence with E2-specific antibody H52. HepG2 cells were grown under standard conditions and stained as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#s4\" target=\"_blank\">materials and methods</a>. Left panel, control cells, right panel, E1E2 transduced HepG2 cells. E2 positive cells are stained in red. (B) Density of apoB and E1E2 positive fractions in the E1E2-HepG2 supernatant. Three day culture supernatant was run on an iodixanol gradient and fractions were analysed by apoB ELISA, upper panel, and western blotting with E2-specific antibody, lower panel. Envelope control proteins were deposited in the last right lane (+). E2 proteins were only present in apoB positive fractions. (C) Immuno-precipitation of E2 positive particles was performed as in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0004233#pone-0004233-g005\" target=\"_blank\">figure 5</a> with HepG2 supernatant collected three days after seeding. Basal culture medium of control and E1E2-HepG2 were collected after two days of culture in serum free medium. E2 positive particles were captured by E2-specific H48 monoclonal antibody and immuno-precipitated particles were analysed by western blotting and stained with E2-specific H52 antibody (upper panel), E1-specific A4 antibody (middle panel) and apoB-specific antibody (lower panel). Molecular weight are indicated on the left, control proteins were deposited in the + lane.</p>", "links"=>[], "tags"=>["particles", "secreted"], "article_id"=>581118, "categories"=>["Infectious Diseases", "Virology"], "users"=>["Vinca Icard", "Olivier Diaz", "Caroline Scholtes", "Laure Perrin-Cocon", "Christophe Ramière", "Ralf Bartenschlager", "François Penin", "Vincent Lotteau", "Patrice André"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0004233.g006", "stats"=>{"downloads"=>2, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Characterization_of_particles_secreted_by_HepG2_/581118", "title"=>"Characterization of particles secreted by HepG2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 07:06:05"}

PMC Usage Stats | Further Information

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Relative Metric

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