Respiratory Syncytial Virus Fusion Glycoprotein Expressed in Insect Cells Form Protein Nanoparticles That Induce Protective Immunity in Cotton Rats
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{"title"=>"Respiratory Syncytial Virus Fusion Glycoprotein Expressed in Insect Cells Form Protein Nanoparticles That Induce Protective Immunity in Cotton Rats", "type"=>"journal", "authors"=>[{"first_name"=>"Gale", "last_name"=>"Smith", "scopus_author_id"=>"7406735656"}, {"first_name"=>"Rama", "last_name"=>"Raghunandan", "scopus_author_id"=>"24462262700"}, {"first_name"=>"Yingyun", "last_name"=>"Wu", "scopus_author_id"=>"55513203000"}, {"first_name"=>"Ye", "last_name"=>"Liu", "scopus_author_id"=>"21742964300"}, {"first_name"=>"Michael", "last_name"=>"Massare", "scopus_author_id"=>"6503883195"}, {"first_name"=>"Margret", "last_name"=>"Nathan", "scopus_author_id"=>"35074618100"}, {"first_name"=>"Bin", "last_name"=>"Zhou", "scopus_author_id"=>"57141323500"}, {"first_name"=>"Hanxin", "last_name"=>"Lu", "scopus_author_id"=>"55503534700"}, {"first_name"=>"Sarathi", "last_name"=>"Boddapati", "scopus_author_id"=>"8836963300"}, {"first_name"=>"Jingning", "last_name"=>"Li", "scopus_author_id"=>"36813683800"}, {"first_name"=>"David", "last_name"=>"Flyer", "scopus_author_id"=>"6701754894"}, {"first_name"=>"Gregory", "last_name"=>"Glenn", "scopus_author_id"=>"36660336200"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"84870659737", "doi"=>"10.1371/journal.pone.0050852", "issn"=>"19326203", "pui"=>"366215625", "isbn"=>"1932-6203 (Electronic) 1932-6203 (Linking)", "pmid"=>"23226404", "scopus"=>"2-s2.0-84870659737"}, "id"=>"46b8de45-d3aa-3653-8c6a-2fca4c0233a1", "abstract"=>"Respiratory Syncytial Virus (RSV) is an important viral agent causing severe respiratory tract disease in infants and children as well as in the elderly and immunocompromised individuals. The lack of a safe and effective RSV vaccine represents a major unmet medical need. RSV fusion (F) surface glycoprotein was modified and cloned into a baculovirus vector for efficient expression in Sf9 insect cells. Recombinant RSV F was glycosylated and cleaved into covalently linked F2 and F1 polypeptides that formed homotrimers. RSV F extracted and purified from insect cell membranes assembled into 40 nm protein nanoparticles composed of multiple RSV F oligomers arranged in the form of rosettes. The immunogenicity and protective efficacy of purified RSV F nanoparticles was compared to live and formalin inactivated RSV in cotton rats. Immunized animals induced neutralizing serum antibodies, inhibited virus replication in the lungs, and had no signs of disease enhancement in the respiratory track of challenged animals. RSV F nanoparticles also induced IgG competitive for binding of palivizumab neutralizing monoclonal antibody to RSV F antigenic site II. Antibodies to this epitope are known to protect against RSV when passively administered in high risk infants. Together these data provide a rational for continued development a recombinant RSV F nanoparticle vaccine candidate.", "link"=>"http://www.mendeley.com/research/respiratory-syncytial-virus-fusion-glycoprotein-expressed-insect-cells-form-protein-nanoparticles-in-3", "reader_count"=>62, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>3, "Researcher"=>14, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>18, "Student > Postgraduate"=>2, "Student > Master"=>9, "Other"=>3, "Student > Bachelor"=>7, "Lecturer > Senior Lecturer"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>3, "Researcher"=>14, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>18, "Student > Postgraduate"=>2, "Student > Master"=>9, "Other"=>3, "Student > Bachelor"=>7, "Lecturer > Senior Lecturer"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>4, "Environmental Science"=>1, "Biochemistry, Genetics and Molecular Biology"=>6, "Agricultural and Biological Sciences"=>29, "Medicine and Dentistry"=>12, "Business, Management and Accounting"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>3, "Chemical Engineering"=>2, "Chemistry"=>1, "Immunology and Microbiology"=>3}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>12}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>29}, "Business, Management and Accounting"=>{"Business, Management and Accounting"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}, "Unspecified"=>{"Unspecified"=>4}, "Environmental Science"=>{"Environmental Science"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>3}, "Chemical Engineering"=>{"Chemical Engineering"=>2}}, "reader_count_by_country"=>{"United States"=>1, "United Kingdom"=>1, "France"=>1}, "group_count"=>3}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/533478"], "description"=>"<p>Cotton rats were immunized on day 0 and 21 and challenged intranasally with 1×10<sup>6</sup> pfu RSV A Long strain virus on day 49. Lung tissues harvested 5 days post challenge were fixed in 10% buffered formalin, paraffin embedded, sectioned and stained with hematoxylin and eosin. A: PBS vaccine-no RSV challenge; B: PBS vaccine-RSV challenge; C: FI-RSV vaccine - RSV challenge; D: 1 µg RSV-F vaccine with alum - RSV challenge; E: 6 µg RSV-F vaccine with alum - RSV challenge; F: 30 µg RSV-F vaccine with alum - RSV challenge.</p>", "links"=>[], "tags"=>["Virology", "immunology"], "article_id"=>203968, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.g006", "stats"=>{"downloads"=>3, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cotton_rat_lung_histopathology_/203968", "title"=>"Cotton rat lung histopathology.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-19 19:26:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/533627"], "description"=>"<p>Lung histopathology scores from cotton rats immunized with the indicated dose of RSV F (RSV-F) nanoparticles without or with aluminum phosphate adjuvant (RSV-F+alum), live RSV then challenged (RSV+Chal), PBS then challenged (PBS+Chal), or PBS alone. Cotton rats (n = 7 or 8 per group) were immunized on day 0 and day 21 and challenged with RSV virus on day 49. Lung tissues were harvested on day 54 and subjected to histopathology and blinded samples scored for severity on a scale of 0 to 4. Total and mean of all measures per animal for bronchiolitis, perivasculitis, bronchitis, alveolitis and pneumonitis are given.</p>", "links"=>[], "tags"=>["histopathology"], "article_id"=>204117, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.t001", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Lung_Histopathology_Cotton_Rats_/204117", "title"=>"Lung Histopathology Cotton Rats.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-19 19:27:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/532734"], "description"=>"<p>(A) RSV F cleavage site mutation where introduced at the proteolytic furin cleavage site II (KKRKRR) and site I (RARR) of wild type RSV F gene (wt). (B) RSV F clone 2 (#514) with a mutation of cleavage site II was further modified with increasing deletions in the fusion peptide starting at Phe137 to Val154 with Δ2, Δ4, Δ6, Δ8, Δ10, Δ12, Δ14, Δ16 and Δ18 amino acid deletions. (C) The modified full length RSV F gene (#683) with a modified cleavage site II (KKQKQQ) and Phe137 - Ser146 fusion domain deletion including RSV F cleavable signal peptide (sp), 27 amino acid peptide <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050852#pone.0050852-RuizArguello1\" target=\"_blank\">[23]</a>, hydrophobic transmembrane (tm), and F2 and F1 polypeptides covalently linked by two disulfides.</p>", "links"=>[], "tags"=>["a2"], "article_id"=>203211, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.g001", "stats"=>{"downloads"=>1, "page_views"=>25, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_RSV_A2_F_gene_modifications_/203211", "title"=>"RSV A2 F gene modifications.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-19 19:22:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/533253"], "description"=>"<p>Cotton rats (n = 8 per group) were immunized on day 0 and 21 with FI-RSV, PBS or the indicated doses of RSV F nanoparticle vaccine in the presence or absence of aluminum phosphate (alum). Negative control animals were immunized with PBS and not challenged (PBS). Positive controls were immunized with PBS then challenged with 1×10<sup>6</sup> pfu RSV (PBS+Chal) or received a single intranasal challenge with 1×10<sup>6</sup> pfu RSV on day 0 then challenged with RSV (RSV+Chal). Blood was drawn on day 49 from all animals for immunological analysis. (A) Day 21 serum anti-RSV F IgG ELISA titers against the purified recombinant RSV F nanoparticle. Titers are expressed as log2 and the geometric mean titer in each group marked with a bar. (B) RSV serum neutralizing antibody titers against RSV A2 providing 100% inhibition of CPE expressed as log2 and the geometric mean titer in each group marked with a bar. (C) Viral lung titers were determined 5 days post-challenge with RSV from homogenized lung tissue by plaque assay in HEp2 cells. Values represent RSV plaque forming units/gram lung tissue expressed as log2 pfu/g of lung tissue with the geometric mean titer in each group marked with a bar (D) palivizumab competitive IgG titers from pooled sera were determined as described in the Methods. Competitive titers (log2) were the reciprocal value of serum dilution that resulted in 50% inhibition of palivizumab monoclonal antibody binding to recombinant RSV F. In cases when the 50% inhibition could not be obtained, a titer of <20 was reported for the sample.</p>", "links"=>[], "tags"=>["Virology", "immunology"], "article_id"=>203737, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.g005", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cotton_rat_challenge_model_/203737", "title"=>"Cotton rat challenge model.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-19 19:25:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/533125"], "description"=>"<p>(A) Negative staining electronmicroscopy of purified RSV F produced in Sf9 cells with the baculovirus vector BV683. RSV F nanoparticles were adsorbed to carbon parlodion-coated copper grids and negatively stained with 1% phosphotungstic acid. Bar represent 20 nm. (B) Reverse phase HPLC analysis on a PLRP-S 4000A, 2.1×150 mm column purified RSV F consisted of 90.1% F1+F2 at retention time of 11.195 min and 9.9% F1 at retention time of 6.256. (C) RSV vaccine particle size estimation by size exclusion HPLC RSV F protein using a BEH200, 1.7 µm, 4.6×300 mm size exclusion column. Size exclusion chromatography showed the RSV F nanoparticles consist primarily of F0 (covalently linked F1 and F2) with a low level of free F1 subunits. F0 (F1+F2) peak is 95.8% and F1 peak is 3.8% of the total peak area. (D) Dynamic light scattering of purified RSV F showing the distribution (%) of the intensity of light scattered by the particles using a detector placed at an angle 173°. Relative light intensity (%) was plotted relative to the particle diameter in nanometers (d.nm) of RSV F.</p>", "links"=>[], "tags"=>["dls", "purified", "rsv"], "article_id"=>203607, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.g004", "stats"=>{"downloads"=>2, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EM_HPLC_and_DLS_analysis_of_purified_RSV_F_/203607", "title"=>"EM, HPLC, and DLS analysis of purified RSV F.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-19 19:24:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/532876"], "description"=>"<p>Sf9 insect cells were infected at MOI = 1 with rBV expressing RSV F containing nine different fusion domain deletions (Δ2, Δ4, Δ6, Δ8, Δ10, Δ12, Δ14, Δ16, and Δ18) engineered into clone #541 with a modification of furin site II an intact fusion domain (Δ0). Infected cells harvested 67 hr post infection, extracted with buffer containing 0.5% Tergitol NP9 and soluble fractions analyzed by SDS-PAGE and Western blot. (A) Western blot analysis with anti-RSV F1 specific monoclonal antibody of nonionic detergent soluble proteins from Sf9 cells infected with baculovirus vectors containing RSV F genes with 2 to 18 amino acid deletions in the fusion domain from Phe137– Val154; each derived from RSV F #541 with a modification of furin site II. (B) Sf9 insect cells infected with rBV expressing the RSV F fusion domain deletions as described above were analyzed for cell surface RSV F protein immunostaining with anti-RSV F hyper-immune sheep serum, followed by staining with PE conjugated donkey anti-sheep IgG and FACS analysis.</p>", "links"=>[], "tags"=>["rsv", "fusion"], "article_id"=>203364, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.g002", "stats"=>{"downloads"=>8, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_RSV_F_fusion_domain_mutants_/203364", "title"=>"Expression of RSV F fusion domain mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-19 19:23:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/532965"], "description"=>"<p>Sf9 insect cells were infected at MOI = 1 with BV683 expressing modified full length RSV F and harvested 67 hr post infection and purified as described in the Methods. Purified RSV F protein was analyzed for purity by SDS-PAGE under non-reducing or reducing conditions to retain or disrupt intra-protein disulfide bond between F1 and F2 subunit. (A) Coomassie blue strained gel of replicate samples of non-reduced or reduced purified RSV F. (B) Western blot using anti-RSV F1 monoclonal antibody of non-reduced and reduced RSV F. The location of non-reduced polypeptide (F), reduced but full length (F0), and F1 and F2 polypeptides are indicated with protein marker molecular weight x 10<sup>3</sup> included in the first lane.</p>", "links"=>[], "tags"=>["blot", "purified", "rsv"], "article_id"=>203455, "categories"=>["Virology", "Immunology"], "users"=>["Gale Smith", "Rama Raghunandan", "Yingyun Wu", "Ye Liu", "Michael Massare", "Margret Nathan", "Bin Zhou", "Hanxin Lu", "Sarathi Boddapati", "Jingning Li", "David Flyer", "Gregory Glenn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050852.g003", "stats"=>{"downloads"=>6, "page_views"=>291, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SDS_PAGE_and_Western_blot_analysis_purified_RSV_F_/203455", "title"=>"SDS-PAGE and Western blot analysis purified RSV F.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-19 19:23:43"}

PMC Usage Stats | Further Information

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Relative Metric

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