Rational Engineering of Recombinant Picornavirus Capsids to Produce Safe, Protective Vaccine Antigen
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{"title"=>"Rational Engineering of Recombinant Picornavirus Capsids to Produce Safe, Protective Vaccine Antigen", "type"=>"journal", "authors"=>[{"first_name"=>"Claudine", "last_name"=>"Porta", "scopus_author_id"=>"7005319054"}, {"first_name"=>"Abhay", "last_name"=>"Kotecha", "scopus_author_id"=>"55199944100"}, {"first_name"=>"Alison", "last_name"=>"Burman", "scopus_author_id"=>"8615904500"}, {"first_name"=>"Terry", "last_name"=>"Jackson", "scopus_author_id"=>"7401595392"}, {"first_name"=>"Jingshan", "last_name"=>"Ren", "scopus_author_id"=>"7403083572"}, {"first_name"=>"Silvia", "last_name"=>"Loureiro", "scopus_author_id"=>"25637393500"}, {"first_name"=>"Ian M.", "last_name"=>"Jones", "scopus_author_id"=>"34769538800"}, {"first_name"=>"Elizabeth E.", "last_name"=>"Fry", "scopus_author_id"=>"7102301301"}, {"first_name"=>"David I.", "last_name"=>"Stuart", "scopus_author_id"=>"56377639700"}, {"first_name"=>"Bryan", "last_name"=>"Charleston", "scopus_author_id"=>"6701319119"}], "year"=>2013, "source"=>"PLoS Pathogens", "identifiers"=>{"scopus"=>"2-s2.0-84875972953", "sgr"=>"84875972953", "issn"=>"15537366", "doi"=>"10.1371/journal.ppat.1003255", "pmid"=>"23544011", "isbn"=>"1553-7374 (Electronic)\\r1553-7366 (Linking)", "pui"=>"368694518"}, "id"=>"07b31442-4d2d-3ad5-8a66-bab6749442fd", "abstract"=>"Foot-and-mouth disease remains a major plague of livestock and outbreaks are often economically catastrophic. Current inactivated virus vaccines require expensive high containment facilities for their production and maintenance of a cold-chain for their activity. We have addressed both of these major drawbacks. Firstly we have developed methods to efficiently express recombinant empty capsids. Expression constructs aimed at lowering the levels and activity of the viral protease required for the cleavage of the capsid protein precursor were used; this enabled the synthesis of empty A-serotype capsids in eukaryotic cells at levels potentially attractive to industry using both vaccinia virus and baculovirus driven expression. Secondly we have enhanced capsid stability by incorporating a rationally designed mutation, and shown by X-ray crystallography that stabilised and wild-type empty capsids have essentially the same structure as intact virus. Cattle vaccinated with recombinant capsids showed sustained virus neutralisation titres and protection from challenge 34 weeks after immunization. This approach to vaccine antigen production has several potential advantages over current technologies by reducing production costs, eliminating the risk of infectivity and enhancing the temperature stability of the product. Similar strategies that will optimize host cell viability during expression of a foreign toxic gene and/or improve capsid stability could allow the production of safe vaccines for other pathogenic picornaviruses of humans and animals.", "link"=>"http://www.mendeley.com/research/rational-engineering-recombinant-picornavirus-capsids-produce-safe-protective-vaccine-antigen", "reader_count"=>139, "reader_count_by_academic_status"=>{"Unspecified"=>7, "Professor > Associate Professor"=>3, "Librarian"=>1, "Researcher"=>38, "Student > Doctoral Student"=>10, "Student > Ph. D. Student"=>32, "Student > Postgraduate"=>3, "Other"=>5, "Student > Master"=>14, "Student > Bachelor"=>20, "Lecturer"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>4}, "reader_count_by_user_role"=>{"Unspecified"=>7, "Professor > Associate Professor"=>3, "Librarian"=>1, "Researcher"=>38, "Student > Doctoral Student"=>10, "Student > Ph. D. Student"=>32, "Student > Postgraduate"=>3, "Other"=>5, "Student > Master"=>14, "Student > Bachelor"=>20, "Lecturer"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>4}, "reader_count_by_subject_area"=>{"Unspecified"=>10, "Agricultural and Biological Sciences"=>82, "Arts and Humanities"=>1, "Veterinary Science and Veterinary Medicine"=>5, "Chemistry"=>4, "Computer Science"=>2, "Economics, Econometrics and Finance"=>1, "Engineering"=>2, "Biochemistry, Genetics and Molecular Biology"=>6, "Materials Science"=>2, "Medicine and Dentistry"=>11, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Physics and Astronomy"=>3, "Social Sciences"=>1, "Immunology and Microbiology"=>7}, "reader_count_by_subdiscipline"=>{"Materials Science"=>{"Materials Science"=>2}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>11}, "Social Sciences"=>{"Social Sciences"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>3}, "Unspecified"=>{"Unspecified"=>10}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}, "Arts and Humanities"=>{"Arts and Humanities"=>1}, "Engineering"=>{"Engineering"=>2}, "Chemistry"=>{"Chemistry"=>4}, "Economics, Econometrics and Finance"=>{"Economics, Econometrics and Finance"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>7}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>82}, "Computer Science"=>{"Computer Science"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>5}}, "reader_count_by_country"=>{"Argentina"=>1, "United States"=>1, "Japan"=>1, "Denmark"=>1, "United Kingdom"=>3, "Australia"=>3, "Kenya"=>1}, "group_count"=>7}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/999654"], "description"=>"<p>(a) The crystal structure of FMDV serotype A22 <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003255#ppat.1003255-Curry1\" target=\"_blank\">[2]</a> was analysed as described in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003255#s4\" target=\"_blank\">Materials and Methods</a>. This led to the prediction and modelling of a potential disulphide bond between pentamers by mutation to cysteine of VP2 histidine residue 93, located on the α-helix at the two-fold symmetry axis. (b) Western blot analyses of A22-wt and A22-H2093C empty capsids, expressed from recombinant vaccinia viruses and sedimented through 15–45% sucrose gradients. Each gradient was fractionated from the bottom. FMDV capsid proteins were detected using an anti-FMDV strain A22 polyclonal antibody raised in guinea pigs. Crude extracts were left untreated, heated to 56°C for 2 h or acidified to pH 5.2 for 15 min. Following both heat and acid treatments A22-H2093C capsids remained intact and migrated to fraction 4, as before treatment, whereas A22-wt capsids fractured, remaining near the top of the gradient in fraction 10.</p>", "links"=>[], "tags"=>["capsids", "fmdv"], "article_id"=>661534, "categories"=>["Virology", "Infectious Diseases", "Biophysics"], "users"=>["Claudine Porta", "Abhay Kotecha", "Alison Burman", "Terry Jackson", "Jingshan Ren", "Silvia Loureiro", "Ian M. Jones", "Elizabeth E. Fry", "David I. Stuart", "Bryan Charleston"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003255.g001", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Rational_design_to_produce_stable_empty_capsids_of_FMDV_A22_/661534", "title"=>"Rational design to produce stable empty capsids of FMDV A22.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-03-28 10:03:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/999669"], "description"=>"<div><p>Foot-and-mouth disease remains a major plague of livestock and outbreaks are often economically catastrophic. Current inactivated virus vaccines require expensive high containment facilities for their production and maintenance of a cold-chain for their activity. We have addressed both of these major drawbacks. Firstly we have developed methods to efficiently express recombinant empty capsids. Expression constructs aimed at lowering the levels and activity of the viral protease required for the cleavage of the capsid protein precursor were used; this enabled the synthesis of empty A-serotype capsids in eukaryotic cells at levels potentially attractive to industry using both vaccinia virus and baculovirus driven expression. Secondly we have enhanced capsid stability by incorporating a rationally designed mutation, and shown by X-ray crystallography that stabilised and wild-type empty capsids have essentially the same structure as intact virus. Cattle vaccinated with recombinant capsids showed sustained virus neutralisation titres and protection from challenge 34 weeks after immunization. This approach to vaccine antigen production has several potential advantages over current technologies by reducing production costs, eliminating the risk of infectivity and enhancing the temperature stability of the product. Similar strategies that will optimize host cell viability during expression of a foreign toxic gene and/or improve capsid stability could allow the production of safe vaccines for other pathogenic picornaviruses of humans and animals.</p> </div>", "links"=>[], "tags"=>["recombinant", "picornavirus", "capsids"], "article_id"=>661548, "categories"=>["Virology", "Infectious Diseases", "Biophysics"], "users"=>["Claudine Porta", "Abhay Kotecha", "Alison Burman", "Terry Jackson", "Jingshan Ren", "Silvia Loureiro", "Ian M. Jones", "Elizabeth E. Fry", "David I. Stuart", "Bryan Charleston"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003255", "stats"=>{"downloads"=>6, "page_views"=>44, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Rational_Engineering_of_Recombinant_Picornavirus_Capsids_to_Produce_Safe_Protective_Vaccine_Antigen_/661548", "title"=>"Rational Engineering of Recombinant Picornavirus Capsids to Produce Safe, Protective Vaccine Antigen", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-03-28 10:07:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/999664"], "description"=>"<p>The quantity of viral genome (Log10/ml) was determined by quantitative real-time PCR in serum samples from each animal on days 0–7 and 9 post-challenge. Individual data for animals vaccinated with (a) A22-wt, (b) A22-H2093C and for non-vaccinated control animals (c). Clinical signs were detected in two of the four animals that had received wild-type empty capsid (FMD140 and FMD143) and in one of the four animals immunised with mutated capsids (FMD144). Both non-vaccinated control animals showed overt clinical signs.</p>", "links"=>[], "tags"=>["genome"], "article_id"=>661543, "categories"=>["Virology", "Infectious Diseases", "Biophysics"], "users"=>["Claudine Porta", "Abhay Kotecha", "Alison Burman", "Terry Jackson", "Jingshan Ren", "Silvia Loureiro", "Ian M. Jones", "Elizabeth E. Fry", "David I. Stuart", "Bryan Charleston"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003255.g005", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Virus_genome_detection_/661543", "title"=>"Virus genome detection.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-03-28 10:06:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/999660"], "description"=>"<p>(a) The electron density map for A22-wt (left panel) presents the expected histidine side chains for VP2 residue 93 whereas the map for A22-H2093C (right panel) shows the disulphide density at the two-fold axis between pentamers. (b) Side by side ribbon drawings of the recombinant empty capsid protomers and beneath the individual VP1, 2 and 4 proteins. There was no difference between the A22-wt and A22-H2093C capsids on the exterior surface; significant disorder observed on the interior of the A22-H2093C capsids is shown as thickened lines and corresponds to the N terminus of VP1 (residues 1 to 12) and VP4 (residues 15 to 38 and 65 to 80) located near the 3-fold axes. To a lesser extent residues 38–41 in VP2 were also disordered.</p>", "links"=>[], "tags"=>["a22-wt", "a22-h2093c"], "article_id"=>661539, "categories"=>["Virology", "Infectious Diseases", "Biophysics"], "users"=>["Claudine Porta", "Abhay Kotecha", "Alison Burman", "Terry Jackson", "Jingshan Ren", "Silvia Loureiro", "Ian M. Jones", "Elizabeth E. Fry", "David I. Stuart", "Bryan Charleston"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003255.g003", "stats"=>{"downloads"=>2, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_analysis_of_A22_wt_and_A22_H2093C_empty_capsids_/661539", "title"=>"Structure analysis of A22-wt and A22-H2093C empty capsids.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-03-28 10:05:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/999662"], "description"=>"<p>The group mean virus neutralising antibody titres (Log2) for animals inoculated with A22-wt (black line) or A22-H2093C (grey line) are shown from week 0 to week 34. All animals were vaccinated on week 0 and week 3. Blood samples were taken at weekly intervals until week 6 and then on week 22 and finally on week 34 when challenge with live virus was carried out. Error bars represent the standard error of the mean.</p>", "links"=>[], "tags"=>["neutralising", "antibody", "titres"], "article_id"=>661541, "categories"=>["Virology", "Infectious Diseases", "Biophysics"], "users"=>["Claudine Porta", "Abhay Kotecha", "Alison Burman", "Terry Jackson", "Jingshan Ren", "Silvia Loureiro", "Ian M. Jones", "Elizabeth E. Fry", "David I. Stuart", "Bryan Charleston"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003255.g004", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Virus_neutralising_antibody_titres_pre_challenge_/661541", "title"=>"Virus neutralising antibody titres pre-challenge.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-03-28 10:05:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/999658"], "description"=>"<p>The extracts from either 2×2125 cm<sup>2</sup> roller flasks of HEK293T cells co-infected with recombinant vaccinia viruses, vA22-wt+vTF7-3 or vA22-H2093C+vTF7-3 (a) or from 300 ml culture of Sf9 cells infected with recombinant baculovirus virus, bA22-wt or bA22-H2093C (b) were each loaded onto a 36 ml 15–45% sucrose gradient and centrifuged at 21,000 rpm for 22 h at 12°C (SW32 rotor, Beckman). Bands were visualised by illumination of the gradients from the top with a halogen fibre optic light source (Schott). Fractionation of the lower halves of the gradients was in 13 aliquots of 1 ml (fractions 1–13) and 3 aliquots of 2 ml (fractions 14–16) collected from the bottom: 10 µl each from fractions 2 to 15 were analysed on 4–12% acrylamide Novex NuPAGE gels (Invitrogen).</p>", "links"=>[], "tags"=>["gradient", "purification", "sds", "a22-wt", "a22-h2093c", "recombinant"], "article_id"=>661537, "categories"=>["Virology", "Infectious Diseases", "Biophysics"], "users"=>["Claudine Porta", "Abhay Kotecha", "Alison Burman", "Terry Jackson", "Jingshan Ren", "Silvia Loureiro", "Ian M. Jones", "Elizabeth E. Fry", "David I. Stuart", "Bryan Charleston"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003255.g002", "stats"=>{"downloads"=>4, "page_views"=>48, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sucrose_gradient_purification_and_SDS_PAGE_analysis_of_A22_wt_and_A22_H2093C_recombinant_capsids_/661537", "title"=>"Sucrose gradient purification and SDS PAGE analysis of A22-wt and A22-H2093C recombinant capsids.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-03-28 10:04:39"}

PMC Usage Stats | Further Information

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Relative Metric

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