Recombinant Bordetella pertussis pertactin (P69) from the yeast Pichia pastoris: high-level production and immunological properties.
Romanos, MA
Clare, JJ
Beesley, KM
Rayment, FB
Ballantine, SP
Makoff, AJ
Dougan, G
Fairweather, NF
Charles, IG
- Publication Type:
- Journal Article
- Citation:
- Vaccine, 1991, 9 (12), pp. 901 - 906
- Issue Date:
- 1991-12
Closed Access
Filename | Description | Size | |||
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2009002891OK.pdf | 1.22 MB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Romanos, MA | en_US |
dc.contributor.author | Clare, JJ | en_US |
dc.contributor.author | Beesley, KM | en_US |
dc.contributor.author | Rayment, FB | en_US |
dc.contributor.author | Ballantine, SP | en_US |
dc.contributor.author | Makoff, AJ | en_US |
dc.contributor.author | Dougan, G | en_US |
dc.contributor.author | Fairweather, NF | en_US |
dc.contributor.author | Charles, IG | en_US |
dc.date.issued | 1991-12 | en_US |
dc.identifier.citation | Vaccine, 1991, 9 (12), pp. 901 - 906 | en_US |
dc.identifier.issn | 0264-410X | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/13749 | |
dc.description.abstract | Acellular whooping cough vaccines are based on pertussis toxoid but their effectiveness may be increased by the addition of other Bordetella pertussis antigens. We expressed the immunogenic outer membrane protein pertactin (P69) from B. pertussis to high levels in multi-copy transformants of the industrial yeast Pichia pastoris. In high-density fermentations, engineered P. pastoris yielded greater than 3 g of the protein per litre of culture. Purified recombinant pertactin was able to stimulate the incomplete protection afforded by toxoid to the level of the whole-cell vaccine, as shown by the Kendrick test, supporting its inclusion in future acellular vaccines. | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | Vaccine | en_US |
dc.relation.isbasedon | 10.1016/0264-410x(91)90011-t | en_US |
dc.subject.classification | Virology | en_US |
dc.subject.mesh | Bordetella pertussis | en_US |
dc.subject.mesh | Pichia | en_US |
dc.subject.mesh | Saccharomyces cerevisiae | en_US |
dc.subject.mesh | Whooping Cough | en_US |
dc.subject.mesh | Bacterial Outer Membrane Proteins | en_US |
dc.subject.mesh | Recombinant Proteins | en_US |
dc.subject.mesh | Virulence Factors, Bordetella | en_US |
dc.subject.mesh | Pertussis Vaccine | en_US |
dc.subject.mesh | Blotting, Western | en_US |
dc.subject.mesh | Gene Expression | en_US |
dc.subject.mesh | Transformation, Genetic | en_US |
dc.subject.mesh | Fermentation | en_US |
dc.subject.mesh | Base Sequence | en_US |
dc.subject.mesh | Genetic Vectors | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.title | Recombinant Bordetella pertussis pertactin (P69) from the yeast Pichia pastoris: high-level production and immunological properties. | en_US |
dc.type | Journal Article | |
utslib.citation.volume | 12 | en_US |
utslib.citation.volume | 9 | en_US |
utslib.location.activity | Netherlands | en_US |
utslib.for | 1107 Immunology | en_US |
utslib.for | 06 Biological Sciences | en_US |
utslib.for | 07 Agricultural and Veterinary Sciences | en_US |
utslib.for | 11 Medical and Health Sciences | en_US |
dc.location.activity | ISI:A1991GQ32600011 | en_US |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation | |
utslib.copyright.status | closed_access | |
pubs.issue | 12 | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 9 | en_US |
Abstract:
Acellular whooping cough vaccines are based on pertussis toxoid but their effectiveness may be increased by the addition of other Bordetella pertussis antigens. We expressed the immunogenic outer membrane protein pertactin (P69) from B. pertussis to high levels in multi-copy transformants of the industrial yeast Pichia pastoris. In high-density fermentations, engineered P. pastoris yielded greater than 3 g of the protein per litre of culture. Purified recombinant pertactin was able to stimulate the incomplete protection afforded by toxoid to the level of the whole-cell vaccine, as shown by the Kendrick test, supporting its inclusion in future acellular vaccines.
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