PaperRecombinant Bordetella pertussis pertactin (P69) from the yeast Pichia pastoris: high-level production and immunological properties
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Quantitative microcapillary electrophoresis immunoassay (mCE IA) for end-to-end analysis of pertactin within in-process samples and Quadracel® vaccine
2021, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Pertactin (PRN or P69) is a cell-surface adhesion protein of B. pertussis and is one of the components of the aP vaccine [14]. Since its discovery, PRN recovery from cell cultures is low in comparison to other antigens [15–17]. Hence, it is important to closely monitor each production step for PRN yield, to ensure maximum recovery.
Development of Process to Produce Recombinant Component for Acellular Pertussis Vaccine
2017, Current Developments in Biotechnology and Bioengineering: Human and Animal Health ApplicationsProduction of LYZL6, a novel human c-type lysozyme, in recombinant Pichia pastoris employing high cell density fed-batch fermentation
2014, Journal of Bioscience and BioengineeringExpression of Apostichopus japonicus lysozyme in the methylotrophic yeast Pichia pastoris
2011, Protein Expression and PurificationComparison of recombinant and native pertactin of Bordetella pertussis
2011, VaccineCitation Excerpt :Thanks to the recombinant DNA technology, some studies have been tried to obtain expression of recombinant Prn (r-Prn) in Escherichia coli, Baculovirus insect cell and Yeast expression systems [15–19]. So far, most of these studies have focused on the immunogenicity, protection efficacy or the antigenic epitope(s) of recombinant protein [16–20]. However, physical and biochemical characterisation of r-Prn have not been investigated systematically.