Current Status of Biopharmaceuticals: Approved Products and Trends in Approvals

Walsh, Gary

doi:10.1002/9783527620982.ch

Cited by 15 publications

(7 citation statements)

References 32 publications

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“…The first therapeutic produced using IC-BEVS was a veterinary vaccine against the swine fever virus, approved in 2000 (Intervet International, The Netherlands). Today, other commercialized veterinary drugs are made using IC-BEVS (Walsh, 2005): Bayovac vaccine from Bayer (Germany), Advasure vaccine from Pfizer and an interferon from Virbac (France).…”

Section: Therapeuticsmentioning

confidence: 99%

Insect cells as factories for biomanufacturing

Drugmand

Schneider

Agathos

2012

Biotechnology Advances

123

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Insect cells (IC) and particularly lepidopteran cells are an attractive alternative to mammalian cells for biomanufacturing. Insect cell culture, coupled with the lytic expression capacity of baculovirus expression vector systems (BEVS), constitutes a powerful platform, IC-BEVS, for the abundant and versatile formation of heterologous gene products, including proteins, vaccines and vectors for gene therapy. Such products can be manufactured on a large scale thanks to the development of efficient and scaleable production processes involving the integration of a cell growth stage and a stage of cell infection with the recombinant baculovirus vector. Insect cells can produce multimeric proteins functionally equivalent to the natural ones and engineered vectors can be used for efficient expression. Insect cells can be cultivated easily in serum- and protein-free media. A growing number of companies are currently developing an interest in producing therapeutics using IC-BEVS, and many products are today in clinical trials and on the market for veterinary and human applications. This review summarizes current knowledge on insect cell metabolism, culture conditions and applications.

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Section: Therapeuticsmentioning

confidence: 99%

Insect cells as factories for biomanufacturing

Drugmand

Schneider

Agathos

2012

Biotechnology Advances

123

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“…These approaches, which do have a clear parallel in plants, have been only partially successful. It is generally accepted that MAb yield is not always a reflection of the abundance Deleted: l Deleted: [41] ... [1] factor that results in the activation of several chaperones, but also apoptosis if certain injury threshold is reached [40] .…”

Section: Deleted: Alsomentioning

confidence: 99%

“…Since the production of human insulin in E. coli, more than one hundred recombinant therapeutic drugs have been approved for commercialization and a tremendous amount of recombinant proteins are being used in diagnosis or research [1]. Fermentation in prokaryotes and yeast accounts for the majority of recombinant products; however, the increasing complexity of products is promoting the use of eukaryotes other than yeast as production systems.…”

Section: Introductionmentioning

confidence: 99%

Manufacturing antibodies in the plant cell

Orzáez

Granell

Blázquez

2009

Biotechnology Journal

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International audiencePlants have long been considered advantageous platforms for large-scale production of antibodies due to their low cost, scalability, and the low chances of pathogen contamination. Much effort has therefore been devoted to efficiently produce mAbs (from nanobodies to secretory antibodies) in plant cells. Several technical difficulties have been encountered and are being coped with. Improvements in production levels have been achieved by manipulation of gene expression and, more efficiently, of cell targeting and protein folding and assembly. Differences in mAb glycosylation patterns between animal and plant cells are being successfully addressed by the elimination and introduction of the appropriate enzyme activities in plant cells. Another relevant battlefield is the dichotomy between production capacity and speed. Classically, stably transformed plant lines have been proposed for large scale mAb production, whereas the use of transient expression systems has always provided production speed at the cost of scalability. However, recent advances in transient expression techniques have brought impressive yield improvements, turning speed and scalability highly compatible assets. In the era of personalized medicines, the combination of yield and speed, and the advances in glyco-engineering have made the plant cell a serious contender in the field of recombinant antibody production

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“…However, the major limitations of baculovirus expression systems are the time and effort required to produce recombinant baculovirus to express the protein of interest, and the protein N-glycosylation pathway of insect cells which is unable to produce complex binary N-linked oligosaccharide side chains with penultimate galactose and terminal sialic acid residues [6,7]. Compared to these three systems, use of mammalian cells provides appropriate solubility, correct folding, and fully processed r-proteins and has become the most desirable system in the pharmaceutical industry for protein-based therapeutic products [8].…”

Section: Introductionmentioning

confidence: 99%

Transient Transfection Factors for High-Level Recombinant Protein Production in Suspension Cultured Mammalian Cells

Liu¹,

Dalby²,

Chen³

et al. 2008

Mol Biotechnol

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The efficient transfection of cloned genes into mammalian cells system plays a critical role in the production of large quantities of recombinant proteins (r-proteins). In order to establish a simple and scaleable transient protein production system, we have used a cationic lipid-based transfection reagent-FreeStyle MAX to study transient transfection in serum-free suspension human embryonic kidney (HEK) 293 and Chinese hamster ovary (CHO) cells. We used quantification of green fluorescent protein (GFP) to monitor transfection efficiency and expression of a cloned human IgG antibody to monitor r-protein production. Parameters including transfection reagent concentration, DNA concentration, the time of complex formation, and the cell density at the time of transfection were analyzed and optimized. About 70% GFP-positive cells and 50-80 mg/l of secreted IgG antibody were obtained in both HEK-293 and CHO cells under optimal conditions. Scale-up of the transfection system to 1 l resulted in similar transfection efficiency and protein production. In addition, we evaluated production of therapeutic proteins such as human erythropoietin and human blood coagulation factor IX in both HEK-293 and CHO cells. Our results showed that the higher quantity of protein production was obtained by using optimal transient transfection conditions in serum-free adapted suspension mammalian cells.

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Current Status of Biopharmaceuticals: Approved Products and Trends in Approvals

Cited by 15 publications

References 32 publications

Insect cells as factories for biomanufacturing

Insect cells as factories for biomanufacturing

Manufacturing antibodies in the plant cell

Transient Transfection Factors for High-Level Recombinant Protein Production in Suspension Cultured Mammalian Cells

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