Transgenic Plants for Therapeutic Proteins: Linking Upstream and Downstream Strategies

Cramer, Carole L.; Boothe, J. G.; Oishi, Karen K.

doi:10.1007/978-3-642-60234-4_5

Cited by 72 publications

(64 citation statements)

References 63 publications

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“…A single tobacco plant is capable of generating a million seeds and 1 acre of tobacco can produce more than 40 metric tons of leaves per year (Cramer et al, 1999;Arlen et al, 2007). Harvesting leaves before flowering can offer nearly complete transgene containment in addition to protection offered by maternal inheritance.…”

Section: Plastid Transformation Of Different Crop Speciesmentioning

confidence: 99%

Chloroplast Vector Systems for Biotechnology Applications

2007

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Chloroplasts are ideal hosts for expression of transgenes. Transgene integration into the chloroplast genome occurs via homologous recombination of flanking sequences used in chloroplast vectors. Identification of spacer regions to integrate transgenes and endogenous regulatory sequences that support optimal expression is the first step in construction of chloroplast vectors. Thirty-five sequenced crop chloroplast genomes provide this essential information. Various steps involved in the design and construction of chloroplast vectors, DNA delivery, and multiple rounds of selection are described. Several crop species have stably integrated transgenes conferring agronomic traits, including herbicide, insect, and disease resistance, drought and salt tolerance, and phytoremediation. Chloroplast-derived vaccine antigens against bacterial (cholera, tetanus, anthrax, plague, and Lyme disease), viral (canine parvovirus [CPV] and rotavirus), and protozoan (amoeba) pathogens have been evaluated by immune responses, neutralizing antibodies, and pathogen or toxin challenge in animals. Chloroplasts have been used as bioreactors for production of biopolymers, amino acids, and industrial enzymes. Oral delivery of plant cells expressing proinsulin (Pins) in chloroplasts offered protection against development of insulitis in diabetic mice; such delivery eliminates expensive fermentation, purification, low temperature storage, and transportation. Chloroplast vector systems used in these biotechnology applications are described.

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Section: Plastid Transformation Of Different Crop Speciesmentioning

confidence: 99%

Chloroplast Vector Systems for Biotechnology Applications

2007

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“…A synthetic gene coding for the human epidermal growth factor was expressed only up to 0.001% of total soluble protein in transgenic tobacco 35,36 . In spite of several successful reports of high-level expression of non-human proteins (e.g.…”

Section: Plant-derived Biopharmaceuticals and Human Proteinsmentioning

confidence: 99%

“…If biopharmaceuticals that are potentially harmful are capable of persisting in the environment and might accumulate in non-target organisms, precautionary measures should be taken. Induction of biopharmaceutical production after harvesting (as was done in the case of glucocerebrosidase 36 ) might be one approach to minimize environmental exposure, provided that the use of viral vectors does not introduce additional environmental or regulatory concerns. Expression of potentially harmful proteins in a form that must be treated for activation might minimize the risk of exposure.…”

Section: Future Perspectivesmentioning

confidence: 99%

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Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants

Daniell

Streatfield²,

Wycoff

2001

Trends in Plant Science

665

412

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The use of plants for medicinal purposes dates back thousands of years but genetic engineering of plants to produce desired biopharmaceuticals is much more recent. As the demand for biopharmaceuticals is expected to increase, it would be wise to ensure that they will be available in significantly larger amounts, on a cost-effective basis. Currently, the cost of biopharmaceuticals limits their availability. Plant-derived biopharmaceuticals are cheap to produce and store, easy to scale up for mass production, and safer than those derived from animals. Here, we discuss recent developments in this field and possible environmental concerns.

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“…Taking into account the important advantages of plants over other expression systems, such as low production and scale-up costs, the natural storage stability of the recombinant proteins in tubers or seeds, and the fact that transgenic plants do not propagate human or animal pathogens (Cramer et al, 2000;Hood and Howard, 1999;Kusnadi et al, 1997), the expression of aprotinin in maize seeds was studied by Zhong et al (1999). Now, recombinant aprotinin produced in maize seeds is commercially available under the name of AproliZean TM (Prodigene, 2004).…”

Section: Introductionmentioning

confidence: 99%

Purification of recombinant aprotinin produced in transgenic corn seed: separation from CTI utilizing ion-exchange chromatography

Azzoni

Takahashi

Woodard

et al. 2005

Braz. J. Chem. Eng.

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-Protein expression in transgenic plants is considered one of the most promising approaches for producing pharmaceutical proteins. As has happened with other recombinant protein production schemes, the downstream processing (dsp) of these proteins produced in plants is key to the technical and economic success of large-scale applications. Since dsp of proteins produced transgenically in plants has not been extensively studied, it is necessary to broaden the investigation in this field in order to more precisely evaluate the commercial feasibility of this route of expression. In this work, we studied the substitution of an IMAC chromatographic step, described in previous work (Azzoni et al., 2002), with ion-exchange chromatography on SP Sepharose Fast Flow resin as the second step in the purification of recombinant aprotinin from transgenic maize seed. The main goal of this second purification step is to separate the recombinant aprotinin from the native corn trypsin inhibitor. Analysis of the adsorption isotherms determined at 25°C under different conditions allowed selection of 0.020 M Tris pH 8.5 as the adsorption buffer. The cation-exchange chromatographic process produced a high-purity aprotinin that was more than ten times more concentrated than that generated using an IMAC step.

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Transgenic Plants for Therapeutic Proteins: Linking Upstream and Downstream Strategies

Cited by 72 publications

References 63 publications

Chloroplast Vector Systems for Biotechnology Applications

Chloroplast Vector Systems for Biotechnology Applications

Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants

Purification of recombinant aprotinin produced in transgenic corn seed: separation from CTI utilizing ion-exchange chromatography

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