Green factory: Plants as bioproduction platforms for recombinant proteins

Arkansas Biosciences Institute, Arkansas State University, Jonesboro, AR 72401, United States.
Biotechnology advances (Impact Factor: 9.02). 09/2011; 30(5):1171-84. DOI: 10.1016/j.biotechadv.2011.08.020
Source: PubMed


Molecular farming, long considered a promising strategy to produce valuable recombinant proteins not only for human and veterinary medicine, but also for agriculture and industry, now has some commercially available products. Various plant-based production platforms including whole-plants, aquatic plants, plant cell suspensions, and plant tissues (hairy roots) have been compared in terms of their advantages and limits. Effective recombinant strategies are summarized along with descriptions of scalable culture systems and examples of commercial progress and success.

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Available from: Maureen Dolan, Dec 15, 2014
    • "Plants have long been proposed as an attractive platform for the production of recombinant proteins for human health, because of perceived safety advantages, as they do not harbour mammalian pathogens, and cost and scalability advantages, as stainless steel fermenters are not required. Results of studies conducted during the last two decades suggest that plants are cost-effective, highly scalable and safe platforms for the production of subunit vaccines, monoclonal antibodies and therapeutic proteins (Basaran and Rodr ıguez-Cerezo, 2008; Stoger et al., 2014; Tiwari et al., 2009; Twyman et al., 2012; Xu et al., 2012). "
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    ABSTRACT: Despite progress in the prevention and treatment of infectious diseases, they continue to present a major threat to public health. The frequency of emerging and reemerging infections and the risk of bioterrorism warrant significant efforts towards the development of prophylactic and therapeutic countermeasures. Vaccines are the mainstay of infectious disease prophylaxis. Traditional vaccines, however, are failing to satisfy the global demand because of limited scalability of production systems, long production timelines and product safety concerns. Subunit vaccines are a highly promising alternative to traditional vaccines. Subunit vaccines, as well as monoclonal antibodies and other therapeutic proteins, can be produced in heterologous expression systems based on bacteria, yeast, insect cells or mammalian cells, in shorter times and at higher quantities, and are efficacious and safe. However, current recombinant systems have certain limitations associated with production capacity and cost. Plants are emerging as a promising platform for recombinant protein production due to time and cost efficiency, scalability, lack of harboured mammalian pathogens and possession of the machinery for eukaryotic post-translational protein modification. So far, a variety of subunit vaccines, monoclonal antibodies and therapeutic proteins (antivirals) have been produced in plants as candidate countermeasures against emerging, reemerging and bioterrorism-related infections. Many of these have been extensively evaluated in animal models and some have shown safety and immunogenicity in clinical trials. Here, we overview ongoing efforts to producing such plant-based countermeasures.
    Plant Biotechnology Journal 09/2015; 13(8):1136-59. DOI:10.1111/pbi.12475 · 5.75 Impact Factor
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    • "An acceptable product shelf-life is also critical for logistics and inventory management, both for the manufacturer and for the end-user. Even so, it is estimated that with 1% protein expression and 50% protein recovery from purification, the cost of plant based protein is 10 and 1000 fold lower than microbial and mammalian based expression systems, respectively (Xu et al., 2012). Post-licensing activities should also be considered. "
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    ABSTRACT: The production of recombinant vaccines in plants may help to reduce the burden of veterinary diseases, which cause major economic losses and in some cases can affect human health. While there is abundant research in this area, a knowledge gap exists between the ability to create and evaluate plant-based products in the laboratory, and the ability to take these products on a path to commercialization. The current report, arising from a workshop sponsored by the Organisation for Economic Co-operation and Development (OECD) Co-operative Research Programme, addresses this gap by providing guidance in planning for the commercialization of plant-made vaccines for animal use. It includes relevant information on developing business plans, assessing market opportunities, manufacturing scale-up, financing, protecting and using intellectual property, and regulatory approval with a focus on Canadian regulations. Copyright © 2015. Published by Elsevier Inc.
    Biotechnology advances 07/2015; DOI:10.1016/j.biotechadv.2015.07.007 · 9.02 Impact Factor
    • "This study suggests that recombinant protein expression is product-specific and needs to be optimized individually. genic plants have gained significant attention in the last few years as a potential host for recombinant proteins due to the high levels of protein achieved and the low cost of cultivation [5] [6]. Nevertheless, critical issues arise from the lack of transgene containment and possible allergic reactions to plant antigens. "
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    ABSTRACT: Microalgae have potential as platforms for the synthesis of high-value recombinant proteins due to their many beneficial attributes including ease of cultivation, lack of pathogenic agents, and low-cost downstream processing. However, current recombinant protein levels are low compared to microbial platforms and stable insertion of transgenes is available in only a few microalgal strains. We have explored different strategies aimed at increasing growth rate and recombinant protein production in the Chlamydomonas reinhardtii chloroplast. A novel fluorescent protein (vivid Verde Fluorescent Protein, VFP) was expressed under the control of the native atpA promoter/5'UTR element. VFP levels were detected by western blotting, with increased protein levels observed when co-expressed with a gene encoding the Escherichia coli Spy chaperone. We used these transformant lines to study the effect of temperature, light and media on recombinant protein production and cell growth. VFP levels and fluorescence, assessed by flow cytometry, allowed a determination of improved cultivation conditions as 30 °C under mixotrophic mode. These conditions were tested for the accumulation of an antimicrobial endolysin (Cpl-1) of potential commercial interest, observing the outcome obtained for VFP could not be easily replicated for Cpl-1. This study indicates that recombinant protein expression is product-specific and needs to be optimised individually. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
    Biotechnology Journal 06/2015; 10(8). DOI:10.1002/biot.201400566 · 3.49 Impact Factor
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