Recombinant protein production from transgenic animals: Systems and applications
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Published:
Oct 23, 2019
Keywords:
Biotechnology, Genetic engineering, transgenic animals, recombinant proteins
Main Article Content
Abstract
The use of transgenic animals for the production of recombinant proteins for therapeutic purposes has been an alternative used for the production of drugs. The ability to make complex post-translational modifications in an efficient manner is an advantage that this type of technology has over the use of other transgenic organisms. For this reason, different transgenic animals (ruminants, rabbits, pigs, birds and insects) have been developed over the years and different systems (milk, egg, blood, urine and seminal fluid) have been studied to obtain recombinant proteins. Each animal and each system has advantages and disadvantages, which should be considered before starting the productive process of the protein of interest. Drugs such as ATryn®, Ruconest® and Kanuma® have already been approved by the FDA for human administration. The future of this type of preparations must be considered, given that there are several therapeutic proteins that are in the research phase or waiting to be approved and commercialized.
Article Details
How to Cite
Alvarado-Madrigal, M. F., Chavarría-Quirós, T., Leiva-Montero, B., & Mora-Román, J. J. (2019). Recombinant protein production from transgenic animals: Systems and applications. Tecnología En Marcha Journal, 32(4), Pág. 133–144. https://doi.org/10.18845/tm.v32i4.4798
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Artículo científico
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References
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[9] J. Sandow, W. Landgraf, R. Becker, and G. Seipke, “Equivalent Recombinant Human Insulin Preparations and their Place in Therapy,” European Endrocrinology, 11(1): 10-16, 2015.
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[16] F. Wegman, R. E. Geuze, Y. J. van der Helm, F. Cumhur Öner, W. J. A. Dhert, and J. Alblas, “Gene delivery of bone morphogenetic protein-2 plasmid DNA promotes bone formation in a large animal model, Journal of Tissue Engineering and Regenerative Medicine, 8(1), 763-770, 2014.
[17] C. E. Catalano, “Bacteriophage lambda: The path from biology to theranostic agent,” Wiley Interdisciplinary Reviews Nanomedicine and Nabiotechnology, 10(5), e1517, 2018.
[18] E. M. Ryan, S. P. Gorman, R. F. Donnelly, and B. F. Gilmore, “Recent advances in bacteriophage therapy: how delivery routes, formulation, concentration and timing influence the success of phage therapy,” Journal of Pharmacy and Pharmacology, 63(10), 1253-1264, 2011.
[19] J. Fan, Z. Zeng, K. Mai, Y. Yang, J. Feng, Y. Bai et al, “Preliminary treatment of bovine mastitis caused by Staphylococcus aureus, with trx-SA1, recombinant endolysin of S. aureus bacteriophage IME-SA1,” Veterinary Microbiology, 191, 65-71, 2016.
[20] C. Kishor, R. R. Mishra, S. K. Saraf, M. Kumar, A. K. Srivastav, and G. Nath, “Phage therapy of staphylococcal chronic osteomyelitis in experimental animal model,” Indian Journal of Medical Research, 143(1), 87-94, 2016.
[21] D. G. Knorre, N. V. Kudryashova, and T. S. Godovikova, “Chemical and Functional Aspects of Posttranslational Modification of Proteins,” Acta Naturae, 1(3), 29-51, 2009.
[22] O. G. Maksimenko, A. V. Deykin, Y. M. Khodarovich, and P. G. Georgiev, “Use of Transgenic Animals in Biotechnology: Prospects and Problems,” Acta Naturae, 5(1), 33-46, 2013.
[23] Y. Durocher and Butler M, “Expression systems for therapeutic glycoprotein production,” Current Opinion in Biotechnology, 20(6), 700-707, 2009.
[24] A. L. Demain and P. Vaishnav, “Production of recombinant proteins by microbes and higher organisms,” Biotechnology Advances, 27(3), 297-306, 2009.
[25] A. Dove, “Uncorking the biomanufacturing bottleneck,” Nature Biotechnology, 20(8), 777-779, 2002.
[26] L. M. Houdebine, “Production of pharmaceutical proteins by transgenic animals,” Comparative Immunology, Microbiology & Infectious Diseases, 32(2), 107-121, 2009.
[27] M. K Dyck, D. Lacroix, F. Pothier, and M. -A. Sirard, “Making recombinant proteins in animals – different systems, different applications,” Trends in Biotechnology, 21(9), 394-399, 2003.
[28] Organización de las Naciones Unidas para la Alimentación y la Agricultura, “Producción y productos: Animales lecheros, 2018. Disponible en: http://www.fao.org/dairy-production-products/production/productiondairy-animals/es/ (Accesado: 9-dic-2018)
[29] Y. Echelard, C. A. Ziomek, and H. M. Meade, “Production of recombinant therapeutic proteins in the milk of transgenic animals,” Biopharm International, 19(8), 36-46, 2006.
[30] W. H. Eyestone, “Production and breeding of transgenic cattle using in vitro embryo production technology,” Theriogenology, 51(2), 509-517, 1999.
[31] M. Massoud, J. Attal, D. Thépot, H. Pointu, M. G. Stinnakre, M. C. Théron et al, “The deleterious effects of human erythropoietin gene driven by the rabbit when acidic protein gene promoter in transgenic rabbits”, Reproduction Nutrition Development, 36(5), 555-563, 1996.
[32] L. M. Houdebine, “The production of pharmaceutical proteins from the milk of transgenic animals,” Reproduction Nutrition Development, 35(6), 609-617, 1995.
[33] K. Potočnik, V. Gantner, K. Kuterovac, and A. Cividini, “Mare´s milk: composition and protein fraction in comparison with different milk species,” Mljekarstvo, 61(2), 107-113, 2011.
[34] R. J. Wall, D. E. Kerr, and K. R. Bondioli, “Transgenic Dairy Cattle: Genetic Engineering on a Large Scale,” Journal of Dairy Science, 80(9), 2213-2224, 1997.
[35] T. D. Wilkins and W. Velander, “Isolation of recombinant proteins from milk,” Journal of Cellular Biochemistry, 49(4), 333-338, 1992.
[36] Z. L. Nikolov and S. L. Woodward, “Downstream processing of recombinant proteins from transgenic feedstock,” Current Opinion in Biotechnology, 15(5), 479-486, 2004.
[37] T. Morçöl, Q. He, and S. J. D. Bell, “Model Process for Removal of Caseins from Milk of Transgenic Animals,” Biotechnology Progress, 17(3), 577-582, 2001.
[38] A. J. Harvey, G. Speksnijder, L. R. Baugh, J. A. Morris, and R. Ivarie, “Expression of exogenous protein in the egg white of transgenic chickens,” Nature Biotechnology, 20(4), 396-399, 2002.
[39] T. S. Park, H. G. Lee, J. K. Moon, H. J. Lee, J. W. Yoon, B. N. Yun et al, “Deposition of bioactive human epidermal growth factor in the egg white of transgenic hens using an oviduct-specific minisynthetic promoter,” The FASEB Journal, 29(6), 2386-2396, 2015.
[40] Y. Wang, S. Zhao, L. Bai, J. Fan, and E. Liu, “Expression Systems and Species Used for Transgenic Animal Bioreactors,” BioMed Research International, 2013, 2013.
[41] E. Rehbinder, M. Engelhard, K. Hagen, and R. B. Jørgensen, R. Pardo-Avellaneda, A. Schnieke et al, “Promises and risks of biopharmaceuticals derived from genetically modified plants and animals,” Berlin: Springer-Verlag Berlin Heidelberg, 2009, p. 26.
[42] M. E. Swanson, M. J. Martin, J. K. O´Donnell, K. Hoover, W. Lago, V. Huntress et al, “Production of functional human hemoglobin in transgenic swine,” Biotechnology (N Y), 10(5), 557-559, 1992.
[43] V. G. Pursel, D. J. Bolt, K. F. Miller, C. A. Pinkert, R. E. Hammer, R. D. Palmiter et al, “Expression and performance in transgenic pigs,” Journal of Reproduction and Fertility. Supplement, 40, 235-245, 1990.
[44] D. E. Kerr, F. Liang, K. R. Bondioli, H. Zhao, G. Kreibich, R. J. Wall et al, “The bladder as a biorreactor: Urothelium production and secretion of growth hormone into urine,” Nature Biotechnology, 16 (1), 75-79, 1998.
[45] H. M. Zbikowska, N. Soukhareva, R. Behnam, R. Chang, R. Drews, H. Lubon et al, “The use of the uromodulin promoter to target production of recombinant proteins into urine of transgenic animals,” Transgenic Research, 11(4), 425-435, 2002.
[46] H. M. Zbikowska, N. Soukhareva, R. Behnam, H. Lubon, D. Hammond, and S. Soukharev, “Uromodulin promoter directs high-level expression of biologically active human α1-antitrypsin into mouse urine,” Biochemical Journal, 365 (Pt 1), 7-11, 2002.
[47] Z. Y. Ryoo, M. O. Kim, K. E. Kim, Y. Y. Bahk, J. W. Lee, S. H. Park et al, “Expression of recombinant human granulocyte macrophage-colony stimulating factor (hGM-CSF) in mouse urine,” Transgenic Research, 10(3), 193-200, 2001.
[48] P. Chrenek, A. V. Makarevich, J. Pivko, and J. Bulla, “Transgenic Farm Animal Production and Application,” Slovak Journal of Animal Science, 43(2): 45-49, 2010.
[49] L. R. Bertolini, H. Meade, C. R. Lazzarotto, L. T. Martins, K. C. Tavares, M. Bertolini et al, “The transgenic animal platform for biopharmaceutical production,” Transgenic Research, 25(3), 329-343, 2016.
[50] G. Wright, A. Carver, D. Cottom, D. Reeves, A. Scott, P. Simons et al, “High Level Expression of Active Human Alpha-1-Antitrypsin in the Milk of Transgenic Sheep,” Biotechnology (N Y), 9(9), 830-834, 1991.
[51] N. Rudolph, “Technologies and economics for protein production in transgenic animal milk”, Genetic Engineering News, 17(16), 36-37, 1997.
[52] H. Luboń and R. K. Paleyanda, “Vitamin K-dependent protein production in transgenic animals,” Thrombosis and Haemostasis, 78(1), 532-536.
[53] M. Tomita, H. Munetsuna, T. Sato, T. Adachi, R. Hino, M. Hayashi et al, “Transgenic silkworms produce recombinant human type III procollagen in cocoons,” Nature Biotechnology, 21(1), 52-56, 2003.
[54] S. Maeda, T. Kawai, M. Obinata, H. Fujiwara, T. Horuchi, Y. Saeki et al, “Production of human alpha-interferon in silkworm using a baculovirus vector,” Nature, 315 (6020), 592-594.
[55] M. Markaki, D. Drabek, I. Livadaras, R. K. Craig, F. Grosveld, and C. Savakis, “Stable expression of human growth hormone over 50 generations in transgenic insect larvae,” Transgenic Research, 16(1): 99-107, 2007.
[56] W. Gavin, “ATryn®: 1st GE (genetically engineered) animal success story for production of a human recombinant pharmaceutical,” BMC Proceedings, 8(Suppl 4), 2014.
[57] A. Sánchez y J. Gadea, “Animales transgénicos para la producción de proteínas humanas,” Anales de Veterinaria de Murcia, 30, 7-18, 2014.
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