ISSN (Electrónico): 2590-5708
Formato: Electrónico / Acceso Abierto
Frecuencia: Números Anuales
Revisión por Pares: Doble Ciego
Keywords
Molecular farming
Heterologous proteins
Plant expression systems
Biosimilars
Plant suspension cells Agricultura molecular
Proteínas heterólogas
Sistemas de expresión vegetal
Biosimilares
Células vegetales en suspensión
Heterologous proteins
Plant expression systems
Biosimilars
Plant suspension cells Agricultura molecular
Proteínas heterólogas
Sistemas de expresión vegetal
Biosimilares
Células vegetales en suspensión
How to Cite
Nova López, C. J., Torres Bonilla, J. M., Mendoza Mesa, D. L., & Arango Isaza, R. E. (2024). Producción de proteínas recombinantes farmacéuticas en sistemas vegetales: Una mirada al Factor de crecimiento epidérmico humano (hEGF). Ciencia, Tecnología E Innovación En Salud, 8, 26–44. https://doi.org/10.23850/25393871.6211
Abstract
Recombinant proteins represent a crucial group of molecules for the treatment of many complex diseases afflicting humanity. Their production method involves not only DNA manipulation but also the utilization of biological production systems, including bacterial, mammalian, or insect cells. Despite the several advantages offered by plant-based or suspension-cultured plant cell production systems, the penetration of recombinant plant proteins into the pharmaceutical market remains low. This review presents the fundamental aspects of protein production technology using plant expression platforms, with a focus on advancements achieved in the production of recombinant human Epidermal Growth Factor (rhEGF), a model protein with pharmaceutical and cosmetic applications.
References
Ebrahimi SB, Samanta D. Engineering protein-based therapeutics through structural and chemical design. Nat Commun. 27 de abril de 2023;14(1):2411.
Lindskog EK, Fischer S, Wenger T, Schulz P. Chapter 6 - Host Cells. En: Jagschies G, Lindskog E, Łącki K, Galliher P, editores. Biopharmaceutical Processing [Internet]. Elsevier; 2018 [citado 22 de noviembre de 2019]. p. 111-30. Disponible en: http://www.sciencedirect.com/science/article/pii/B9780081006238000062
Eidenberger L, Kogelmann B, Steinkellner H. Plant-based biopharmaceutical engineering. Nat Rev Bioeng. 21 de marzo de 2023;1-14.
Fox JL. First plant-made biologic approved. Nat Biotechnol. 1 de junio de 2012;30(6):472-472.
Schillberg S, Raven N, Spiegel H, Rasche S, Buntru M. Critical Analysis of the Commercial Potential of Plants for the Production of Recombinant Proteins. Front Plant Sci [Internet]. 2019 [citado 23 de noviembre de 2019];10. Disponible en: https://www.frontiersin.org/articles/10.3389/fpls.2019.00720/full
Huang TK, Falk BW, Dandekar AM, McDonald KA. Enhancement of Recombinant Protein Production in Transgenic Nicotiana benthamiana Plant Cell Suspension Cultures with Co-Cultivation of Agrobacterium Containing Silencing Suppressors. Int J Mol Sci [Internet]. 24 de mayo de 2018 [citado 23 de noviembre de 2019];19(6). Disponible en: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6032394/
Takaiwa F. Increasing the production yield of recombinant protein in transgenic seeds by expanding the deposition space within the intracellular compartment. Bioengineered. 1 de mayo de 2013;4(3):136-9.
Habibi P, Prado GS, Pelegrini PB, Hefferon KL, Soccol CR, Grossi-de-Sa MF. Optimization of inside and outside factors to improve recombinant protein yield in plant. Plant Cell Tissue Organ Cult PCTOC. 1 de septiembre de 2017;130(3):449-67.
Yamamoto T, Hoshikawa K, Ezura K, Okazawa R, Fujita S, Takaoka M, et al. Improvement of the transient expression system for production of recombinant proteins in plants. Sci Rep. 19 de marzo de 2018;8(1):1-10.
Wilken LR, Nikolov ZL. Recovery and purification of plant-made recombinant proteins. Biotechnol Adv. abril de 2012;30(2):419-33.
Łojewska E, Kowalczyk T, Olejniczak S, Sakowicz T. Extraction and purification methods in downstream processing of plant-based recombinant proteins. Protein Expr Purif. abril de 2016;120:110-7.
Rozov SM, Permyakova NV, Deineko EV. Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins. Biochem Mosc. 1 de marzo de 2018;83(3):215-32.
Schoberer J, Strasser R. Plant glyco-biotechnology. Semin Cell Dev Biol. 2018;80:133-41.
de la Riva GA, González-Cabrera J, Vázquez-Padrón R, Ayra-Pardo C. Agrobacterium tumefaciens: a natural tool for plant transformation. Electron J Biotechnol. diciembre de 1998;1(3):24-5.
Hwang HH, Yu M, Lai EM. Agrobacterium-Mediated Plant Transformation: Biology and Applications. Arab Book [Internet]. octubre de 2017 [citado 23 de noviembre de 2019];2017(15). Disponible en: https://bioone.org/journals/The-Arabidopsis-Book/volume-2017/issue-15/tab.0186/Agrobacterium-Mediated-Plant-Transformation-Biology-and-Applications/10.1199/tab.0186.full
Naseri Z, Khezri G, Davarpanah SJ, Ofoghi H. Virus-Based Vectors: A New Approach for Production of Recombinant Proteins. J Appl Biotechnol Rep. 15 de marzo de 2019;6(1):6-14.
Davies HM. Review article: Commercialization of whole-plant systems for biomanufacturing of protein products: evolution and prospects. Plant Biotechnol J. 1 de octubre de 2010;8(8):845-61.
Firsov A, Shaloiko L, Kozlov O, Vinokurov L, Vainstein A, Dolgov S. Purification and characterization of recombinant supersweet protein thaumatin II from tomato fruit. Protein Expr Purif. 1 de julio de 2016;123:1-5.
Zhang H, Liu M, Li Y, Zhao Y, He H, Yang G, et al. Oral immunogenicity and protective efficacy in mice of a carrot-derived vaccine candidate expressing UreB subunit against Helicobacter pylori. Protein Expr Purif. febrero de 2010;69(2):127-31.
Hernández M, Cabrera-Ponce JL, Fragoso G, López-Casillas F, Guevara-García A, Rosas G, et al. A new highly effective anticysticercosis vaccine expressed in transgenic papaya. Vaccine. 22 de mayo de 2007;25(21):4252-60.
Concha C, Cañas R, Macuer J, Torres MJ, Herrada AA, Jamett F, et al. Disease Prevention: An Opportunity to Expand Edible Plant-Based Vaccines? Vaccines [Internet]. 30 de mayo de 2017 [citado 24 de noviembre de 2019];5(2). Disponible en: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5492011/
Lau OS, Sun SSM. Plant seeds as bioreactors for recombinant protein production. Biotechnol Adv. noviembre de 2009;27(6):1015-22.
Nykiforuk CL, Boothe JG, Murray EW, Keon RG, Goren HJ, Markley NA, et al. Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds. Plant Biotechnol J. enero de 2006;4(1):77-85.
Huang TK, McDonald KA. Bioreactor engineering for recombinant protein production in plant cell suspension cultures. Biochem Eng J. 15 de agosto de 2009;45(3):168-84.
Hellwig S, Drossard J, Twyman RM, Fischer R. Plant cell cultures for the production of recombinant proteins. Nat Biotechnol. noviembre de 2004;22(11):1415-22.
Xu J, Ge X, Dolan MC. Towards high-yield production of pharmaceutical proteins with plant cell suspension cultures. Biotechnol Adv. junio de 2011;29(3):278-99.
Tekoah Y, Shulman A, Kizhner T, Ruderfer I, Fux L, Nataf Y, et al. Large-scale production of pharmaceutical proteins in plant cell culture-the Protalix experience. Plant Biotechnol J. octubre de 2015;13(8):1199-208.
Medina-Bolívar F, Cramer C. Production of recombinant proteins by hairy roots cultured in plastic sleeve bioreactors. Methods Mol Biol Clifton NJ. 2004;267:351-63.
Yao Q, Yu Z, Liu P, Zheng H, Xu Y, Sai S, et al. High Efficient Expression and Purification of Human Epidermal Growth Factor in Arachis Hypogaea L. Int J Mol Sci. 25 de abril de 2019;20(8).
Fallah A, Akhavian A, Kazemi R, Jafari M, Salmanian AH. Production of Recombinant LSC Protein in Nicotiana tabacum Hairy Root: Direct vs. Indirect, a Comparison. J Appl Biotechnol Rep. 30 de marzo de 2018;5(1):1-7.
Lu Y, Oyler GA. Green algae as a platform to express therapeutic proteins. Discov Med. junio de 2009;8(40):28-30.
Dyo YM, Purton S. The algal chloroplast as a synthetic biology platform for production of therapeutic proteins. Microbiology. 2018;164(2):113-21.
Reski R, Parsons J, Decker EL. Moss‐made pharmaceuticals: from bench to bedside. Plant Biotechnol J. octubre de 2015;13(8):1191-8.
Pastores GM, Petakov M, Giraldo P, Rosenbaum H, Szer J, Deegan PB, et al. A Phase 3, multicenter, open-label, switchover trial to assess the safety and efficacy of taliglucerase alfa, a plant cell-expressed recombinant human glucocerebrosidase, in adult and pediatric patients with Gaucher disease previously treated with imiglucerase. Blood Cells Mol Dis. diciembre de 2014;53(4):253-60.
Farkash U, Avisar E, Volk I, Slevin O, Shohat N, El Haj M, et al. First clinical experience with a new injectable recombinant human collagen scaffold combined with autologous platelet-rich plasma for the treatment of lateral epicondylar tendinopathy (tennis elbow). J Shoulder Elbow Surg. marzo de 2019;28(3):503-9.
Qiu X, Wong G, Audet J, Bello A, Fernando L, Alimonti JB, et al. Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp. Nature [Internet]. 29 de agosto de 2014 [citado 7 de julio de 2015];advance online publication. Disponible en: http://www.nature.com/nature/journal/vnfv/ncurrent/full/nature13777.html
McCormick AA, Reddy S, Reinl SJ, Cameron TI, Czerwinkski DK, Vojdani F, et al. Plant-produced idiotype vaccines for the treatment of non-Hodgkin’s lymphoma: Safety and immunogenicity in a phase I clinical study. Proc Natl Acad Sci [Internet]. 21 de julio de 2008 [citado 7 de julio de 2015]; Disponible en: http://www.pnas.org/content/early/2008/07/18/0803636105
Shoji Y, Chichester JA, Jones M, Manceva SD, Damon E, Mett V, et al. Plant-based rapid production of recombinant subunit hemagglutinin vaccines targeting H1N1 and H5N1 influenza. Hum Vaccin. febrero de 2011;7 Suppl:41-50.
Whaley KJ, Hiatt A, Zeitlin L. Emerging antibody products and Nicotiana manufacturing. Hum Vaccin. marzo de 2011;7(3):349-56.
Fedosov SN, Laursen NB, Nexø E, Moestrup SK, Petersen TE, Jensen EØ, et al. Human intrinsic factor expressed in the plant Arabidopsis thaliana. Eur J Biochem. agosto de 2003;270(16):3362-7.
Thomas BR. Production of Therapeutic Proteins in Plants. 1 de diciembre de 2002 [citado 24 de noviembre de 2019]; Disponible en: https://escholarship.org/uc/item/5gp9s5r3
Day CD, Lee E, Kobayashi J, Holappa LD, Albert H, Ow DW. Transgene integration into the same chromosome location can produce alleles that express at a predictable level, or alleles that are differentially silenced. Genes Dev. 15 de noviembre de 2000;14(22):2869-80.
Gelvin SB. Integration of Agrobacterium T-DNA into the Plant Genome. Annu Rev Genet. 2017;51(1):195-217.
Kooter null, Matzke null, Meyer null. Listening to the silent genes: transgene silencing, gene regulation and pathogen control. Trends Plant Sci. septiembre de 1999;4(9):340-7.
Nugent JM, Joyce SM. Producing human therapeutic proteins in plastids. Curr Pharm Des. 2005;11(19):2459-70.
Khan MS, Joyia FA, Mustafa G. Seeds as Economical Production Platform for Recombinant Proteins. Protein Pept Lett. 2020;27(2):89-104.
Abrahamian P, Hammond RW, Hammond J. Plant Virus–Derived Vectors: Applications in Agricultural and Medical Biotechnology. Annu Rev Virol. 2020;7(1):513-35.
Avesani L, Merlin M, Gecchele E, Capaldi S, Brozzetti A, Falorni A, et al. Comparative analysis of different biofactories for the production of a major diabetes autoantigen. Transgenic Res. 1 de abril de 2014;23(2):281-91.
Gleba YY, Tusé D, Giritch A. Plant viral vectors for delivery by Agrobacterium. Curr Top Microbiol Immunol. 2014;375:155-92.
Klimyuk V, Pogue G, Herz S, Butler J, Haydon H. Production of recombinant antigens and antibodies in Nicotiana benthamiana using «magnifection» technology: GMP-compliant facilities for small- and large-scale manufacturing. Curr Top Microbiol Immunol. 2014;375:127-54.
Fischer R, Schillberg S, Hellwig S, Twyman RM, Drossard J. GMP issues for recombinant plant-derived pharmaceutical proteins. Biotechnol Adv. abril de 2012;30(2):434-9.
James E, Lee JM. The Production of Foreign Proteins from Genetically Modified Plant Cells. En: Zhong PDJJ, Byun SY, Cho GH, Choi JW, Haigh JR, Honda H, et al., editores. Plant Cells [Internet]. Springer Berlin Heidelberg; 2001 [citado 13 de septiembre de 2014]. p. 127-56. (Advances in Biochemical Engineering/Biotechnology). Disponible en: http://link.springer.com/chapter/10.1007/3-540-45302-4_5
Ponce. Propagación y mejora genética de plantas por biotecnología. Vol. 1. Cuba: Instituto de Biotecnología de las plantas; 1998. 390 p.
Xu J, Ge X, Dolan MC. Towards high-yield production of pharmaceutical proteins with plant cell suspension cultures. Biotechnol Adv. junio de 2011;29(3):278-99.
Xu J, Towler M, Weathers PJ. Platforms for Plant-Based Protein Production. En: Pavlov A, Bley T, editores. Bioprocessing of Plant In Vitro Systems [Internet]. Cham: Springer International Publishing; 2016 [citado 24 de noviembre de 2019]. p. 1-40. (Reference Series in Phytochemistry). Disponible en: https://doi.org/10.1007/978-3-319-32004-5_14-1
Shokri Gharelo R, Oliaei E, Bandehagh A, Khodadadi E, Motie Noparvar P. Production of therapeutic proteins through plant tissue and cell culture. J Biosci Biotechnol. 22 de marzo de 2016;5:93-104.
Häkkinen ST, Reuter L, Nuorti N, Joensuu JJ, Rischer H, Ritala A. Tobacco BY-2 Media Component Optimization for a Cost-Efficient Recombinant Protein Production. Front Plant Sci. 26 de enero de 2018;9:45-45.
Holland T, Sack M, Rademacher T, Schmale K, Altmann F, Stadlmann J, et al. Optimal nitrogen supply as a key to increased and sustained production of a monoclonal full-size antibody in BY-2 suspension culture. Biotechnol Bioeng. 1 de octubre de 2010;107(2):278-89.
Santos RB, Abranches R, Fischer R, Sack M, Holland T. Putting the Spotlight Back on Plant Suspension Cultures. Front Plant Sci [Internet]. 11 de marzo de 2016 [citado 24 de noviembre de 2019];7. Disponible en: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786539/
Corbin JM, Hashimoto BI, Karuppanan K, Kyser ZR, Wu L, Roberts BA, et al. Semicontinuous Bioreactor Production of Recombinant Butyrylcholinesterase in Transgenic Rice Cell Suspension Cultures. Front Plant Sci [Internet]. 31 de marzo de 2016 [citado 24 de noviembre de 2019];7. Disponible en: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4814504/
Raven N, Rasche S, Kuehn C, Anderlei T, Klöckner W, Schuster F, et al. Scaled-up manufacturing of recombinant antibodies produced by plant cells in a 200-L orbitally-shaken disposable bioreactor. Biotechnol Bioeng. febrero de 2015;112(2):308-21.
Huang LF, Tan CC, Yeh JF, Liu HY, Liu YK, Ho SL, et al. Efficient Secretion of Recombinant Proteins from Rice Suspension-Cultured Cells Modulated by the Choice of Signal Peptide. PLOS ONE. 16 de octubre de 2015;10(10):e0140812.
Li J, Hegeman CE, Hanlon RW, Lacy GH, Denbow DM, Grabau EA. Secretion of Active Recombinant Phytase from Soybean Cell-Suspension Cultures. Plant Physiol. 1 de julio de 1997;114(3):1103-11.
Huang TK, Plesha MA, McDonald KA. Semicontinuous bioreactor production of a recombinant human therapeutic protein using a chemically inducible viral amplicon expression system in transgenic plant cell suspension cultures. Biotechnol Bioeng. 15 de junio de 2010;106(3):408-21.
Bortesi L, Rademacher T, Schiermeyer A, Schuster F, Pezzotti M, Schillberg S. Development of an optimized tetracycline-inducible expression system to increase the accumulation of interleukin-10 in tobacco BY-2 suspension cells. BMC Biotechnol. 11 de julio de 2012;12:40.
Chilton MD, Tepfer DA, Petit A, David C, Casse-Delbart F, Tempé J. Agrobacterium rhizogenes inserts T-DNA into the genomes of the host plant root cells. Nature. febrero de 1982;295(5848):432-4.
Schmülling T, Schell J, Spena A. Single genes from Agrobacterium rhizogenes influence plant development. EMBO J. septiembre de 1988;7(9):2621-9.
Gaume A, Komarnytsky S, Borisjuk N, Raskin I. Rhizosecretion of recombinant proteins from plant hairy roots. Plant Cell Rep. agosto de 2003;21(12):1188-93.
Cardon F, Pallisse R, Bardor M, Caron A, Vanier J, Ele Ekouna JP, et al. Brassica rapa hairy root based expression system leads to the production of highly homogenous and reproducible profiles of recombinant human alpha-L-iduronidase. Plant Biotechnol J. 2019;17(2):505-16.
Rodriguez-Hernandez M, Triggiani D, Ivison F, Demurtas OC, Illiano E, Marino C, et al. Expression of a Functional Recombinant Human Glycogen Debranching Enzyme (hGDE) in N. benthamiana Plants and in Hairy Root Cultures. Protein Pept Lett. 14 de 2019;
Woods RR, Geyer BC, Mor TS. Hairy-root organ cultures for the production of human acetylcholinesterase. BMC Biotechnol. 23 de diciembre de 2008;8:95.
Carpenter G, Cohen S. Epidermal Growth Factor. Annu Rev Biochem. 1979;48(1):193-216.
Fernández-Montequín JI, Infante-Cristiá E, Valenzuela-Silva C, Franco-Pérez N, Savigne-Gutierrez W, Artaza-Sanz H, et al. Intralesional injections of Citoprot-P® (recombinant human epidermal growth factor) in advanced diabetic foot ulcers with risk of amputation. Int Wound J. 1 de diciembre de 2007;4(4):333-43.
Zheng J, Huang XY, Wei X. [The effects of epidermal growth factor on the wound healing of deep partial thickness burn in rats]. Zhonghua Shao Shang Za Zhi Zhonghua Shaoshang Zazhi Chin J Burns. octubre de 2003;19(5):289-92.
Liaño F, Teruel JL. Tratamiento de la necrosis tubular aguda. Rev Clínica Esp. 1 de marzo de 2001;201(3):145-7.
Martínez-carpio PA. El factor de crecimiento epidérmico cuarenta años después de su descubrimiento: de la bioquímica a la clínica. Endocrinol Nutr. 2003;50(8):334-44.
Schouest JM, Luu TK, Moy RL. Improved texture and appearance of human facial skin after daily topical application of barley produced, synthetic, human-like epidermal growth factor (EGF) serum. J Drugs Dermatol JDD. mayo de 2012;11(5):613-20.
Gold MH, Goldman MP, Biron J. Efficacy of novel skin cream containing mixture of human growth factors and cytokines for skin rejuvenation. J Drugs Dermatol JDD. febrero de 2007;6(2):197-201.
Gold MH, Goldman MP, Biron J. Efficacy of novel skin cream containing mixture of human growth factors and cytokines for skin rejuvenation. J Drugs Dermatol JDD. febrero de 2007;6(2):197-201.
Berlanga-Acosta J, Gavilondo-Cowley J, López-Saura P, González-López T, Castro-Santana MD, López-Mola E, et al. Epidermal growth factor in clinical practice – a review of its biological actions, clinical indications and safety implications. Int Wound J. 1 de octubre de 2009;6(5):331-46.
Eissazadeh S, Moeini H, Dezfouli MG, Heidary S, Nelofer R, Abdullah MP. Production of recombinant human epidermal growth factor in Pichia pastoris. Braz J Microbiol. 7 de abril de 2017;48(2):286-93.
Faizal A, Razis A, Ismail EN, Hambali Z, Nazrul M, Abdullah H, et al. The Periplasmic Expression of Recombinant Human Epidermal Growth Factor (hEGF) in Escherichia coli. 2006 [citado 21 de febrero de 2020]; Disponible en: http://citeseerx.ist.psu.edu/viewdoc/similar;jsessionid=1F801B3121FE5FC3AA5105FCC7C4C5DE?doi=10.1.1.549.9478&type=ab
Valdés J, Mantilla E, Márquez G, Bonilla RM, Lugo VM, Pérez M, et al. Incremento de la expresión del Factor de Crecimiento Epidérmico en Saccharomyces cerevisiae mediante la manipulación de las condiciones de cultivo. Biotecnol Apl. marzo de 2009;26(1):34-8.
Tong WY, Yao SJ, Zhu ZQ, Yu J. An improved procedure for production of human epidermal growth factor from recombinant E. coli. Appl Microbiol Biotechnol. diciembre de 2001;57(5-6):674-9.
Hanittinan O, Oo Y, Chaotham C, Rattanapisit K, Shanmugaraj B, Phoolcharoen W. Expression optimization, purification and in vitro characterization of human epidermal growth factor produced in Nicotiana benthamiana. Biotechnol Rep Amst Neth. diciembre de 2020;28:e00524.
Morgenfeld MM, Vater CF, Alfano EF, Boccardo NA, Bravo-Almonacid FF. Translocation from the chloroplast stroma into the thylakoid lumen allows expression of recombinant epidermal growth factor in transplastomic tobacco plants. Transgenic Res. junio de 2020;29(3):295-305.
Wang Y, Fan J, Wei Z, Xing S. Efficient expression of fusion human epidermal growth factor in tobacco chloroplasts. BMC Biotechnol. 7 de enero de 2023;23(1):1.
He Y, Schmidt MA, Erwin C, Guo J, Sun R, Pendarvis K, et al. Transgenic Soybean Production of Bioactive Human Epidermal Growth Factor (EGF). PLoS ONE [Internet]. 17 de junio de 2016 [citado 21 de septiembre de 2019];11(6). Disponible en: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4912142/
Zhi QW, Zhang FY, Chai M, Yu XH, Sun MJ. Success expression of human epidermal growth factor in transgenic tomato. Chin Pharmacol Bull. 1 de mayo de 2007;23:692+693-695.
Bai JY, Zeng L, Hu YL, Li YF, Lin ZP, Shang SC, et al. Expression and characteristic of synthetic human epidermal growth factor (hEGF) in transgenic tobacco plants. Biotechnol Lett. diciembre de 2007;29(12):2007-12.
Thomas D, Maree A. Improved expression of recombinant plant-made hEGF. Plant Cell Rep. 1 de noviembre de 2014;33(11):1801-14.
Wu CS, Kuo WT, Chang CY, Kuo JY, Tsai YT, Yu SM, et al. The modified rice αAmy8 promoter confers high-level foreign gene expression in a novel hypoxia-inducible expression system in transgenic rice seedlings. Plant Mol Biol. mayo de 2014;85(1-2):147-61.
Wirth S, Calamante G, Mentaberry A, Bussmann L, Lattanzi M, Barañao L, et al. Expression of active human epidermal growth factor (hEGF) in tobacco plants by integrative and non-integrative systems. Mol Breed. enero de 2004;13(1):23-35.
Su Z, Huang Y, Zhou Q, Wu Z, Wu X, Zheng Q, et al. High-level expression and purification of human epidermal growth factor with SUMO fusion in Escherichia coli. Protein Pept Lett. 2006;13(8):785-92.
Ishikawa T, Terai H, Kitajima T. Production of a biologically active epidermal growth factor fusion protein with high collagen affinity. J Biochem (Tokyo). abril de 2001;129(4):627-33.
Mauro VP. Codon Optimization in the Production of Recombinant Biotherapeutics: Potential Risks and Considerations. BioDrugs Clin Immunother Biopharm Gene Ther. febrero de 2018;32(1):69-81.
Laguía-Becher M, Martín V, Kraemer M, Corigliano M, Yacono ML, Goldman A, et al. Effect of codon optimization and subcellular targeting on Toxoplasma gondii antigen SAG1 expression in tobacco leaves to use in subcutaneous and oral immunization in mice. BMC Biotechnol. 15 de julio de 2010;10:52.
Parsons J, Wirth SA, Dominguez M, Bravo Almonacid FF, Giulietti AM, Rodriguez Talou J. Production of human epidermal growth factor (hEGF) by in vitro cultures of Nicotiana tabacum: effect of tissue differentiation and sodium nitroprusside addition. diciembre de 2010 [citado 4 de noviembre de 2019]; Disponible en: http://ri.conicet.gov.ar/handle/11336/15359
Diamos AG, Mason HS. Chimeric 3’ flanking regions strongly enhance gene expression in plants. Plant Biotechnol J. 2018;16(12):1971-82.
Allen GC, Spiker S, Thompson WF. Use of matrix attachment regions (MARs) to minimize transgene silencing. Plant Mol Biol. 1 de junio de 2000;43(2):361-76.
Moeller L, Gan Q, Wang K. A bacterial signal peptide is functional in plants and directs proteins to the secretory pathway. J Exp Bot. 1 de agosto de 2009;60(12):3337-52.
Ma Y, Yu J, Lin J, Wu S, Li S, Wang J. BioMed Research International. 2016 [citado 21 de septiembre de 2019]. High Efficient Expression, Purification, and Functional Characterization of Native Human Epidermal Growth Factor in Escherichia coli. Disponible en: https://www.hindawi.com/journals/bmri/2016/3758941/
Esipov RS, Stepanenko VN, Chupova LA, Boyarskikh UA, Filipenko ML, Miroshnikov AI. Production of recombinant human epidermal growth factor using Ssp dnaB mini-intein system. Protein Expr Purif. 1 de septiembre de 2008;61(1):1-6.
Zhang Y, Zhang K, Wan Y, Zi J, Wang Y, Wang J, et al. A pH-induced, intein-mediated expression and purification of recombinant human epidermal growth factor in Escherichia coli. Biotechnol Prog. 2015;31(3):758-64.
Shams D, Alizadeh M, Azari S, Hosseini S, Yasami-Khiabani S, Samani S, et al. High expression level of human epidermal growth factor (hEGF) using a well-designed fusion protein-tagged construct in E. coli. Bratisl Lek Listy. 2019;120(10):757-63.
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