Biology:List of recombinant proteins
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The following is a list of notable proteins that are produced from recombinant DNA, using biomolecular engineering.[1] In many cases, recombinant human proteins have replaced the original animal-derived version used in medicine. The prefix "rh" for "recombinant human" appears less and less in the literature. A much larger number of recombinant proteins is used in the research laboratory. These include both commercially available proteins (for example most of the enzymes used in the molecular biology laboratory), and those that are generated in the course specific research projects.
Human recombinants that largely replaced animal or harvested from human types
Medicinal applications
- Human growth hormone (rHGH): Humatrope from Lilly and Serostim from Serono replaced cadaver harvested human growth hormone
- human insulin (BHI): Humulin from Lilly and Novolin from Novo Nordisk among others largely replaced bovine and porcine insulin for human therapy. Some prefer to continue using the animal-sourced preparations, as there is some evidence that synthetic insulin varieties are more likely to induce hypoglycemia unawareness. Remaining manufacturers of highly purified animal-sourced insulin include the U.K.'s Wockhardt Ltd. (headquartered in India), Argentina's Laboratorios Beta S.A., and China's Wanbang Biopharma Co.
- Follicle-stimulating hormone (FSH) as a recombinant gonadotropin preparation replaced Serono's Pergonal which was previously isolated from post-menopausal female urine
- Factor VIII: Kogenate from Bayer replaced blood harvested factor VIII
Research applications
- Ribosomal proteins: For the studies of individual ribosomal proteins, the use of proteins that are produced and purified from recombinant sources[2][3][4][5] has largely replaced those that are obtained through isolation.[6][7] However, isolation is still required for the studies of the whole ribosome.[8][9]
- Lysosomal proteins: Lysosomal proteins are difficult to produce recombinantly due to the number and type of post-translational modifications that they have (e.g. glycosylation). As a result, recombinant lysosomal proteins are usually produced in mammalian cells.[10] Plant cell culture was used to produce FDA-approved glycosylated lysosomal protein-drug, and additional drug candidates.[11] Recent studies have shown that it may be possible to produce recombinant lysosomal proteins with microorganisms such as Escherichia coli and Saccharomyces cerevisiae.[12] Recombinant lysosomal proteins are used for both research and medical applications, such as enzyme replacement therapy.[13]
Human recombinants with recombination as only source
Medicinal applications
- Erythropoietin (EPO):[14] Epogen from Amgen
- Granulocyte colony-stimulating factor (G-CSF): filgrastim sold as Neupogen from Amgen; pegfilgrastim sold as Neulasta
- alpha-galactosidase A: Fabrazyme by Genzyme[15]
- alpha-L-iduronidase: (rhIDU; laronidase) Aldurazyme by BioMarin Pharmaceutical and Genzyme
- N-acetylgalactosamine-4-sulfatase (rhASB; galsulfase): Naglazyme by BioMarin Pharmaceutical
- Dornase alfa, a DNase sold under the trade name Pulmozyme by Genentech
- Tissue plasminogen activator (TPA) Activase by Genentech
- Glucocerebrosidase: Ceredase by Genzyme
- Interferon (IF) Interferon-beta-1a: Avonex from Biogen Idec; Rebif from Serono; Interferon beta-1b as Betaseron from Schering.[16] It is being investigated for the treatments of diseases including Guillain-Barré syndrome[17] and multiple sclerosis.[18]
- Insulin-like growth factor 1 (IGF-1)[19]
- Rasburicase, a Urate Oxidase analog sold as Elitek from Sanofi[20]
Animal recombinants
Medicinal applications
- Bovine somatotropin (bST)
- Porcine somatotropin (pST)
- Bovine Chymosin
Bacterial recombinants
Industrial applications
- Xylanases[21]
- Proteases, which have found applications in both the industrial (such as the food industry)[22] and domestic settings.[23]
Viral recombinants
Medicinal applications
- Envelope protein of the hepatitis B virus marketed as Engerix-B by SmithKline Beecham
- HPV Vaccine proteins
Plant recombinants
Research applications
- Polyphenol oxidases (PPOs): These include both catechol oxidases and tyrosinases.[24][25][26][27][28][29] In additional to research, PPOs have also found applications as biocatalysts.[30]
- Cystatins are proteins that inhibit cysteine proteases.[31][32][33][34] Research are ongoing to evaluate the potential of using cystatins in crop protection to control herbivorous pests and pathogens.[35]
Industrial applications
- Laccases have found a wide range of application, from food additive and beverage processing to biomedical diagnosis, and as cross‐linking agents for furniture construction or in the production of biofuels.[30][36][37][38][39]
- The tyrosinase‐induced polymerization of peptides offers facile access to artificial mussel foot protein analogues. Next generation universal glues can be envisioned that perform effectively even under rigorous seawater conditions and adapt to a broad range of difficult surfaces.[40]
See also
References
- ↑ "Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications" (in en). Biotechnology Journal 7 (5): 620–34. May 2012. doi:10.1002/biot.201100155. PMID 22442034.
- ↑ "An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli". Scientific Reports 9 (1): 8884. June 2019. doi:10.1038/s41598-019-45323-8. PMID 31222068. Bibcode: 2019NatSR...9.8884C.
- ↑ "Recombinant human ribosomal protein S16: expression, purification, refolding, and structural stability". Biochemistry. Biokhimiia 70 (7): 777–81. July 2005. doi:10.1007/s10541-005-0183-3. PMID 16097941.
- ↑ "Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26". Protein Expression and Purification 28 (1): 57–62. March 2003. doi:10.1016/S1046-5928(02)00652-6. PMID 12651107.
- ↑ "Overexpression in Escherichia coli, purification, and characterization of recombinant 60S ribosomal acidic proteins from Saccharomyces cerevisiae". Protein Expression and Purification 15 (1): 40–7. February 1999. doi:10.1006/prep.1998.0997. PMID 10024468.
- ↑ "Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26, S27', and S29". The Journal of Biological Chemistry 252 (24): 9071–80. December 1977. doi:10.1016/S0021-9258(17)38346-1. PMID 925037.
- ↑ "Extraction and isolation of individual ribosomal proteins from Escherichia coli". Journal of Bacteriology 96 (2): 358–64. August 1968. doi:10.1128/JB.96.2.358-364.1968. PMID 4877123.
- ↑ "Ribosome Purification Approaches for Studying Interactions of Regulatory Proteins and RNAs with the Ribosome" (in en). Bacterial Regulatory RNA. Methods in Molecular Biology. 905. 2012. pp. 273–89. doi:10.1007/978-1-61779-949-5_18. ISBN 978-1-61779-948-8.
- ↑ "Purification of ribosomes from human cell lines" (in en). Current Protocols in Cell Biology Chapter 3: Unit 3.40. December 2010. doi:10.1002/0471143030.cb0340s49. PMID 21154551.
- ↑ "Effects of lysosomal biotherapeutic recombinant protein expression on cell stress and protease and general host cell protein release in Chinese hamster ovary cells" (in en). Biotechnology Progress 33 (3): 666–676. May 2017. doi:10.1002/btpr.2455. PMID 28249362.
- ↑ "Large-scale production of pharmaceutical proteins in plant cell culture-the Protalix experience". Plant Biotechnology Journal 13 (8): 1199–208. October 2015. doi:10.1111/pbi.12428. PMID 26102075.
- ↑ "Human recombinant lysosomal enzymes produced in microorganisms" (in en). Molecular Genetics and Metabolism 116 (1–2): 13–23. 2015. doi:10.1016/j.ymgme.2015.06.001. PMID 26071627.
- ↑ "Lysosomal enzyme replacement therapies: Historical development, clinical outcomes, and future perspectives" (in en). Advanced Drug Delivery Reviews 118: 109–134. September 2017. doi:10.1016/j.addr.2017.05.004. PMID 28502768.
- ↑ "The production of recombinant human erythropoietin" (in en). Biotechnology Annual Review Volume 1. 1. 1995. pp. 297–313. doi:10.1016/S1387-2656(08)70055-3. ISBN 9780444818904.
- ↑ "Recombinant Interleukin-2 (rIL-2), aldesleukin" (in en). Journal of Biotechnology 95 (3): 277–80. May 2002. doi:10.1016/S0168-1656(02)00019-6. PMID 12007868.
- ↑ "Comparative pharmacokinetics and pharmacodynamics of recombinant human interferon beta-1a after intramuscular and subcutaneous administration" (in en). European Journal of Neurology 5 (2): 187–193. March 1998. doi:10.1046/j.1468-1331.1998.520187.x. PMID 10210831.
- ↑ "A randomized controlled trial of recombinant interferon-beta 1a in Guillain-Barré syndrome" (in en). Neurology 61 (9): 1282–4. November 2003. doi:10.1212/01.WNL.0000092019.53628.88. PMID 14610140.
- ↑ "Magnetic resonance imaging changes with recombinant human interferon-beta-1a: a short term study in relapsing-remitting multiple sclerosis" (in en). Journal of Neurology, Neurosurgery, and Psychiatry 61 (3): 251–8. September 1996. doi:10.1136/jnnp.61.3.251. PMID 8795595.
- ↑ "Expression, purification and characterization of recombinant human insulin-like growth factor I in yeast" (in en). Gene 66 (2): 235–44. June 1988. doi:10.1016/0378-1119(88)90360-5. PMID 3049246.
- ↑ "Efficacy and safety of rasburicase, a recombinant urate oxidase (Elitek), in the management of malignancy-associated hyperuricemia in pediatric and adult patients: final results of a multicenter compassionate use trial" (in en). Leukemia 19 (1): 34–8. January 2005. doi:10.1038/sj.leu.2403566. PMID 15510203.
- ↑ "Microbial xylanases: engineering, production and industrial applications" (in en). Biotechnology Advances 30 (6): 1219–27. 2012. doi:10.1016/j.biotechadv.2011.11.006. PMID 22138412.
- ↑ "Microbiology and Industrial Biotechnology of Food-Grade Proteases: A Perspective." (in en). Food Technology and Biotechnology 44: 211–220. 2006.
- ↑ "Detergent proteases" (in en). Current Opinion in Biotechnology 15 (4): 330–4. August 2004. doi:10.1016/j.copbio.2004.06.005. PMID 15296930.
- ↑ "An approach to recombinantly produce mature grape polyphenol oxidase" (in en). Biochimie 165: 40–47. October 2019. doi:10.1016/j.biochi.2019.07.002. PMID 31283975.
- ↑ "Purification and Characterization of Latent Polyphenol Oxidase from Apricot (Prunus armeniaca L.)" (in en). Journal of Agricultural and Food Chemistry 65 (37): 8203–8212. September 2017. doi:10.1021/acs.jafc.7b03210. PMID 28812349.
- ↑ "Recombinant expression, purification, and characterization of polyphenol oxidase 2 (VvPPO2) from "Shine Muscat" (Vitis labruscana Bailey × Vitis vinifera L.)" (in en). Bioscience, Biotechnology, and Biochemistry 81 (12): 2330–2338. December 2017. doi:10.1080/09168451.2017.1381017. PMID 29017399.
- ↑ "Recombinant Tyrosinase from Polyporus arcularius: Overproduction in Escherichia coli, Characterization, and Use in a Study of Aurones as Tyrosinase Effectors" (in en). Journal of Agricultural and Food Chemistry 64 (14): 2925–31. April 2016. doi:10.1021/acs.jafc.6b00286. PMID 26961852.
- ↑ "Parameters that enhance the bacterial expression of active plant polyphenol oxidases" (in en). PLOS ONE 8 (10): e77291. 2013. doi:10.1371/journal.pone.0077291. PMID 24204791. Bibcode: 2013PLoSO...877291D.
- ↑ "Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases". Scientific Reports 7 (1): 8860. August 2017. doi:10.1038/s41598-017-08097-5. PMID 28821733. Bibcode: 2017NatSR...7.8860K.
- ↑ 30.0 30.1 "Recent developments in the use of tyrosinase and laccase in environmental applications" (in en). Critical Reviews in Biotechnology 37 (7): 819–832. November 2017. doi:10.1080/07388551.2016.1261081. PMID 28330374.
- ↑ "Recombinant cystatins in plants" (in en). Biochimie 166: 184–193. November 2019. doi:10.1016/j.biochi.2019.06.006. PMID 31194996.
- ↑ "Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II" (in en). The Journal of Biological Chemistry 265 (26): 15832–7. September 1990. doi:10.1016/S0021-9258(18)55473-9. PMID 1697595.
- ↑ "Purification and Characterization of a Rice Cysteine Proteinase Inhibitor." (in en). Agricultural and Biological Chemistry 51 (10): 2763–2768. 1987. doi:10.1080/00021369.1987.10868462.
- ↑ "Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds" (in en). The Journal of Biological Chemistry 262 (35): 16793–7. December 1987. doi:10.1016/S0021-9258(18)45453-1. PMID 3500172.
- ↑ "Potential use of phytocystatins in crop improvement, with a particular focus on legumes" (in en). Journal of Experimental Botany 66 (12): 3559–70. June 2015. doi:10.1093/jxb/erv211. PMID 25944929.
- ↑ "Laccase: a multi-purpose biocatalyst at the forefront of biotechnology" (in en). Microbial Biotechnology 10 (6): 1457–1467. November 2017. doi:10.1111/1751-7915.12422. PMID 27696775.
- ↑ "Different recombinant forms of polyphenol oxidase A, a laccase from Marinomonas mediterranea" (in en). Protein Expression and Purification 123: 60–9. July 2016. doi:10.1016/j.pep.2016.03.011. PMID 27050199.
- ↑ "Uses of laccases in the food industry" (in en). Enzyme Research 2010: 918761. September 2010. doi:10.4061/2010/918761. PMID 21048873.
- ↑ "Potential applications of laccase in the food industry." (in en). Trends Food Sci. Technol. 13 (6–7): 205–216. 2002. doi:10.1016/S0924-2244(02)00155-3.
- ↑ "Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues". Angewandte Chemie 57 (48): 15728–15732. November 2018. doi:10.1002/anie.201809587. PMID 30246912.
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