Large-scale production of recombinant human lactoferrin from high-expression, marker-free transgenic cloned cows
Human lactoferrin (hLF) is a valuable protein for pharmaceutical products and functional foods, and worldwide demand for this protein has steadily increased. However, large-scale recombinant human lactoferrin (rhLF) production using current animal bioreactor techniques is limited by the low expressi...
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Published in | Scientific reports Vol. 7; no. 1; pp. 10733 - 10 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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Nature Publishing Group
06.09.2017
Nature Publishing Group UK |
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Abstract | Human lactoferrin (hLF) is a valuable protein for pharmaceutical products and functional foods, and worldwide demand for this protein has steadily increased. However, large-scale recombinant human lactoferrin (rhLF) production using current animal bioreactor techniques is limited by the low expression of foreign proteins, the use of antibiotic resistance genes and the down-regulation of endogenous milk proteins. Here, we generated a herd of marker-free, hLF bacterial artificial chromosome (BAC) transgenic cloned cows, as confirmed by Polymerase chain reaction, Southern blot and Western blot analyses. These transgenic cloned cows produced rhLF in milk at concentrations of 4.5-13.6 g/L. Moreover, the total protein content of the milk was increased. Over two hundred transgenic cloned cows were propagated by multiple ovulation and embryo transfer (MOET). A total of 400-450 g of rhLF protein, which shows similar enzymatic activity to natural hLF in iron binding and release, can be purified on a large scale from >100 L of milk per day. Our results suggested that transgenic bovine mammary bioreactors have the potential for large-scale protein production. |
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AbstractList | Human lactoferrin (hLF) is a valuable protein for pharmaceutical products and functional foods, and worldwide demand for this protein has steadily increased. However, large-scale recombinant human lactoferrin (rhLF) production using current animal bioreactor techniques is limited by the low expression of foreign proteins, the use of antibiotic resistance genes and the down-regulation of endogenous milk proteins. Here, we generated a herd of marker-free, hLF bacterial artificial chromosome (BAC) transgenic cloned cows, as confirmed by Polymerase chain reaction, Southern blot and Western blot analyses. These transgenic cloned cows produced rhLF in milk at concentrations of 4.5–13.6 g/L. Moreover, the total protein content of the milk was increased. Over two hundred transgenic cloned cows were propagated by multiple ovulation and embryo transfer (MOET). A total of 400–450 g of rhLF protein, which shows similar enzymatic activity to natural hLF in iron binding and release, can be purified on a large scale from >100 L of milk per day. Our results suggested that transgenic bovine mammary bioreactors have the potential for large-scale protein production. Abstract Human lactoferrin (hLF) is a valuable protein for pharmaceutical products and functional foods, and worldwide demand for this protein has steadily increased. However, large-scale recombinant human lactoferrin (rhLF) production using current animal bioreactor techniques is limited by the low expression of foreign proteins, the use of antibiotic resistance genes and the down-regulation of endogenous milk proteins. Here, we generated a herd of marker-free, hLF bacterial artificial chromosome (BAC) transgenic cloned cows, as confirmed by Polymerase chain reaction, Southern blot and Western blot analyses. These transgenic cloned cows produced rhLF in milk at concentrations of 4.5–13.6 g/L. Moreover, the total protein content of the milk was increased. Over two hundred transgenic cloned cows were propagated by multiple ovulation and embryo transfer (MOET). A total of 400–450 g of rhLF protein, which shows similar enzymatic activity to natural hLF in iron binding and release, can be purified on a large scale from >100 L of milk per day. Our results suggested that transgenic bovine mammary bioreactors have the potential for large-scale protein production. |
ArticleNumber | 10733 |
Author | Li, Ning Fu, Mingbo Yu, Tian Li, Ling Huang, Jinming Dai, Yunping Wang, Haiping Sun, Zhaolin Ding, Fangrong Wang, Ming Wang, Xi |
Author_xml | – sequence: 1 givenname: Ming surname: Wang fullname: Wang, Ming organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China – sequence: 2 givenname: Zhaolin surname: Sun fullname: Sun, Zhaolin organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China – sequence: 3 givenname: Tian surname: Yu fullname: Yu, Tian organization: Kejienuo Biotechnology Company, Wuxi, China – sequence: 4 givenname: Fangrong surname: Ding fullname: Ding, Fangrong organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China – sequence: 5 givenname: Ling surname: Li fullname: Li, Ling organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China – sequence: 6 givenname: Xi surname: Wang fullname: Wang, Xi organization: Kejienuo Biotechnology Company, Wuxi, China – sequence: 7 givenname: Mingbo surname: Fu fullname: Fu, Mingbo organization: Kejienuo Biotechnology Company, Wuxi, China – sequence: 8 givenname: Haiping surname: Wang fullname: Wang, Haiping organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China – sequence: 9 givenname: Jinming surname: Huang fullname: Huang, Jinming organization: Dairy cattle Research Center, Academy of Agricultural Sciences, Shandong, China – sequence: 10 givenname: Ning surname: Li fullname: Li, Ning email: ninglcau@cau.edu.cn organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China. ninglcau@cau.edu.cn – sequence: 11 givenname: Yunping surname: Dai fullname: Dai, Yunping email: daiyunping@sina.com organization: State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China. daiyunping@sina.com |
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Snippet | Human lactoferrin (hLF) is a valuable protein for pharmaceutical products and functional foods, and worldwide demand for this protein has steadily increased.... Abstract Human lactoferrin (hLF) is a valuable protein for pharmaceutical products and functional foods, and worldwide demand for this protein has steadily... |
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StartPage | 10733 |
SubjectTerms | Antibiotic resistance Artificial chromosomes Bacterial artificial chromosomes Bioreactors Embryo transfer Enzymatic activity Gene regulation Lactoferrin Milk Nutrient content Ovulation Polymerase chain reaction Proteins |
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Title | Large-scale production of recombinant human lactoferrin from high-expression, marker-free transgenic cloned cows |
URI | https://www.ncbi.nlm.nih.gov/pubmed/28878310 https://www.proquest.com/docview/1957746135/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC5587717 |
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