Adenoviral Vector Mediates High Expression Levels of Human Lactoferrin in the Milk of Rabbits

  • Han, Zeng-Sheng (Department of Biological Engineering, College of Environment and Chemical Engineering, Yanshan University) ;
  • Li, Qing-Wang (Department of Biological Engineering, College of Environment and Chemical Engineering, Yanshan University) ;
  • Zhang, Zhi-Ying (College of Animal Science and Veterinary Medicine, Northwest A&F University) ;
  • Yu, Yong-Sheng (College of Animal Science and Veterinary Medicine, Northwest A&F University) ;
  • Xiao, Bo (College of Animal Science and Veterinary Medicine, Northwest A&F University) ;
  • Wu, Shu-Yun (College of Animal Science and Veterinary Medicine, Northwest A&F University) ;
  • Jiang, Zhong-Liang (College of Animal Science and Veterinary Medicine, Northwest A&F University) ;
  • Zhao, Hong-Wei (Department of Biological Engineering, College of Environment and Chemical Engineering, Yanshan University) ;
  • Zhao, Rui (Department of Biological Engineering, College of Environment and Chemical Engineering, Yanshan University) ;
  • Li, Jian (Department of Biological Engineering, College of Environment and Chemical Engineering, Yanshan University)
  • Published : 2008.01.31

Abstract

The limitations in current technology for generating transgenic animals, such as the time and the expense, hampered its extensive use in recombinant protein production for therapeutic purpose. In this report, we present a simple and less expensive alternative by directly infusing a recombinant adenovirus vector carrying human lactoferrin cDNA into rabbit mammary glands. The milk serum was collected from the infected mammary gland 48 h post-infection and subjected to a 10% SDS-PAGE and Western blotting. An 80-kDa protein was visualized after viral vector infection. With this method, we obtained a high level of expressed human lactoferrin of up to 2.3mg/ml in the milk. Taken together, the method is useful for the transient high-level expression recombinant proteins, and the approach established here is probably one of the most economical and efficient ways for large-scale production of recombinant proteins of biopharmaceutical interest.

Keywords

References

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