Biotechnology Letters

, Volume 30, Issue 10, pp 1705–1711

Cloning and expression of a prion protein (PrP) gene from Korean bovine (Bos taurus coreanae) and production of rabbit anti-bovine PrP antibody


  • Wooseok Shin
    • Department of Genetic EngineeringSungkyunkwan University
  • Byungwoo Lee
    • Department of Genetic EngineeringSungkyunkwan University
  • Sungyoul Hong
    • Department of Genetic EngineeringSungkyunkwan University
  • Chongsuk Ryou
    • Sanders Brown Center on AgingUniversity of Kentucky
    • Department of Microbiology, Immunology and Molecular Genetics, College of MedicineUniversity of Kentucky
    • Department of Genetic EngineeringSungkyunkwan University
Original Research Paper

DOI: 10.1007/s10529-008-9768-4

Cite this article as:
Shin, W., Lee, B., Hong, S. et al. Biotechnol Lett (2008) 30: 1705. doi:10.1007/s10529-008-9768-4


A PrP gene, from a Korean bovine, exhibiting a nonsense and a missense polymorphism respectively at nucleotides 576 and 652 has been cloned. The latter resulted in Glu to Lys substitution at amino acid residue 218. After expression and purification of the recombinant bovine PrP (recBoPrP) with Glu218Lys substitution, a polyclonal antibody against this protein was raised. ELISA and Western blot analysis suggested that the recBoPrP obtained in this study had a unique conformation not presented in native PrPC, and the polyclonal antibody recognized PrP in a conformation dependent manner. These reagents will be valuable tools for studying PrP conformation.


Anti-bovine prion protein antibodyKorean bovinePrion proteinPrion protein gene

Copyright information

© Springer Science+Business Media B.V. 2008