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KMID : 0380420100340040293
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Journal of Prventive Veterinary Medicine
2010 Volume.34 No. 4 p.293 ~ p.300
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xpression, purification, and characterization of Elk recombinant prion protein
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Kim Hyo-Jin
Lee Yoon-Hee
Jeoung Hye-Young
Kim Min-Jeong
Tark Dong-Seob
Cho In-Soo
Sohn Hyun-Joo
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Abstract
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Abnormal prions are infectious agents involved in a neuro-degenerative disease, which occurs naturally such as Chronic Wasting Disease (CWD) in deer and elk, Bovine Spongiform Encephalopathy (BSE) in cattle, Scrapie in sheep and goats and Creutzfeldt-Jakob Disease (CJD) in humans. The cellular prion protein of the elk consists of 233 amino acids (residues 25-257), which represents an autonomous folding unit with three α-helices and two-stranded anti-parallel β-sheets. Here, we demonstrated elk-recPrP (Elk recombinant prion protein) which can be obtained as follows; (1) Cloning of elk PrP gene, (2) Expression of a histidine-tagged full-length elk PrP by induction with IPTG in E. coli and (3) Purification by affinity chromatography using Ni-NTA agarose resin. In Western blot and ELISA analysis, elk-recPrP showed specific activity against anti-PrP monoclonal antibody. Thus, our elk-recPrP would be a useful tool for the understanding of basic structure and mechanism studies of PrPSC formation.
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KEYWORD
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Prion, Recombinant PrP, elk, CWD, TSE
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