구.농수식품
Yong-Chan Kim1,2, Kyung-Je Park3, Ji-Yong Hwang3, Hoo-Chang Park3, Hae-Eun Kang3, Hyun-Joo Sohn3,*, Byung-Hoon Jeong1,2,*
1Korea Zoonosis Research Institute, Jeonbuk National University, Iksan, Republic of Korea
2Department of Bioactive Material Sciencesand Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju, Republic of Korea
3Reference Laboratory for CWD, Foreign Animal Disease Division, Animal and Plant Quarantine Agency, Gimcheon, Republic of Korea
*Correspondence :
Byung-Hoon Jeong, Korea Zoonosis ResearchInstitute, Jeonbuk National University, 820-120, Hana-ro, Iksan, Jeonbuk 54531, Republicof Korea
Hyun-Joo Sohn, Reference Laboratory for CWD, ForeignAnimal Disease Division, Animal and Plant Quarantine Agency, Gimcheon, 39660, Republic of Korea
Abstract
Prion diseases are transmissible spongiform encephalopathies caused by deleterious prion protein (PrPSc) derived from normal prion protein (PrPC), which is encoded by the prion protein gene (PRNP). We performed an in-depth examination to detect PrPSc by using enzyme immunoassay (EIA), real-time quaking-induced conversion reactions (RT-QuIC) and protein misfolding cyclic amplification (PMCA) in nine brain tissues derived from three Holstein cattle carrying the E211K somatic mutation of the bovine PRNP gene. The EIA, RT-QuIC and PMCA analyses were not able to detect the PrPSc band in any tested samples. To the best of our knowledge, this report is the first to describe an in-depth examination of PrPSc in cattle carrying the E211K somatic mutation of the bovine PRNP gene.
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