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Volume 20, Number 1—January 2014

Research

Molecular Barriers to Zoonotic Transmission of Prions

Marcelo A. Barria, Aru Balachandran, Masanori Morita, Tetsuyuki Kitamoto, Rona Barron, Jean Manson, Richard Knight, James W. Ironside, and Mark W. HeadComments to Author 
Author affiliations: The University of Edinburgh, Edinburgh, Scotland, UK (M.A. Barria, R. Knight, J.W. Ironside, M.W Head); Canadian Food Inspection Agency, Ottawa, Ontario, Canada (A. Balachandran); Japan Blood Products Organization, Kobe, Japan (M. Morita); Tohoku University Graduate School of Medicine, Sendai, Japan (T. Kitamoto); University of Edinburgh, Easter Bush, Scotland, UK (R. Barron, J. Manson)

Main Article

Figure 6

PrPres typing of the CWD amplification product. The CWD PMCA product derived from amplification in a human brain homogenate substrate (PRNP codon 129MM) was compared by Western blotting with PrPres from human brain samples from cases of sCJD of the MM1 subtype, sCJD of the VV2 subtype, and variant CJD. The PrP detection antibody was 3F4. PrPres, protease-resistant prion protein; CWD, chronic wasting disease; PMCA, protein misfolding cyclic amplification; sCJD sporadic Creutzfeldt-Jakob disease;

Figure 6. . PrPres typing of the CWD amplification product. The CWD PMCA product derived from amplification in a human brain homogenate substrate (PRNP codon 129MM) was compared by Western blotting with PrPres from human brain samples from cases of sCJD of the MM1 subtype, sCJD of the VV2 subtype, and variant CJD. The PrP detection antibody was 3F4. PrPres, protease-resistant prion protein; CWD, chronic wasting disease; PMCA, protein misfolding cyclic amplification; sCJD sporadic Creutzfeldt-Jakob disease; vCJD, variant CJD; hu, human; M, molecular marker.

Main Article

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