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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 3

Susceptibility of human brain, humanized transgenic mice brain, and 293F cell extract PrPC to in vitro conversion by CWD brain homogenate. PMCA seeded with serial dilutions of CWD brain homogenate (1:6, 1:12, and 1:24) were mixed with substrate from 3 different sources: human brain homogenate (A, D); transgenic mice that express the human PrP (B, E); and 293F human cell extract (C, F). The substrates contained human PrP 129M (A–C) or PrP 129V (D–F). These same substrates were seeded with vCJD br

Figure 3. . Susceptibility of human brain, humanized transgenic mice brain, and 293F cell extract PrPC to in vitro conversion by CWD brain homogenate. PMCA seeded with serial dilutions of CWD brain homogenate (1:6, 1:12, and 1:24) were mixed with substrate from 3 different sources: human brain homogenate (A, D); transgenic mice that express the human PrP (B, E); and 293F human cell extract (C, F). The substrates contained human PrP 129M (A–C) or PrP 129V (D–F). These same substrates were seeded with vCJD brain homogenate at 1:100 (G). Odd-numbered lanes show the samples without PMCA. Even-numbered lanes were subjected to PMCA. The PrP detection antibody was 3F4. PrPc, normal cellular prion protein; CWD, chronic wasting disease; PMCA, protein misfolding cyclic amplification; vCJD variant Creutzfeldt-Jakob disease.

Main Article

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