Volume 24, Number 8—August 2018
Research
Susceptibility of Human Prion Protein to Conversion by Chronic Wasting Disease Prions
Figure 5

Figure 5. Schematic representation of the partial purification of misfolded, disease-associated prion protein from chronic wasting disease (CWD)–affected deer brain specimens and its continued ability to seed the conversion of human prion protein (PrP) during protein misfolding cyclic amplification (PMCA) reactions. We normalized PrP, partially purified by detergent insolubility from reindeer and white-tailed deer CWD specimens, by using protease-resistant prion protein (PrPres) and subjected PrP to a single round of PMCA in humanized transgenic PRNP codon 129 homozygous methionine. We performed Western blot analysis by using mAb 3F4 (for detection of human PrPres) and mAb 6H4 (for detection of CWD PrPres and human PrPres). Molecular mass of electrophoretic markers is given. Odd and even number lanes show reaction mixtures before and after PMCA. mAb, monoclonal antibody; PMCA, protein misfolding cyclic amplification; PrPc, normal isoform of the prion protein; PrPsc, disease-associated isoform of the prion protein.