Abstract
Prions are composed mainly, if not entirely, of PrP Sc, an infectious misfolded isoform of PrP C, the normal isoform of the prion protein. Here we show that protein misfolding cyclic amplification (PMCA)-generated hypertransmissible mink encephalopathy (HY TME) PrP Sc is highly infectious and has a titer that is similar, if not identical, to that associated with brain tissue from animals infected with the HY TME agent that are in the terminal stage of disease. These data demonstrate that PMCA efficiently replicates the prion agent and provide further support for the hypothesis that in vitro-generated prions are bona fide and are not due to contamination.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 13439-13442 |
| Number of pages | 4 |
| Journal | Journal of Virology |
| Volume | 85 |
| Issue number | 24 |
| DOIs | |
| State | Published - Dec 1 2011 |
All Science Journal Classification (ASJC) codes
- Microbiology
- Immunology
- Insect Science
- Virology
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Shikiya, R. A., & Bartz, J. C. (2011). Notes: In vitro generation of high-titer prions. Journal of Virology, 85(24), 13439-13442. https://doi.org/10.1128/JVI.06134-11