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 |
|---|---|
| Pages (from-to) | 13439-13442 |
| Number of pages | 4 |
| Journal | Journal of Virology |
| Volume | 85 |
| Issue number | 24 |
| DOIs | |
| State | Published - Dec 2011 |
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All Science Journal Classification (ASJC) codes
- Immunology
- Virology
Cite this
Notes : In vitro generation of high-titer prions. / Shikiya, Ronald A.; Bartz, Jason C.
In: Journal of Virology, Vol. 85, No. 24, 12.2011, p. 13439-13442.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Notes
T2 - In vitro generation of high-titer prions
AU - Shikiya, Ronald A.
AU - Bartz, Jason C.
PY - 2011/12
Y1 - 2011/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84855857565&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84855857565&partnerID=8YFLogxK
U2 - 10.1128/JVI.06134-11
DO - 10.1128/JVI.06134-11
M3 - Article
C2 - 21957291
AN - SCOPUS:84855857565
VL - 85
SP - 13439
EP - 13442
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 24
ER -