Notes: In vitro generation of high-titer prions

Ronald A. Shikiya; Jason C. Bartz

doi:10.1128/JVI.06134-11

Notes: In vitro generation of high-titer prions

Ronald A. Shikiya, Jason C. Bartz

Department of Medical Microbiology and Immunology

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

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	https://doi.org/10.1128/JVI.06134-11
State	Published - Dec 2011

All Science Journal Classification (ASJC) codes

Microbiology
Immunology
Insect Science
Virology

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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.

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Notes: In vitro generation of high-titer prions

Abstract

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