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Amyloid Aggregates of the HET-s Prion Protein are Infectious

Marie-Lise Maddelein, Suzana Dos Reis, Stéphane Duvezin-Caubet, Bénédicte Coulary-Salin and Sven J. Saupe
Proceedings of the National Academy of Sciences of the United States of America
Vol. 99, No. 11 (May 28, 2002), pp. 7402-7407
Stable URL: http://www.jstor.org/stable/3058837
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Amyloid Aggregates of the HET-s Prion Protein are Infectious
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Abstract

The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion. We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo, the protein aggregates specifically in the [Het-s] prion strains. Here, we show that biolistic introduction of aggregated recombinant HET-s protein into fungal cells induces emergence of the [Het-s] prion with a high frequency. Thus, we demonstrate that prion infectivity can be created de novo, in vitro from recombinant protein in this system. Although the amyloid filaments formed from HET-s could transmit [Het-s] efficiently, neither the soluble form of the protein nor amorphous aggregates would do so. In addition, we have found that (i) [Het-s] infectivity correlates with the ability to convert HET-s to amyloids in vitro, (ii) [Het-s] infectivity is resistant to proteinase K digestion, and (iii) HET-s aggregates formed in vivo in [Het-s] strains have the ability to convert the recombinant protein to aggregates. Together, our data designate the HET-s amyloids as the molecular basis of [Het-s] prion propagation.

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