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10.7554/eLife.02949.007 Figure 4. E. coli can propagate the Sup35 NM prion over ∼100 generations.
More specifically, we demonstrate maintenance of the Sup35 NM prion over multiple rounds of restreaking in E. coli cells no longer capable of synthesizing the New1 protein.
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The objectives of this study were to evaluate differences in prion adsorption and replication efficiency as a function of adsorption solution and to evaluate desorption and replication of soil-bound prions over time periods up to 1 year.
The study design was meant to mirror the daily habits and movements of a deer in its natural setting in which it may return to an area contaminated with small amounts of infectious prions over time.
Once that happens, the prion form takes over rapidly.
(And the fight is real: While kuru has faded and mad cow is contained, the number of people exposed to prion contamination over the years, who may now be dormant carriers, suggests we're headed down a road of pain and confusion in the future for which we have few medical tools).
In our model, animals released between 52 and 160 (mean = 106) infectious prion units over their infectious lifetime and 100 prion units upon death.
Exposure of RML brain homogenate to 1 mg/ml pronase E led to a rapid decrease in prion titre over time and after a 60 min digestion only ∼10% of the starting infectivity remained (Figure 3).
No inoculated mice showed clinical signs of prion disease over their normal lifespan (up to 857 dpi) (Table 4).
We conclude that E. coli cells can propagate Sup35 NM in an infectious prion conformation over at least ∼100 generations under conditions that do not permit de novo prion formation.
Yuan et al. now reveal that the bacterium Escherichia coli can propagate a yeast prion for over a hundred generations, even when the cells can no longer make the protein that serves as the trigger for the initial conversion.
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