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Scientists identify prion's infectious secret

of tiny protein fragments. Traditionally, these arrays are used for finding binding sites within well-behaved proteins. Here, Tessier designed the arrays so that he could observe protein folding and amyloid formation in real time.

Tessier covered the array with peptides from baker’s yeast and then added prion protein to the array, also from the same yeast species. He found that a small cluster of peptides recruited the prion proteins to misfold into an amyloid structure. This region of the protein, which Tessier called a "recognition element," constitutes about 10 percent of the prion. Tessier repeated this experiment with peptides and a prion taken from pathogenic fungi. The results were the same.

Both prions also maintained a rigid species barrier. The baker’s yeast prion could not recruit peptides from the pathogenic fungi cells, and vice versa.

To further verify these results, Tessier accessed a synthetic yeast prion, one that another research group had assembled from pieces of both the baker’s yeast and the pathogenic fungi prion. Earlier studies had shown that this synthetic prion could cross the species barrier but did not identify the mechanism. Tessier found that this synthetic prion contained two recognition elements, one for baker’s yeast and one for pathogenic fungi. When the prion was placed with peptide fragments from baker’s yeast, the baker’s yeast recognition element was activated, and likewise for the pathogenic fungi.

Even more striking, Tessier could activate different recognition elements by manipulating environmental conditions, such as temperature. For example, when he conducted the experiment at 4 degrees Celsius, the baker’s yeast recognition element switched on. At 37 degrees Celsius, the pathogenic fungi element was activated. In other words, temperature alone could dictate which yeast species the prion could infect. Additionally, the prion’s behavior could be altered by subtle alterations in th
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Source:Whitehead Institute for Biomedical Research


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