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Scientists identify prion's infectious secret

e recognition element’s amino acid sequence.

While this prion is a laboratory construct not found in nature, these findings provide researchers with a new way to approach old questions, such as why some prion diseases can jump from one species to another but others can’t. Tessier and Lindquist say it is likely that natural prions contain more than one recognition element, and recognition elements can slide into a neighboring region. Many external factors can determine which recognition element is activated, in turn influencing the downstream behavior of the prion.

"These findings are remarkable for two reasons," says Lindquist, who is also an investigator for Howard Hughes Medical Institute. "For one thing, this is the first time that these peptide arrays have been used to study protein folding. We’ve taken this platform to a whole new level. Also, we’ve seen just one small part of this prion inducing proteins to fold. This is an entirely new concept."

Earlier research from the Lindquist lab, published in Nature in 2005, identified the amino acid regions where prions connect with one another to form amyloids. Those interaction regions turn out to be the same regions Tessier identified as recognition elements?further confirmation that these regions are key to prion activity.

Tessier and his colleagues plan to further investigate this process in mammalian prions, such as those responsible for mad cow and Cruetzfeldt-Jakob diseases, as well as in other non-prion proteins that can also form amyloid structures.
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Source:Whitehead Institute for Biomedical Research


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