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Brown team finds crucial protein role in deadly prion spread

ese ideas, Serio and members of her lab studied Sup35, a yeast protein similar to the human prion protein PrP. They put Sup35 together with Hsp104, then activated and deactivated Hsp104. They found that the protein does, indeed, chop up Sup35 complexes ?the first direct evidence that this process occurs in a living cell and that Hsp104 is the culprit.

"To understand how fragmentation speeds the spread of prions, think of a dandelion," Serio said. "A dandelion head is a cluster of flowers that each carries a seed. When the flower dries up and the wind blows, the seeds disperse. Prion protein works the same way. Hsp104 acts like the wind, blowing apart the flower and spreading the seeds."

Serio said that prions still multiply without fragmentation. However, she said, they do so at a much slower rate. So a drug that blocked the activity of Hsp104 could seriously slow progression of prion-related diseases.


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Source:Brown University


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