Btn2p sequesters prion amyloid filaments, curing the prion.

<p>Btn2p gathers filaments of Ure2p amyloid (the [URE3] prion) to a single site in the cell, possibly the endosome. If the prion has a low seed number then even the normal levels of Btn2p are sufficient to sequester nearly all of the seeds, so that daughter cells without seeds, and therefore cured of the prion, are often produced.</p

Protein conformation templating mechanism.

<p>The in-register parallel amyloid architecture naturally suggests a mechanism for transfer of conformation information from molecules in the filament to those joining the filament. H-bonding or hydrophobic favorable interactions among identical side chains require in-register alignment for the interactions. This directs the monomer joining the end of the filament to have its folds/turns at the same residues as previous molecules in the filament. Different prion variants have folds/turns at different locations, but each is faithfully propagated by this mechanism. Modified from [<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004584#ppat.1004584.ref006" target="_blank">6</a>].</p