10.1371/journal.ppat.1002128.g006 Michael B. Miller Michael B. Miller James C. Geoghegan James C. Geoghegan Surachai Supattapone Surachai Supattapone Model of PrP replicative interaction mechanisms. Public Library of Science 2011 prp replicative 2011-07-14 02:11:26 Figure https://plos.figshare.com/articles/figure/_Model_of_PrP_replicative_interaction_mechanisms_/427886 <p>This diagram summarizes a proposed model for the interaction, propagation, and infectivity behavior of wild-type and polybasic deletion mutant PrP molecules. Wild-type PrP<sup>Sc</sup> seed binds and propagates efficiently with autologous PrP<sup>C</sup> substrate, using PrP<sup>C</sup> polybasic domains (represented by rectangular protrusion) for docking. However, if PrP<sup>C</sup> lacks one or both polybasic domains, PrP<sup>Sc</sup> binds less well and exhibits impaired propagation. If PrP<sup>Sc</sup> molecules lacking polybasic domains can be formed, they can bind and propagate efficiently with an expanded range of PrP<sup>C</sup> substrates. ΔPBD-PrP<sup>Sc</sup> may propagate by a different mechanism than wild-type PrP<sup>Sc</sup>, utilizing different residues (symbolized by round protrusion) of PrP<sup>C</sup> for binding. A neoepitope (round depression) may be exposed in the polybasic mutant PrP<sup>Sc</sup> molecules. Legend: Sc = PrP<sup>Sc</sup>; C = PrP<sup>C</sup>; WT = wild-type. ΔPBD = deletion in polybasic domain; ++ = polybasic domain.</p>