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>