Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.

Previous studies identified two mammalian prion protein (PrP) polybasic domains that bind the disease-associated conformer PrP(Sc), suggesting that these domains of cellular prion protein (PrP(C)) serve as docking sites for PrP(Sc) during prion propagation. To examine the role of polybasic domains i...

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Bibliographic Details
Main Authors: Michael B Miller, James C Geoghegan, Surachai Supattapone
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-07-01
Series:PLoS Pathogens
Online Access:http://europepmc.org/articles/PMC3136465?pdf=render