Author: ["Eustache Paramithiotis","Marc Pinard","Trebor Lawton","Sylvie LaBoissiere","Valerie L Leathers","Wen-Quan Zou","Lisa A Estey","Julie Lamontagne","Marty T Lehto","Leslie H Kondejewski","Gregory P Francoeur","Maria Papadopoulos","Ashkan Haghighat","Stephen J Spatz","Mark Head","Robert Will","James Ironside","Katherine O'Rourke","Quentin Tonelli","Harry C Ledebur","Avi Chakrabartty","Neil R Cashman"]
CITE.CC academic search helps you expand the influence of your papers.
Abstract
Conformational conversion of proteins in disease is likely to be accompanied by molecular surface exposure of previously sequestered amino-acid side chains. We found that induction of β-sheet structures in recombinant prion proteins is associated with increased solvent accessibility of tyrosine. Antibodies directed against the prion protein repeat motif, tyrosine-tyrosine-arginine, recognize the pathological isoform of the prion protein but not the normal cellular isoform, as assessed by immunoprecipitation, plate capture immunoassay and flow cytometry. Antibody binding to the pathological epitope is saturable and specific, and can be created in vitro by partial denaturation of normal brain prion protein. Conformation-selective exposure of Tyr-Tyr-Arg provides a probe for the distribution and structure of pathologically misfolded prion protein, and may lead to new diagnostics and therapeutics for prion diseases.Cite this article
Paramithiotis, E., Pinard, M., Lawton, T. et al. A prion protein epitope selective for the pathologically misfolded conformation. Nat Med 9, 893–899 (2003). https://doi.org/10.1038/nm883 