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Title: Anti-prion activity of an RNA aptamer and its structural basis.
Authors: Mashima, Tsukasa  kyouindb  KAKEN_id
Nishikawa, Fumiko
Kamatari, Yuji O
Fujiwara, Hiromichi
Saimura, Masayuki
Nagata, Takashi  kyouindb  KAKEN_id  orcid (unconfirmed)
Kodaki, Tsutomu  kyouindb  KAKEN_id
Nishikawa, Satoshi
Kuwata, Kazuo
Katahira, Masato  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 片平, 正人
Issue Date: Jan-2013
Publisher: Oxford University Press
Journal title: Nucleic acids research
Volume: 41
Issue: 2
Start page: 1355
End page: 1362
Abstract: Prion proteins (PrPs) cause prion diseases, such as bovine spongiform encephalopathy. The conversion of a normal cellular form (PrP(C)) of PrP into an abnormal form (PrP(Sc)) is thought to be associated with the pathogenesis. An RNA aptamer that tightly binds to and stabilizes PrP(C) is expected to block this conversion and to thereby prevent prion diseases. Here, we show that an RNA aptamer comprising only 12 residues, r(GGAGGAGGAGGA) (R12), reduces the PrP(Sc) level in mouse neuronal cells persistently infected with the transmissible spongiform encephalopathy agent. Nuclear magnetic resonance analysis revealed that R12, folded into a unique quadruplex structure, forms a dimer and that each monomer simultaneously binds to two portions of the N-terminal half of PrP(C), resulting in tight binding. Electrostatic and stacking interactions contribute to the affinity of each portion. Our results demonstrate the therapeutic potential of an RNA aptamer as to prion diseases.
Rights: © The Author(s) 2012. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact
DOI(Published Version): 10.1093/nar/gks1132
PubMed ID: 23180780
Appears in Collections:Journal Articles

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