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Nucleic Acids Research 2004 32(20):6120-6128; doi:10.1093/nar/gkh949
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Published online 23 November 2004

Nucleic Acids Research, Vol. 32 No. 20 © Oxford University Press 2004; all rights reserved

RNA aptamers selected against the receptor activator of NF-{kappa}B acquire general affinity to proteins of the tumor necrosis factor receptor family

Tadashi Mori, Akihiro Oguro1, Takashi Ohtsu1 and Yoshikazu Nakamura1,*

Research and Development Division, Mitsubishi Pharma Corporation, 1000, Kamoshida-cho, Aoba-ku, Yokohama 227-0033, Japan and 1 Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

* To whom correspondence should be addressed. Tel: +81 3 5449 5307; Fax: +81 3 5449 5415; Email: nak{at}ims.u-tokyo.ac.jp

Received October 12, 2004; Revised and Accepted October 31, 2004

The receptor activator of NF-{kappa}B (RANK) is a member of the tumor necrosis factor (TNF) receptor family and acts to cause osteoclastgenesis through the interaction with its ligand, RANKL. We isolated RNA aptamers with high affinity to human RANK by SELEX. Sequence and mutational analysis revealed that the selected RNAs form a G-quartet conformation that is crucial for binding to RANK. When the aptamer binding to RANK was challenged by RANKL, there was no competition between the aptamer and RANKL. Instead, the formation of a ternary complex, aptamer–RANK–RANKL, was detected by a spin down assay and by BIAcore surface plasmon resonance analysis. Moreover, the selected aptamer efficiently bound to other TNF receptor family proteins, such as TRAIL-R2, CD30, NGFR as well as osteoprotegerin, a decoy receptor for RANK. These results suggest that the selected aptamer recognizes not the ligand-binding site, but rather a common structure conserved in the TNF receptor family proteins.


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