tetano
Editor, Senior Moderator
Nucleic Acids Res. 2011 Nov 29. [Epub ahead of print]
5'-Triphosphate-RNA-independent activation of RIG-I via RNA aptamer with enhanced antiviral activity.
Hwang SY, Sun HY, Lee KH, Oh BH, Cha YJ, Kim BH, Yoo JY.
Source
Department of Life Sciences, Division of Molecular and Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Department of Life Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon and Department of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Abstract
RIG-I is a cytosolic receptor for non-self RNA that mediates immune responses against viral infections through IFNα/β production. In an attempt to identify novel tools that modulate IFNα/β production, we used SELEX technology to screen RNA aptamers that specifically target RIG-I protein. Most of the selected RIG-I aptamers contained polyU motifs in the second half regions that played critical roles in the activation of RIG-I-mediated IFNβ production. Unlike other known ligands, RIG-I aptamer bound and activated RIG-I in a 5'-triphosphate-independent manner. The helicase and RD domain of RIG-I were used for aptamer binding, but intact RIG-I protein was required to exert aptamer-mediated signaling activation. Furthermore, replication of NDV, VSV and influenza virus in infected host cells was efficiently blocked by pre- or post-treatment with RIG-I aptamer. Based on these data, we propose that RIG-I aptamer has strong potential to be an antiviral agent that specifically boosts the RIG-I-dependent signaling cascade.
PMID:
22127865
[PubMed - as supplied by publisher]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/22127865
5'-Triphosphate-RNA-independent activation of RIG-I via RNA aptamer with enhanced antiviral activity.
Hwang SY, Sun HY, Lee KH, Oh BH, Cha YJ, Kim BH, Yoo JY.
Source
Department of Life Sciences, Division of Molecular and Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Department of Life Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon and Department of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang, Republic of Korea.
Abstract
RIG-I is a cytosolic receptor for non-self RNA that mediates immune responses against viral infections through IFNα/β production. In an attempt to identify novel tools that modulate IFNα/β production, we used SELEX technology to screen RNA aptamers that specifically target RIG-I protein. Most of the selected RIG-I aptamers contained polyU motifs in the second half regions that played critical roles in the activation of RIG-I-mediated IFNβ production. Unlike other known ligands, RIG-I aptamer bound and activated RIG-I in a 5'-triphosphate-independent manner. The helicase and RD domain of RIG-I were used for aptamer binding, but intact RIG-I protein was required to exert aptamer-mediated signaling activation. Furthermore, replication of NDV, VSV and influenza virus in infected host cells was efficiently blocked by pre- or post-treatment with RIG-I aptamer. Based on these data, we propose that RIG-I aptamer has strong potential to be an antiviral agent that specifically boosts the RIG-I-dependent signaling cascade.
PMID:
22127865
[PubMed - as supplied by publisher]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/22127865