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Editor, Senior Moderator
Mol Cells. 2019 Oct 10. doi: 10.14348/molcells.2019.0157. [Epub ahead of print] [h=1]Recovery of TRIM25-Mediated RIG-I Ubiquitination through Suppression of NS1 by RNA Aptamers.[/h]
Woo HM[SUP]1,[/SUP][SUP]2,[/SUP][SUP]3[/SUP], Lee JM[SUP]1,[/SUP][SUP]4,[/SUP][SUP]3[/SUP], Kim CJ[SUP]5[/SUP], Lee JS[SUP]5[/SUP], Jeong YJ[SUP]1[/SUP].
[h=3]Author information[/h] 1 School of Applied Chemistry, Kookmin University, Seoul 02707, Korea. 2 Division of Emerging Infectious Disease and Vector Research, Korea National Institute of Health, Cheongju 28159, Korea. 3 These authors contributed equally to this work. 4 Pharmacological Research Division, National Institute of Food and Drug Safety Evaluation, Cheongju 28159, Korea. 5 College of Veterinary Medicine, Chungnam National University, Daejeon 34134, Korea.
[h=3]Abstract[/h] Non-structural protein 1 (NS1) of influenza virus has been shown to inhibit the innate immune response by blocking the induction of interferon (IFN). In this study, we isolated two single-stranded RNA aptamers specific to NS1 with Kd values of 1.62 ? 0.30 nM and 1.97 ? 0.27 nM, respectively, using a systematic evolution of ligand by exponential enrichment (SELEX) procedure. The selected aptamers were able to inhibit the interaction of NS1 with tripartite motif-containing protein 25 (TRIM25), and suppression of NS1 enabled retinoic acid inducible gene I (RIG-I) to be ubiquitinated regularly by TRIM25. Additional luciferase reporter assay and quantitative real-time PCR (RT-PCR) experiments demonstrated that suppression of NS1 by the selected aptamers induced IFN production. It is noted that viral replication was also inhibited through IFN induction in the presence of the selected aptamers. These results suggest that the isolated aptamers are strongly expected to be new therapeutic agents against influenza infection.
[h=4]KEYWORDS:[/h] aptamer; influenza virus; non-structural 1; systematic evolution of ligands by exponential enrichment; ubiquitination
PMID: 31600868 DOI: 10.14348/molcells.2019.0157
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Woo HM[SUP]1,[/SUP][SUP]2,[/SUP][SUP]3[/SUP], Lee JM[SUP]1,[/SUP][SUP]4,[/SUP][SUP]3[/SUP], Kim CJ[SUP]5[/SUP], Lee JS[SUP]5[/SUP], Jeong YJ[SUP]1[/SUP].
[h=3]Author information[/h] 1 School of Applied Chemistry, Kookmin University, Seoul 02707, Korea. 2 Division of Emerging Infectious Disease and Vector Research, Korea National Institute of Health, Cheongju 28159, Korea. 3 These authors contributed equally to this work. 4 Pharmacological Research Division, National Institute of Food and Drug Safety Evaluation, Cheongju 28159, Korea. 5 College of Veterinary Medicine, Chungnam National University, Daejeon 34134, Korea.
[h=3]Abstract[/h] Non-structural protein 1 (NS1) of influenza virus has been shown to inhibit the innate immune response by blocking the induction of interferon (IFN). In this study, we isolated two single-stranded RNA aptamers specific to NS1 with Kd values of 1.62 ? 0.30 nM and 1.97 ? 0.27 nM, respectively, using a systematic evolution of ligand by exponential enrichment (SELEX) procedure. The selected aptamers were able to inhibit the interaction of NS1 with tripartite motif-containing protein 25 (TRIM25), and suppression of NS1 enabled retinoic acid inducible gene I (RIG-I) to be ubiquitinated regularly by TRIM25. Additional luciferase reporter assay and quantitative real-time PCR (RT-PCR) experiments demonstrated that suppression of NS1 by the selected aptamers induced IFN production. It is noted that viral replication was also inhibited through IFN induction in the presence of the selected aptamers. These results suggest that the isolated aptamers are strongly expected to be new therapeutic agents against influenza infection.
[h=4]KEYWORDS:[/h] aptamer; influenza virus; non-structural 1; systematic evolution of ligands by exponential enrichment; ubiquitination
PMID: 31600868 DOI: 10.14348/molcells.2019.0157
Free full text