Dependence of RIG-I Nucleic Acid-Binding and ATP Hydrolysis on Activation of Type I Interferon Response.
- Author:
Yu Mi BAEK
1
;
Soojin YOON
;
Yeo Eun HWANG
;
Dong Eun KIM
Author Information
- Publication Type:Brief Communication
- Keywords: Retinoic acid inducible gene I (RIG-I); Interferon induction; 5'-terminal triphosphate; ATP hydrolysis; RNA binding
- MeSH: Adenosine Triphosphatases; Adenosine Triphosphate*; Hydrolysis*; Immunity, Innate; Interferon Type I*; Ligands; Nucleic Acids; RNA; RNA, Double-Stranded
- From:Immune Network 2016;16(4):249-255
- CountryRepublic of Korea
- Language:English
- Abstract: Exogenous nucleic acids induce an innate immune response in mammalian host cells through activation of the retinoic acid-inducible gene I (RIG-I). We evaluated RIG-I protein for RNA binding and ATPase stimulation with RNA ligands to investigate the correlation with the extent of immune response through RIG-I activation in cells. RIG-I protein favored blunt-ended, double-stranded RNA (dsRNA) ligands over sticky-ended dsRNA. Moreover, the presence of the 5'-triphosphate (5'-ppp) moiety in dsRNA further enhanced binding affinity to RIG-I. Two structural motifs in RNA, blunt ends in dsRNA and 5'-ppp, stimulated the ATP hydrolysis activity of RIG-I. These structural motifs also strongly induced IFN expression as an innate immune response in cells. Therefore, we suggest that IFN induction through RIG-I activation is mainly determined by structural motifs in dsRNA that increase its affinity for RIG-I protein and stimulate ATPase activity in RIG-I.
