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Dependence of RIG-I Nucleic Acid-Binding and ATP Hydrolysis on Activation of Type I Interferon Response
Immune Network ; : 249-255, 2016.
Article in English | WPRIM | ID: wpr-97829
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.
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Full text: Available Index: WPRIM (Western Pacific) Main subject: RNA / RNA, Double-Stranded / Nucleic Acids / Interferon Type I / Adenosine Triphosphate / Adenosine Triphosphatases / Hydrolysis / Immunity, Innate / Ligands Language: English Journal: Immune Network Year: 2016 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: RNA / RNA, Double-Stranded / Nucleic Acids / Interferon Type I / Adenosine Triphosphate / Adenosine Triphosphatases / Hydrolysis / Immunity, Innate / Ligands Language: English Journal: Immune Network Year: 2016 Type: Article