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.
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
Similar
MEDLINE
...
LILACS
LIS