ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon.

Abstract:

:The cytosolic pathogen sensor RIG-I is activated by RNAs with exposed 5'-triphosphate (5'-ppp) and terminal double-stranded structures, such as those that are generated during viral infection. RIG-I has been shown to translocate on dsRNA in an ATP-dependent manner. However, the precise role of the ATPase activity in RIG-I activation remains unclear. Using in vitro-transcribed Sendai virus defective interfering RNA as a model ligand, we show that RIG-I oligomerizes on 5'-ppp dsRNA in an ATP hydrolysis-dependent and dsRNA length-dependent manner, which correlates with the strength of type-I interferon (IFN-I) activation. These results establish a clear role for the ligand-induced ATPase activity of RIG-I in the stimulation of the IFN response.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Patel JR,Jain A,Chou YY,Baum A,Ha T,García-Sastre A

doi

10.1038/embor.2013.102

subject

Has Abstract

pub_date

2013-09-01 00:00:00

pages

780-7

issue

9

eissn

1469-221X

issn

1469-3178

pii

embor2013102

journal_volume

14

pub_type

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