RNA binding by the NS3 protease of the hepatitis C virus.

Abstract:

:The hepatitis C virus (HCV) nonstructural protein 3 (NS3) is essential for the processing of the HCV polyprotein, the replication of HCV RNA, and to short circuit innate immunity signaling. NS3 contains an N-terminal domain with protease activity and a C-terminal domain with helicase activity. The two domains communicate with each other along with other HCV and cellular proteins. Herein we show that RNAs can bind directly to the active site cleft of the NS3 protease domain (NS3P) and inhibit proteolysis of peptide substrates. RNAs that are less apt to form intramolecular structures have a stronger inhibitory activity than RNAs with more stable base paired regions. Two mutations in the protease domain that resulted in decreased affinity to ssRNA were also defective in RNA-induced ATPase activity from the helicase domain of NS3. The coordinated effects on inhibition of protease activity and stimulation of ATPase activity raise the possibility that RNA serves as a regulatory switch for the two processes.

journal_name

Virus Res

journal_title

Virus research

authors

Vaughan R,Li Y,Fan B,Ranjith-Kumar CT,Kao CC

doi

10.1016/j.virusres.2012.07.007

subject

Has Abstract

pub_date

2012-10-01 00:00:00

pages

80-90

issue

1

eissn

0168-1702

issn

1872-7492

pii

S0168-1702(12)00256-0

journal_volume

169

pub_type

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