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 Resjournal_title
Virus researchauthors
Vaughan R,Li Y,Fan B,Ranjith-Kumar CT,Kao CCdoi
10.1016/j.virusres.2012.07.007subject
Has Abstractpub_date
2012-10-01 00:00:00pages
80-90issue
1eissn
0168-1702issn
1872-7492pii
S0168-1702(12)00256-0journal_volume
169pub_type
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