Premium
SUMO ylation of nonstructural 5A protein regulates hepatitis C virus replication
Author(s) -
Lee H. S.,
Lim Y. S.,
Park E. M.,
Baek S. H.,
Hwang S. B.
Publication year - 2014
Publication title -
journal of viral hepatitis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 100
eISSN - 1365-2893
pISSN - 1352-0504
DOI - 10.1111/jvh.12241
Subject(s) - sumo protein , ns5a , viral replication , replicon , biology , hepatitis c virus , subgenomic mrna , ubiquitin , ns5b , microbiology and biotechnology , gene silencing , virology , chemistry , virus , genetics , hepacivirus , gene , genome
Summary Viruses exploit cellular SUMO ylation machinery to favour their own propagation. We show that NS 5A is a target protein of small ubiquitin‐like modifier ( SUMO ) and is SUMO ylated at lysine residue 348. We demonstrated that SUMO ylation increased protein stability of NS 5A by inhibiting ubiquitylation, and SUMO ylation was also required for protein interaction with NS 5B. These data imply that SUMO modification may contribute to HCV replication. Indeed, silencing of UBC 9 impaired HCV replication in Jc1‐infected cells, and HCV replication level was also significantly reduced in SUMO ‐defective subgenomic replicon cells. Taken together, these data indicate that HCV replication is regulated by SUMO modification of NS 5A protein. We provide evidence for the first time that HCV exploits host cellular SUMO modification system to favour its own replication.