Unconjugated interferon-stimulated gene 15 specifically interacts with the hepatitis C virus NS5A protein via domain I

被引：10
作者：
Minami, Nanae [1 ]
Abe, Takayuki [1 ]
Deng, Lin [1 ]
Matsui, Chieko [1 ]
Fukuhara, Takasuke [2 ]
Matsuura, Yoshiharu [2 ]
Shoji, Ikuo [1 ]
机构：
[1] Kobe Univ, Grad Sch Med, Ctr Infect Dis, Div Infect Dis Control,Chuo Ku, 7-5-1 Kusunoki Cho, Kobe, Hyogo 6500017, Japan
[2] Osaka Univ, Microbial Dis Res Inst, Dept Mol Virol, 3-1 Yamada Oka, Suita, Osaka 5650871, Japan
来源：
MICROBIOLOGY AND IMMUNOLOGY | 2017年 / 61卷 / 07期
基金：
日本学术振兴会;
关键词：
Hepatitis C virus; interferon-stimulated gene 15; nonstructural protein 5A; FUNCTIONAL INTERACTION; ISG15; IFN; REPLICATION; EXPRESSION; INFECTION; IDENTIFICATION; VITRO; RNA;
D O I：
10.1111/1348-0421.12493
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
Interferon-stimulated gene 15 (ISG15), a ubiquitin-like protein, is induced by type I INF. Although several groups have reported ISGylation of the HCV NS5A protein, it is still unclear whether ISGylation of NS5A has anti- or pro-viral effects in hepatitis C virus (HCV) infection. In the present study, the role of ISGylation-independent, unconjugated ISG15 in HCV infection was examined. Immunoprecipitation analyses revealed that ISG15 interacts specifically with NS5A domain I. ISG15 mutants lacking the C-terminal glycine residue that is essential for ISGylation still interacted with NS5A protein. Taken together, these results suggest that unconjugated ISG15 affects the functions of HCV NS5A through protein-protein interaction.
引用
收藏
页码：287 / 292
页数：6
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