Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus

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Title
Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus
Author(s)
Jiwon AhnKyung Sook ChungDong Uk KimMi Sun Won; Lila Kim; K S Kim; Miyoung Nam; Shin Jung Choi; Hyoung-Chin Kim; M Yoon; S K Chae; Kwang Lae Hoe
Bibliographic Citation
BMB Reports, vol. 37, no. 6, pp. 741-748
Publication Year
2004
Abstract
The hepatitis C virus is associated with the development of liver cirrhosis and hepatocellular carcinomas. Among the 10 polyproteins produced by the virus, no function has been clearly assigned to the non-structural 5A (NS5A) protein. This study was designed to identify the hepatocellular proteins that interact with NS5A of the HCV. Yeast two-hybrid experiments were performed with a human liver cDNA prey-library, using five different NS5A derivatives as baits, the full-length NS5A (NS5A-F, amino acid (aa) 1-447) and its four different derivatives, denoted as NS5A-A (aa 1-150), -B (aa 1-300), -C (aa 300-447) and D (aa 150-447). NS5A-F, NS5A-B and NS5A-C gave two, two and 10 candidate clones, respectively, including an AHNAK-related protein, the secreted frizzled-related protein 4 (SFRP4), the N-myc downstream regulated gene 1 (NDRG1), the cellular retinoic acid binding protein 1 (CRABP-1), ferritin heavy chain (FTH1), translokin, tumor-associated calcium signal transducer 2 (TACSTD2), phosphatidylinositol 4-kinase (PI4K) and centaurinδ 2 (CENTδ2). However, NS5A-A produced no candidates and NS5A-D was not suitable as bait due to transcriptional activity. Based on an in vitro binding assay, CRABP-1, PI4K, CENTδ2 and two unknown fusion proteins with maltose binding protein (MBP), were confirmed to interact with the glutathione S-transferase (GST)/NS5A fusion protein. Furthermore, the interactions of CRABP-1, PI4K and CENTδ2 were not related to the PXXP motif (class II), as judged by a domain analysis. While their biological relevance is under investigation, the results contribute to a better understanding of the possible role of NS5A in hepatocellular signaling pathways.
Keyword
HCVNS5APXXP domainyeast two-hybrid
ISSN
1225-8687
Publisher
South Korea
DOI
http://dx.doi.org/10.5483/bmbrep.2004.37.6.741
Type
Article
Appears in Collections:
Division of Research on National Challenges > Stem Cell Convergenece Research Center > 1. Journal Articles
Division of Research on National Challenges > 1. Journal Articles
Division of Biomedical Research > Rare Disease Research Center > 1. Journal Articles
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
Ochang Branch Institute > Division of Bioinfrastructure > 1. Journal Articles
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