scholarly journals Discovery of Hepatitis C Virus NS3 Helicase Inhibitors by a Multiplexed, High-Throughput Helicase Activity Assay Based on Graphene Oxide

2013 ◽  
Vol 125 (8) ◽  
pp. 2396-2400 ◽  
Author(s):  
Hongje Jang ◽  
Soo-Ryoon Ryoo ◽  
Young-Kwan Kim ◽  
Soojin Yoon ◽  
Henna Kim ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Throughput ◽  
Helicase Activity ◽  
Activity Assay

scholarly journals Discovery of Hepatitis C Virus NS3 Helicase Inhibitors by a Multiplexed, High-Throughput Helicase Activity Assay Based on Graphene Oxide

2013 ◽  
Vol 52 (8) ◽  
pp. 2340-2344 ◽  
Author(s):  
Hongje Jang ◽  
Soo-Ryoon Ryoo ◽  
Young-Kwan Kim ◽  
Soojin Yoon ◽  
Henna Kim ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Throughput ◽  
Helicase Activity ◽  
Activity Assay

P760 HIGH-THROUGHPUT AND ULTRASENSITIVE NEXT-GENERATION PCR ASSAY FOR THE QUANTIFICATION OF THE HEPATITIS C VIRUS MUTATION AT CORE AMINO ACID 70

2014 ◽  
Vol 60 (1) ◽  
pp. S324
Author(s):  
M. Mukaide ◽  
M. Sugiyama ◽  
M. Korenaga ◽  
K. Murata ◽  
T. Kanto ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Amino Acid ◽  
High Throughput ◽  
Next Generation ◽  
Pcr Assay

scholarly journals Identification of novel anti-hepatitis C virus agents by a quantitative high throughput screen in a cell-based infection assay

2015 ◽  
Vol 124 ◽  
pp. 20-29 ◽  
Author(s):  
Zongyi Hu ◽  
Xin Hu ◽  
Shanshan He ◽  
Hyung Joon Yim ◽  
Jingbo Xiao ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Throughput ◽  
High Throughput Screen ◽  
Infection Assay ◽  
A Cell

scholarly journals Development of NS3/4A Protease-Based Reporter Assay Suitable for Efficiently Assessing Hepatitis C Virus Infection

2009 ◽  
Vol 53 (11) ◽  
pp. 4825-4834 ◽  
Author(s):  
Kao-Lu Pan ◽  
Jin-Ching Lee ◽  
Hsing-Wen Sung ◽  
Teng-Yuang Chang ◽  
John T.-A. Hsu
Keyword(s):  
Cell Culture ◽  
Life Cycle ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Virus Infection ◽  
High Throughput ◽  
High Throughput Screening ◽  
Reporter System ◽  
Viral Protease ◽  
Peptide Cleavage

ABSTRACT A cell culture system for the production of hepatitis C virus (HCV) whole virions has greatly accelerated studies of the virus life cycle and the discovery of anti-HCV agents. However, the quantification of the HCV titers in a whole-virus infection/replication system currently relies mostly on reverse transcription-PCR or immunofluorescence assay, which would be cumbersome for high-throughput drug screening. To overcome this problem, this study has generated a novel cell line, Huh7.5-EG(Δ4B5A)SEAP, that carries a dual reporter, EG(Δ4B5A)SEAP. The EG(Δ4B5A)SEAP reporter is a viral protease-cleavable fusion protein in which the enhanced green fluorescence protein is linked to secreted alkaline phosphatase (SEAP) in frame via Δ4B5A, a short peptide cleavage substrate for NS3/4A viral protease. This study demonstrates that virus replication/infection in the Huh7.5-EG(Δ4B5A)SEAP cells can be quantitatively indicated by measuring the SEAP activity in cell culture medium. The levels of SEAP released from HCV-infected Huh7.5-EG(Δ4B5A)SEAP cells correlated closely with the amounts of HCV in the inocula. The Huh7.5-EG(Δ4B5A)SEAP cells were also shown to be a suitable host for the discovery of anti-HCV inhibitors by using known compounds that target multiple stages of the HCV life cycle. The Z′-factor of this assay ranged from 0.64 to 0.74 in 96-well plates, indicating that this reporter system is suitable for high-throughput screening of prospective anti-HCV agents.

scholarly journals Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis

2017 ◽  
Vol 13 (12) ◽  
pp. e1006735 ◽  
Author(s):  
Radhika Gopal ◽  
Kelli Jackson ◽  
Netanel Tzarum ◽  
Leopold Kong ◽  
Andrew Ettenger ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Throughput ◽  
Envelope Glycoprotein ◽  
Virus Envelope ◽  
Glycoprotein Complex
Sign in / Sign up

Export Citation Format

Share Document