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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/42917
Title: Inhibition of HCV replication by humanized-single domain transbodies to NS4B
Authors: Kittirat Glab-ampai
Aijaz Ahmad Malik
Monrat Chulanetra
Jeeraphong Thanongsaksrikul
Kanyarat Thueng-in
Potjanee Srimanote
Pongsri Tongtawe
Wanpen Chaicumpa
Mahidol University
Thammasat University
Suranaree University of Technology
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 5-Aug-2016
Citation: Biochemical and Biophysical Research Communications. Vol.476, No.4 (2016), 654-664
Abstract: © 2016 Elsevier Inc. NS4B of hepatitis C virus (HCV) initiates membrane web formation, binds RNA and other HCV proteins for viral replication complex (RC) formation, hydrolyses NTP, and inhibits innate anti-viral immunity. Thus, NS4B is an attractive target of a novel anti-HCV agent. In this study, humanized-nanobodies (VHs/VHHs) that bound to recombinant NS4B were produced by means of phage display technology. The nanobodies were linked molecularly to a cell penetrating peptide, penetratin (PEN), for making them cell penetrable (become transbodies). Human hepatic (Huh7) cells transfected with HCV JFH1-RNA that were treated with transbodies from four Escherichia coli clones (PEN-VHH7, PEN-VHH9, PEN-VH33, and PEN-VH43) had significant reduction of HCV RNA amounts in their culture fluids and intracellularly when compared to the transfected cells treated with control transbody and medium alone. The results were supported by the HCV foci assay. The transbody treated-transfected cells also had upregulation of the studied innate cytokine genes, IRF3, IFNβ and IL-28b. The transbodies have high potential for testing further as a novel anti-HCV agent, either alone, adjunct of existing anti-HCV agents/remedies, or in combination with their cognates specific to other HCV enzymes/proteins.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84971645642&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/42917
ISSN: 10902104
0006291X
Appears in Collections:Scopus 2016-2017

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