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Citation
Tags
HERO ID
7000816
Reference Type
Journal Article
Title
The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug, Amantadine
Author(s)
Griffin, SDC; Beales, LP; Clarke, DS; Worsfold, O; Evans, SD; Jaeger, J; Harris, MPG; Rowlands, DJ; ,
Year
2003
Is Peer Reviewed?
Yes
Journal
FEBS Letters
ISSN:
0014-5793
EISSN:
1873-3468
Publisher
ELSEVIER SCIENCE BV
Location
AMSTERDAM
Page Numbers
34-38
PMID
12560074
DOI
10.1016/S0014-5793(02)03851-6
Web of Science Id
WOS:000180734900008
Abstract
Hepatitis C virus (HCV) cannot be grown in vitro, making biochemical identification of new drug targets especially important. HCV p7 is a small hydrophobic protein of unknown function, yet necessary for particle infectivity in related viruses [Harada, T. et al., (2000) J. Virol. 74, 9498-9506]. We show that p7 can be cross-linked in vivo as hexamers. Escherichia coli expressed p7 fusion proteins also form hexamers in vitro. These and HIS-tagged p7 function as calcium ion channels in black lipid membranes. This activity is abrogated by Amantadine, a compound that inhibits ion channels of influenza [Hay, A.J. et al. (1985) EMBO J. 4, 3021-3024; Duff, K.C. and Ashley, R.H. (1992) Virology 190, 485-489] and has recently been shown to be active in combination with current HCV therapies. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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