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      The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug, Amantadine.

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          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.

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          Author and article information

          Journal
          FEBS Lett
          FEBS letters
          Elsevier BV
          0014-5793
          0014-5793
          Jan 30 2003
          : 535
          : 1-3
          Affiliations
          [1 ] School of Biochemistry and Molecular Biology, University of Leeds, Division of Microbiology Old Medical School, Thoresby Place, Leeds LS2 9JT, UK.
          Article
          S0014579302038516
          10.1016/s0014-5793(02)03851-6
          12560074
          6232cdd0-af25-42db-8479-3fb3fdfec2f0
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